메뉴 건너뛰기




Volumn 3, Issue 1, 2008, Pages

Biosynthesis of membrane lipids

Author keywords

[No Author keywords available]

Indexed keywords


EID: 84959064442     PISSN: None     EISSN: 23246200     Source Type: Journal    
DOI: 10.1128/ecosalplus.3.6.4     Document Type: Article
Times cited : (41)

References (319)
  • 1
    • 0001517649 scopus 로고    scopus 로고
    • Biosynthesis of membrane lipids
    • Curtiss R III, Ingraham JL, Lin ECC, Low KB, Magasanik B, Reznikoff WS, Riley M, Schaechter M, and Umbarger HE (ed), Escherichia coli and Salmonella typhimurium:, ASM Press, Washington, DC
    • Cronan JE, Rock CO. 1996. Biosynthesis of membrane lipids, p 612-636. In Curtiss R III, Ingraham JL, Lin ECC, Low KB, Magasanik B, Reznikoff WS, Riley M, Schaechter M, and Umbarger HE (ed), Escherichia coli and Salmonella typhimurium: Cellular and Molecular Biology, vol. 1. ASM Press, Washington, DC.
    • (1996) Cellular and Molecular Biology , vol.1 , pp. 612-636
    • Cronan, J.E.1    Rock, C.O.2
  • 2
    • 22244466130 scopus 로고    scopus 로고
    • The structural biology of type II fatty acid biosynthesis
    • White SW, Zheng J, Zhang YM, Rock CO. 2005. The structural biology of type II fatty acid biosynthesis. Annu Rev Biochem 74:791-831.
    • (2005) Annu Rev Biochem , vol.74 , pp. 791-831
    • White, S.W.1    Zheng, J.2    Zhang, Y.M.3    Rock, C.O.4
  • 3
    • 33644907784 scopus 로고    scopus 로고
    • Gene-specific random mutagenesis of Escherichia coli in vivo: isolation of temperature-sensitive mutations in the acyl carrier protein of fatty acid synthesis
    • De Lay NR, Cronan JE. 2006. Gene-specific random mutagenesis of Escherichia coli in vivo: isolation of temperature-sensitive mutations in the acyl carrier protein of fatty acid synthesis. J Bacteriol 188:287-296.
    • (2006) J Bacteriol , vol.188 , pp. 287-296
    • De Lay, N.R.1    Cronan, J.E.2
  • 5
    • 31344443676 scopus 로고    scopus 로고
    • A protein network for phospholipid synthesis uncovered by a variant of the tandem affinity purification method in Escherichia coli
    • Gully D, Bouveret E. 2006. A protein network for phospholipid synthesis uncovered by a variant of the tandem affinity purification method in Escherichia coli. Proteomics 6:282-293.
    • (2006) Proteomics , vol.6 , pp. 282-293
    • Gully, D.1    Bouveret, E.2
  • 6
    • 0042737485 scopus 로고    scopus 로고
    • New partners of acyl carrier protein detected in Escherichia coli by tandem affinity purification
    • Gully D, Moinier D, Loiseau L, Bouveret E. 2003. New partners of acyl carrier protein detected in Escherichia coli by tandem affinity purification. FEBS Lett 548:90-96.
    • (2003) FEBS Lett , vol.548 , pp. 90-96
    • Gully, D.1    Moinier, D.2    Loiseau, L.3    Bouveret, E.4
  • 7
    • 33846165487 scopus 로고    scopus 로고
    • Absolute protein expression profiling estimates the relative contributions of transcriptional and translational regulation
    • Lu P, Vogel C, Wang R, Yao X, Marcotte EM. 2007. Absolute protein expression profiling estimates the relative contributions of transcriptional and translational regulation. Nat Biotechnol 25:117-124.
    • (2007) Nat Biotechnol , vol.25 , pp. 117-124
    • Lu, P.1    Vogel, C.2    Wang, R.3    Yao, X.4    Marcotte, E.M.5
  • 10
    • 33846811742 scopus 로고    scopus 로고
    • Atromentin and leucomelone, the first inhibitors specific to enoyl-ACP reductase (FabK) of Streptococcus pneumoniae
    • Zheng CJ, Sohn MJ, Kim WG. 2006. Atromentin and leucomelone, the first inhibitors specific to enoyl-ACP reductase (FabK) of Streptococcus pneumoniae. J Antibiot (Tokyo) 59:808-812.
    • (2006) J Antibiot (Tokyo) , vol.59 , pp. 808-812
    • Zheng, C.J.1    Sohn, M.J.2    Kim, W.G.3
  • 12
    • 0034780806 scopus 로고    scopus 로고
    • Bacterial fatty acid biosynthesis:targets for antibacterial drug discovery
    • Campbell JW, Cronan JE Jr. 2001. Bacterial fatty acid biosynthesis:targets for antibacterial drug discovery. Annu Rev Microbiol 55:305-332.
    • (2001) Annu Rev Microbiol , vol.55 , pp. 305-332
    • Campbell, J.W.1    Cronan, J.E.2
  • 13
    • 0036247948 scopus 로고    scopus 로고
    • Inhibitors of fatty acid synthesis as antimicrobial chemotherapeutics
    • Heath RJ, White SW, Rock CO. 2002. Inhibitors of fatty acid synthesis as antimicrobial chemotherapeutics. Appl Microbiol Biotechnol 58:695-703.
    • (2002) Appl Microbiol Biotechnol , vol.58 , pp. 695-703
    • Heath, R.J.1    White, S.W.2    Rock, C.O.3
  • 14
    • 0034804919 scopus 로고    scopus 로고
    • Lipid biosynthesis as a target for antibacterial agents
    • Heath RJ, White SW, Rock CO. 2001. Lipid biosynthesis as a target for antibacterial agents. Prog Lipid Res 40:467-497.
    • (2001) Prog Lipid Res , vol.40 , pp. 467-497
    • Heath, R.J.1    White, S.W.2    Rock, C.O.3
  • 15
    • 33745817391 scopus 로고    scopus 로고
    • Inhibiting bacterial fatty acid synthesis
    • Zhang YM, White SW, Rock CO. 2006. Inhibiting bacterial fatty acid synthesis. J Biol Chem 281:17541-17544.
    • (2006) J Biol Chem , vol.281 , pp. 17541-17544
    • Zhang, Y.M.1    White, S.W.2    Rock, C.O.3
  • 16
    • 0242693130 scopus 로고    scopus 로고
    • Bacterial membrane lipids: where do we stand?
    • Cronan JE. 2003. Bacterial membrane lipids: where do we stand? Annu Rev Microbiol 57:203-224.
    • (2003) Annu Rev Microbiol , vol.57 , pp. 203-224
    • Cronan, J.E.1
  • 17
    • 39149115737 scopus 로고    scopus 로고
    • Membrane lipid homeostasis in bacteria
    • Zhang YM, Rock CO. 2008. Membrane lipid homeostasis in bacteria. Nat Rev Microbiol 6:222-233.
    • (2008) Nat Rev Microbiol , vol.6 , pp. 222-233
    • Zhang, Y.M.1    Rock, C.O.2
  • 19
    • 0028357474 scopus 로고
    • The presence of linoleic acid in Escherichia coli cannot be confirmed
    • Cronan JE Jr, Rock CO. 1994. The presence of linoleic acid in Escherichia coli cannot be confirmed. J Bacteriol 176:3069-3071.
    • (1994) J Bacteriol , vol.176 , pp. 3069-3071
    • Cronan, J.E.1    Rock, C.O.2
  • 20
    • 0017795757 scopus 로고
    • Molecular biology of bacterial membrane lipids
    • Cronan JE Jr. 1978. Molecular biology of bacterial membrane lipids. Annu Rev Biochem 47:163-189.
    • (1978) Annu Rev Biochem , vol.47 , pp. 163-189
    • Cronan, J.E.1
  • 21
    • 0015505380 scopus 로고
    • Metabolism and function of the membrane phospholipids of Escherichia coli
    • Cronan JE, Vagelos PR. 1972. Metabolism and function of the membrane phospholipids of Escherichia coli. Biochim Biophys Acta 265:25-60.
    • (1972) Biochim Biophys Acta , vol.265 , pp. 25-60
    • Cronan, J.E.1    Vagelos, P.R.2
  • 22
    • 0024618579 scopus 로고
    • Uptake and acylation of 2- acyl-lysophospholipids by Escherichia coli
    • Hsu L, Jackowski S, Rock CO. 1989. Uptake and acylation of 2- acyl-lysophospholipids by Escherichia coli. J Bacteriol 171:1203-1205.
    • (1989) J Bacteriol , vol.171 , pp. 1203-1205
    • Hsu, L.1    Jackowski, S.2    Rock, C.O.3
  • 25
    • 7244248683 scopus 로고    scopus 로고
    • MsbA-dependent translocation of lipids across the inner membrane of Escherichia coli
    • Doerrler WT, Gibbons HS, Raetz CR. 2004. MsbA-dependent translocation of lipids across the inner membrane of Escherichia coli. J Biol Chem 279:45102-45109.
    • (2004) J Biol Chem , vol.279 , pp. 45102-45109
    • Doerrler, W.T.1    Gibbons, H.S.2    Raetz, C.R.3
  • 26
    • 0014960942 scopus 로고
    • Localization of acyl carrier protein in Escherichia coli
    • Van Den Bosch H, Williamson JR, Vagelos PR. 1970. Localization of acyl carrier protein in Escherichia coli. Nature 228:338-341.
    • (1970) Nature , vol.228 , pp. 338-341
    • Van Den Bosch, H.1    Williamson, J.R.2    Vagelos, P.R.3
  • 27
  • 28
    • 0001220339 scopus 로고
    • Biosynthesis of membrane lipids
    • Neidhardt FC, Ingraham JL, Low KB, Magasanik B, Schaechter M, and Umbarger HE (ed), Escherichia coli and Salmonella typhimurium:, American Society for Microbiology, Washington, DC
    • Cronan JE, Rock CO. 1987. Biosynthesis of membrane lipids, p 3474-3497. In Neidhardt FC, Ingraham JL, Low KB, Magasanik B, Schaechter M, and Umbarger HE (ed), Escherichia coli and Salmonella typhimurium: Cellular and Molecular Biology, vol. 1. American Society for Microbiology, Washington, DC.
    • (1987) Cellular and Molecular Biology , vol.1 , pp. 3474-3497
    • Cronan, J.E.1    Rock, C.O.2
  • 29
    • 34547791319 scopus 로고    scopus 로고
    • Coupling of fatty acid and phospholipid synthesis in Bacillus subtilis
    • Paoletti L, Lu YJ, Schujman GE, de Mendoza D, Rock CO. 2007. Coupling of fatty acid and phospholipid synthesis in Bacillus subtilis. J Bacteriol 189:5816-5824.
    • (2007) J Bacteriol , vol.189 , pp. 5816-5824
    • Paoletti, L.1    Lu, Y.J.2    Schujman, G.E.3    de Mendoza, D.4    Rock, C.O.5
  • 30
    • 0036731699 scopus 로고    scopus 로고
    • Listening in on bacteria: acylhomoserine lactone signalling
    • Fuqua C, Greenberg EP. 2002. Listening in on bacteria: acylhomoserine lactone signalling. Nat Rev Mol Cell Biol 3:685-695.
    • (2002) Nat Rev Mol Cell Biol , vol.3 , pp. 685-695
    • Fuqua, C.1    Greenberg, E.P.2
  • 33
    • 0019345428 scopus 로고
    • Acyl carrier protein from Escherichia coli
    • Rock CO, Cronan JE Jr. 1981. Acyl carrier protein from Escherichia coli. Methods Enzymol 71(Pt C):341-351.
    • (1981) Methods Enzymol , vol.71 , pp. 341-351
    • Rock, C.O.1    Cronan, J.E.2
  • 34
    • 0018787395 scopus 로고
    • Re-evaluation of the solution structure of acyl carrier protein
    • Rock CO, Cronan JE Jr. 1979. Re-evaluation of the solution structure of acyl carrier protein. J Biol Chem 254:9778-9785.
    • (1979) J Biol Chem , vol.254 , pp. 9778-9785
    • Rock, C.O.1    Cronan, J.E.2
  • 35
    • 16644400323 scopus 로고    scopus 로고
    • Structure of apo acyl carrier protein and a proposal to engineer protein crystallization through metal ions
    • Qiu X, Janson CA. 2004. Structure of apo acyl carrier protein and a proposal to engineer protein crystallization through metal ions. Acta Crystallogr D Biol Crystallogr 60:1545-1554.
    • (2004) Acta Crystallogr D Biol Crystallogr , vol.60 , pp. 1545-1554
    • Qiu, X.1    Janson, C.A.2
  • 36
    • 34547131328 scopus 로고    scopus 로고
    • In vivo functional analyses of the type II acyl carrier proteins of fatty acid biosynthesis
    • De Lay NR, Cronan JE. 2007. In vivo functional analyses of the type II acyl carrier proteins of fatty acid biosynthesis. J Biol Chem 282:20319-20328.
    • (2007) J Biol Chem , vol.282 , pp. 20319-20328
    • De Lay, N.R.1    Cronan, J.E.2
  • 37
    • 0034662753 scopus 로고    scopus 로고
    • Crystal structures of substrate binding to Bacillus subtilis holo-(acyl carrier protein) synthase reveal a novel trimeric arrangement of molecules resulting in three active sites
    • Parris KD, Lin L, Tam A, Mathew R, Hixon J, Stahl M, Fritz CC, Seehra J, Somers WS. 2000. Crystal structures of substrate binding to Bacillus subtilis holo-(acyl carrier protein) synthase reveal a novel trimeric arrangement of molecules resulting in three active sites. Structure 8:883-895.
    • (2000) Structure , vol.8 , pp. 883-895
    • Parris, K.D.1    Lin, L.2    Tam, A.3    Mathew, R.4    Hixon, J.5    Stahl, M.6    Fritz, C.C.7    Seehra, J.8    Somers, W.S.9
  • 38
    • 0024435205 scopus 로고
    • A dynamic model for the structure of acyl carrier protein in solution
    • Kim Y, Prestegard JH. 1989. A dynamic model for the structure of acyl carrier protein in solution. Biochemistry 28:8792-8797.
    • (1989) Biochemistry , vol.28 , pp. 8792-8797
    • Kim, Y.1    Prestegard, J.H.2
  • 39
    • 0025613125 scopus 로고
    • Refinement of the NMR structures for acyl carrier protein with scalar coupling data
    • Kim Y, Prestegard JH. 1990. Refinement of the NMR structures for acyl carrier protein with scalar coupling data. Proteins 8:377-385.
    • (1990) Proteins , vol.8 , pp. 377-385
    • Kim, Y.1    Prestegard, J.H.2
  • 40
    • 33744954170 scopus 로고    scopus 로고
    • Solution structures of conformationally equilibrium forms of holoacyl carrier protein (PfACP) from Plasmodium falciparum provides insight into the mechanism of activation of ACPs
    • Sharma AK, Sharma SK, Surolia A, Surolia N, Sarma SP. 2006. Solution structures of conformationally equilibrium forms of holoacyl carrier protein (PfACP) from Plasmodium falciparum provides insight into the mechanism of activation of ACPs. Biochemistry 45:6904-6916.
    • (2006) Biochemistry , vol.45 , pp. 6904-6916
    • Sharma, A.K.1    Sharma, S.K.2    Surolia, A.3    Surolia, N.4    Sarma, S.P.5
  • 42
    • 33751512907 scopus 로고    scopus 로고
    • Structural studies of fatty acyl-(acyl carrier protein) thioesters reveal a hydrophobic binding cavity that can expand to fit longer substrates
    • Roujeinikova A, Simon WJ, Gilroy J, Rice DW, Rafferty JB, Slabas AR. 2007. Structural studies of fatty acyl-(acyl carrier protein) thioesters reveal a hydrophobic binding cavity that can expand to fit longer substrates. J Mol Biol 365:135-145.
    • (2007) J Mol Biol , vol.365 , pp. 135-145
    • Roujeinikova, A.1    Simon, W.J.2    Gilroy, J.3    Rice, D.W.4    Rafferty, J.B.5    Slabas, A.R.6
  • 43
    • 0020478991 scopus 로고
    • Molecular properties of short chain acyl thioesters of acyl carrier protein
    • Cronan JE Jr. 1982. Molecular properties of short chain acyl thioesters of acyl carrier protein. J Biol Chem 257:5013-5017.
    • (1982) J Biol Chem , vol.257 , pp. 5013-5017
    • Cronan, J.E.1
  • 44
    • 0021112871 scopus 로고
    • Ratio of active to inactive forms of acyl carrier protein in Escherichia coli
    • Jackowski S, Rock CO. 1983. Ratio of active to inactive forms of acyl carrier protein in Escherichia coli. J Biol Chem 258:15186-15191.
    • (1983) J Biol Chem , vol.258 , pp. 15186-15191
    • Jackowski, S.1    Rock, C.O.2
  • 45
    • 0015884219 scopus 로고
    • The stability of acyl carrier protein in Escherichia coli
    • Powell GL, Bauza M, Larrabee AR. 1973. The stability of acyl carrier protein in Escherichia coli. J Biol Chem 248:4461-4466.
    • (1973) J Biol Chem , vol.248 , pp. 4461-4466
    • Powell, G.L.1    Bauza, M.2    Larrabee, A.R.3
  • 46
    • 0014691159 scopus 로고
    • Acyl carrier protein. XII Synthesis and turnover of the prosthetic group of acyl carrier protein in vivo
    • Powell GL, Elovson J, Vagelos PR. 1969. Acyl carrier protein. XII Synthesis and turnover of the prosthetic group of acyl carrier protein in vivo. J Biol Chem 244:5616-5624.
    • (1969) J Biol Chem , vol.244 , pp. 5616-5624
    • Powell, G.L.1    Elovson, J.2    Vagelos, P.R.3
  • 47
    • 27144441544 scopus 로고    scopus 로고
    • The enigmatic acyl carrier protein phosphodiesterase of Escherichia coli: genetic and enzymological characterization
    • Thomas J, Cronan JE. 2005. The enigmatic acyl carrier protein phosphodiesterase of Escherichia coli: genetic and enzymological characterization. J Biol Chem 280:34675-34683.
    • (2005) J Biol Chem , vol.280 , pp. 34675-34683
    • Thomas, J.1    Cronan, J.E.2
  • 48
    • 0028835496 scopus 로고
    • The unmodified (apo) form of Escherichia coli acyl carrier protein is a potent inhibitor of cell growth
    • Keating DH, Carey MR, Cronan JE Jr. 1995. The unmodified (apo) form of Escherichia coli acyl carrier protein is a potent inhibitor of cell growth. J Biol Chem 270:22229-22235.
    • (1995) J Biol Chem , vol.270 , pp. 22229-22235
    • Keating, D.H.1    Carey, M.R.2    Cronan, J.E.3
  • 49
    • 33745208688 scopus 로고    scopus 로고
    • A genome rearrangement has orphaned the Escherichia coli K-12 AcpT phosphopantetheinyl transferase from its cognate Escherichia coli O157:H7 substrates
    • De Lay NR, Cronan JE. 2006. A genome rearrangement has orphaned the Escherichia coli K-12 AcpT phosphopantetheinyl transferase from its cognate Escherichia coli O157:H7 substrates. Mol Microbiol 61:232-242.
    • (2006) Mol Microbiol , vol.61 , pp. 232-242
    • De Lay, N.R.1    Cronan, J.E.2
  • 50
    • 0033955033 scopus 로고    scopus 로고
    • Holo-(acyl carrier protein) synthase and phosphopantetheinyl transfer in Escherichia coli
    • Flugel RS, Hwangbo Y, Lambalot RH, Cronan JE Jr, Walsh CT. 2000. Holo-(acyl carrier protein) synthase and phosphopantetheinyl transfer in Escherichia coli. J Biol Chem 275:959-968.
    • (2000) J Biol Chem , vol.275 , pp. 959-968
    • Flugel, R.S.1    Hwangbo, Y.2    Lambalot, R.H.3    Cronan, J.E.4    Walsh, C.T.5
  • 51
    • 0019416792 scopus 로고
    • A mutant of Escherichia coli conditionally defective in the synthesis of holo-[acyl carrier protein]
    • Polacco ML, Cronan JE Jr. 1981. A mutant of Escherichia coli conditionally defective in the synthesis of holo-[acyl carrier protein]. J Biol Chem 256:5750-5754.
    • (1981) J Biol Chem , vol.256 , pp. 5750-5754
    • Polacco, M.L.1    Cronan, J.E.2
  • 52
    • 0031419005 scopus 로고    scopus 로고
    • Holo-[acyl-carrier-protein] synthase of Escherichia coli
    • Lambalot RH, Walsh CT. 1997. Holo-[acyl-carrier-protein] synthase of Escherichia coli. Methods Enzymol 279:254-262.
    • (1997) Methods Enzymol , vol.279 , pp. 254-262
    • Lambalot, R.H.1    Walsh, C.T.2
  • 53
    • 33745439554 scopus 로고    scopus 로고
    • Acyl carrier protein synthases from gram-negative, gram-positive, and atypical bacterial species: biochemical and structural properties and physiological implications
    • McAllister KA, Peery RB, Zhao G. 2006. Acyl carrier protein synthases from gram-negative, gram-positive, and atypical bacterial species: biochemical and structural properties and physiological implications. J Bacteriol 188:4737-4748.
    • (2006) J Bacteriol , vol.188 , pp. 4737-4748
    • McAllister, K.A.1    Peery, R.B.2    Zhao, G.3
  • 55
    • 34547102510 scopus 로고    scopus 로고
    • The ubiquitous carrier protein-a window to metabolite biosynthesis
    • Mercer AC, Burkart MD. 2007. The ubiquitous carrier protein-a window to metabolite biosynthesis. Nat Prod Rep 24:750-773.
    • (2007) Nat Prod Rep , vol.24 , pp. 750-773
    • Mercer, A.C.1    Burkart, M.D.2
  • 56
    • 0033485259 scopus 로고    scopus 로고
    • Crystal structure of the surfactin synthetase-activating enzyme Sfp: a prototype of the 4′-phosphopantetheinyl transferase superfamily
    • Reuter K, Mofid MR, Marahiel MA, Ficner R. 1999. Crystal structure of the surfactin synthetase-activating enzyme Sfp: a prototype of the 4′-phosphopantetheinyl transferase superfamily. EMBO J 18:6823-6831.
    • (1999) EMBO J , vol.18 , pp. 6823-6831
    • Reuter, K.1    Mofid, M.R.2    Marahiel, M.A.3    Ficner, R.4
  • 57
    • 0014216564 scopus 로고
    • Acyl carrier protein. IX Acyl carrier protein hydrolase
    • Vagelos PR, Larrabes AR. 1967. Acyl carrier protein. IX Acyl carrier protein hydrolase. J Biol Chem 242:1776-1781.
    • (1967) J Biol Chem , vol.242 , pp. 1776-1781
    • Vagelos, P.R.1    Larrabes, A.R.2
  • 58
    • 0025143156 scopus 로고
    • Isolation and properties of acyl carrier protein phosphodiesterase of Escherichia coli
    • Fischl AS, Kennedy EP. 1990. Isolation and properties of acyl carrier protein phosphodiesterase of Escherichia coli. J Bacteriol 172:5445-5449.
    • (1990) J Bacteriol , vol.172 , pp. 5445-5449
    • Fischl, A.S.1    Kennedy, E.P.2
  • 59
    • 46649109607 scopus 로고    scopus 로고
    • Expansion of substrate specificity and catalytic mechanism of azoreductase by X-ray crystallography and site-directed mutagenesis
    • Ito K, Nakanishi M, Lee WC, Zhi Y, Sasaki H, Zenno S, Saigo K, Kitade Y, Tanokura M. 2008. Expansion of substrate specificity and catalytic mechanism of azoreductase by X-ray crystallography and site-directed mutagenesis. J Biol Chem 283:13889-13896.
    • (2008) J Biol Chem , vol.283 , pp. 13889-13896
    • Ito, K.1    Nakanishi, M.2    Lee, W.C.3    Zhi, Y.4    Sasaki, H.5    Zenno, S.6    Saigo, K.7    Kitade, Y.8    Tanokura, M.9
  • 60
    • 0035824553 scopus 로고    scopus 로고
    • Putative ACP phosphodiesterase gene (acpD) encodes an azoreductase
    • Nakanishi M, Yatome C, Ishida N, Kitade Y. 2001. Putative ACP phosphodiesterase gene (acpD) encodes an azoreductase. J Biol Chem 276:46394-46399.
    • (2001) J Biol Chem , vol.276 , pp. 46394-46399
    • Nakanishi, M.1    Yatome, C.2    Ishida, N.3    Kitade, Y.4
  • 61
    • 33846065944 scopus 로고    scopus 로고
    • Acyl carrier protein phosphodiesterase (AcpH) of Escherichia coli is a non-canonical member of the HD phosphatase/phosphodiesterase family
    • Thomas J, Rigden DJ, Cronan JE. 2007. Acyl carrier protein phosphodiesterase (AcpH) of Escherichia coli is a non-canonical member of the HD phosphatase/phosphodiesterase family. Biochemistry 46:129-136.
    • (2007) Biochemistry , vol.46 , pp. 129-136
    • Thomas, J.1    Rigden, D.J.2    Cronan, J.E.3
  • 62
    • 0028335691 scopus 로고
    • Inhibition of fatty acid synthesis in Escherichia coli in the absence of phospholipid synthesis and release of inhibition by thioesterase action
    • Jiang P, Cronan JE Jr. 1994. Inhibition of fatty acid synthesis in Escherichia coli in the absence of phospholipid synthesis and release of inhibition by thioesterase action. J Bacteriol 176:2814-2821.
    • (1994) J Bacteriol , vol.176 , pp. 2814-2821
    • Jiang, P.1    Cronan, J.E.2
  • 63
    • 0020351537 scopus 로고
    • Regulation of phospholipid synthesis in Escherichia coli. Composition of the acyl-acyl carrier protein pool in vivo
    • Rock CO, Jackowski S. 1982. Regulation of phospholipid synthesis in Escherichia coli. Composition of the acyl-acyl carrier protein pool in vivo. J Biol Chem 257:10759-10765.
    • (1982) J Biol Chem , vol.257 , pp. 10759-10765
    • Rock, C.O.1    Jackowski, S.2
  • 64
    • 0026703235 scopus 로고
    • The gene encoding Escherichia coli acyl carrier protein lies within a cluster of fatty acid biosynthetic genes
    • Rawlings M, Cronan JE Jr. 1992. The gene encoding Escherichia coli acyl carrier protein lies within a cluster of fatty acid biosynthetic genes. J Biol Chem 267:5751-5754.
    • (1992) J Biol Chem , vol.267 , pp. 5751-5754
    • Rawlings, M.1    Cronan, J.E.2
  • 65
    • 0023518276 scopus 로고
    • The function of acyl carrier protein in the synthesis of membrane-derived oligosaccharides does not require its phosphopantetheine prosthetic group
    • Therisod H, Kennedy EP. 1987. The function of acyl carrier protein in the synthesis of membrane-derived oligosaccharides does not require its phosphopantetheine prosthetic group. Proc Natl Acad Sci USA 84:8235-8238.
    • (1987) Proc Natl Acad Sci USA , vol.84 , pp. 8235-8238
    • Therisod, H.1    Kennedy, E.P.2
  • 66
    • 0022524388 scopus 로고
    • An essential function for acyl carrier protein in the biosynthesis of membranederived oligosaccharides of Escherichia coli
    • Therisod H, Weissborn AC, Kennedy EP. 1986. An essential function for acyl carrier protein in the biosynthesis of membranederived oligosaccharides of Escherichia coli. Proc Natl Acad Sci USA 83:7236-7240.
    • (1986) Proc Natl Acad Sci USA , vol.83 , pp. 7236-7240
    • Therisod, H.1    Weissborn, A.C.2    Kennedy, E.P.3
  • 67
    • 0030280423 scopus 로고    scopus 로고
    • Specific nicking at the 3′ ends of the terminal inverted repeat sequences in transposon Tn3 by transposase and an E. coli protein ACP
    • Maekawa T, Yanagihara K, Ohtsubo E. 1996. Specific nicking at the 3′ ends of the terminal inverted repeat sequences in transposon Tn3 by transposase and an E. coli protein ACP Genes Cells 1:1017-1030.
    • (1996) Genes Cells , vol.1 , pp. 1017-1030
    • Maekawa, T.1    Yanagihara, K.2    Ohtsubo, E.3
  • 68
    • 0032189817 scopus 로고    scopus 로고
    • Host proteins can stimulate Tn7 transposition: a novel role for the ribosomal protein L29 and the acyl carrier protein
    • Sharpe PL, Craig NL. 1998. Host proteins can stimulate Tn7 transposition: a novel role for the ribosomal protein L29 and the acyl carrier protein. EMBO J 17:5822-5831.
    • (1998) EMBO J , vol.17 , pp. 5822-5831
    • Sharpe, P.L.1    Craig, N.L.2
  • 69
    • 0026432638 scopus 로고
    • Activation of Escherichia coli prohaemolysin to the mature toxin by acyl carrier protein-dependent fatty acylation
    • Issartel JP, Koronakis V, Hughes C. 1991. Activation of Escherichia coli prohaemolysin to the mature toxin by acyl carrier protein-dependent fatty acylation. Nature 351:759-761.
    • (1991) Nature , vol.351 , pp. 759-761
    • Issartel, J.P.1    Koronakis, V.2    Hughes, C.3
  • 70
    • 0037435617 scopus 로고    scopus 로고
    • Amino acid residues of Escherichia coli acyl carrier protein involved in heterologous protein interactions
    • Worsham LM, Earls L, Jolly C, Langston KG, Trent MS, Ernst-Fonberg ML. 2003. Amino acid residues of Escherichia coli acyl carrier protein involved in heterologous protein interactions. Biochemistry 42:167-176.
    • (2003) Biochemistry , vol.42 , pp. 167-176
    • Worsham, L.M.1    Earls, L.2    Jolly, C.3    Langston, K.G.4    Trent, M.S.5    Ernst-Fonberg, M.L.6
  • 71
    • 13444278560 scopus 로고    scopus 로고
    • Thermodynamics of a protein acylation: activation of Escherichia coli hemolysin toxin
    • Worsham LM, Langston KG, Ernst-Fonberg ML. 2005. Thermodynamics of a protein acylation: activation of Escherichia coli hemolysin toxin. Biochemistry 44:1329-1337.
    • (2005) Biochemistry , vol.44 , pp. 1329-1337
    • Worsham, L.M.1    Langston, K.G.2    Ernst-Fonberg, M.L.3
  • 72
    • 0035856528 scopus 로고    scopus 로고
    • Insights into the catalytic mechanism of HlyC, the internal protein acyltransferase that activates Escherichia coli hemolysin toxin
    • Worsham LM, Trent MS, Earls L, Jolly C, Ernst-Fonberg ML. 2001. Insights into the catalytic mechanism of HlyC, the internal protein acyltransferase that activates Escherichia coli hemolysin toxin. Biochemistry 40:13607-13616.
    • (2001) Biochemistry , vol.40 , pp. 13607-13616
    • Worsham, L.M.1    Trent, M.S.2    Earls, L.3    Jolly, C.4    Ernst-Fonberg, M.L.5
  • 74
    • 0028855972 scopus 로고
    • Enoyl-acyl carrier protein reductase (fabI) plays a determinant role in completing cycles of fatty acid elongation in Escherichia coli
    • Heath RJ, Rock CO. 1995. Enoyl-acyl carrier protein reductase (fabI) plays a determinant role in completing cycles of fatty acid elongation in Escherichia coli. J Biol Chem 270:26538-26542.
    • (1995) J Biol Chem , vol.270 , pp. 26538-26542
    • Heath, R.J.1    Rock, C.O.2
  • 75
    • 77956919832 scopus 로고
    • β-Hydroxydecanoyl thioester dehydrase
    • Boyer PD (ed), 3rd ed. Academic Press, New York, NY
    • Bloch K. 1971. β-Hydroxydecanoyl thioester dehydrase, p 441-464. In Boyer PD (ed), The Enzymes, 3rd ed. Academic Press, New York, NY.
    • (1971) The Enzymes , pp. 441-464
    • Bloch, K.1
  • 76
    • 0034666431 scopus 로고    scopus 로고
    • Overproduction of acetyl-CoA carboxylase activity increases the rate of fatty acid biosynthesis in Escherichia coli
    • Davis MS, Solbiati J, Cronan JE Jr. 2000. Overproduction of acetyl-CoA carboxylase activity increases the rate of fatty acid biosynthesis in Escherichia coli. J Biol Chem 275:28593-28598.
    • (2000) J Biol Chem , vol.275 , pp. 28593-28598
    • Davis, M.S.1    Solbiati, J.2    Cronan, J.E.3
  • 77
    • 0036018143 scopus 로고    scopus 로고
    • Multi-subunit acetyl-CoA carboxylases
    • Cronan JE Jr, Waldrop GL. 2002. Multi-subunit acetyl-CoA carboxylases. Prog Lipid Res 41:407-435.
    • (2002) Prog Lipid Res , vol.41 , pp. 407-435
    • Cronan, J.E.1    Waldrop, G.L.2
  • 78
    • 84959058068 scopus 로고
    • Acyl-CoA carboxylases
    • Boyer PD (ed), Academic Press, New York, NY
    • Alberts AW, Vagelos PR. 1972. Acyl-CoA carboxylases. In Boyer PD (ed), The Enzymes. Academic Press, New York, NY.
    • (1972) The Enzymes
    • Alberts, A.W.1    Vagelos, P.R.2
  • 80
    • 0026495408 scopus 로고
    • Sequence of the sodium ion pump oxaloacetate decarboxylase from Salmonella typhimurium
    • Woehlke G, Wifling K, Dimroth P. 1992. Sequence of the sodium ion pump oxaloacetate decarboxylase from Salmonella typhimurium. J Biol Chem 267:22798-22803.
    • (1992) J Biol Chem , vol.267 , pp. 22798-22803
    • Woehlke, G.1    Wifling, K.2    Dimroth, P.3
  • 81
    • 0042232285 scopus 로고    scopus 로고
    • The biotin carboxylase-biotin carboxyl carrier protein complex of Escherichia coli acetyl-CoA carboxylase
    • Choi-Rhee E, Cronan JE. 2003. The biotin carboxylase-biotin carboxyl carrier protein complex of Escherichia coli acetyl-CoA carboxylase. J Biol Chem 278:30806-30812.
    • (2003) J Biol Chem , vol.278 , pp. 30806-30812
    • Choi-Rhee, E.1    Cronan, J.E.2
  • 82
    • 0029986466 scopus 로고    scopus 로고
    • Purification and characterization of intact and truncated forms of the Escherichia coli biotin carboxyl carrier subunit of acetyl-CoA carboxylase
    • Nenortas E, Beckett D. 1996. Purification and characterization of intact and truncated forms of the Escherichia coli biotin carboxyl carrier subunit of acetyl-CoA carboxylase. J Biol Chem 271:7559-7567.
    • (1996) J Biol Chem , vol.271 , pp. 7559-7567
    • Nenortas, E.1    Beckett, D.2
  • 83
    • 0016285541 scopus 로고
    • Acetyl coenzyme A carboxylase system of Escherichia coli. Purification and properties of the biotin carboxylase, carboxyltransferase, and carboxyl carrier protein components
    • Guchhait RB, Polakis SE, Dimroth P, Stoll E, Moss J, Lane MD. 1974. Acetyl coenzyme A carboxylase system of Escherichia coli. Purification and properties of the biotin carboxylase, carboxyltransferase, and carboxyl carrier protein components. J Biol Chem 249:6633-6645.
    • (1974) J Biol Chem , vol.249 , pp. 6633-6645
    • Guchhait, R.B.1    Polakis, S.E.2    Dimroth, P.3    Stoll, E.4    Moss, J.5    Lane, M.D.6
  • 84
    • 0017180688 scopus 로고
    • Stabilization of an acetyl-coenzyme A carboxylase complex from Pseudomonas citronellolis
    • Fall RR. 1976. Stabilization of an acetyl-coenzyme A carboxylase complex from Pseudomonas citronellolis. Biochim Biophys Acta 450:475-480.
    • (1976) Biochim Biophys Acta , vol.450 , pp. 475-480
    • Fall, R.R.1
  • 85
    • 0027428006 scopus 로고
    • Organization and nucleotide sequences of the genes encoding the biotin carboxyl carrier protein and biotin carboxylase protein of Pseudomonas aeruginosa acetyl coenzyme A carboxylase
    • Best EA, Knauf VC. 1993. Organization and nucleotide sequences of the genes encoding the biotin carboxyl carrier protein and biotin carboxylase protein of Pseudomonas aeruginosa acetyl coenzyme A carboxylase. J Bacteriol 175:6881-6889.
    • (1993) J Bacteriol , vol.175 , pp. 6881-6889
    • Best, E.A.1    Knauf, V.C.2
  • 88
    • 0026502763 scopus 로고
    • The gene encoding the biotin carboxylase subunit of Escherichia coli acetyl-CoA carboxylase
    • Li SJ, Cronan JE Jr. 1992. The gene encoding the biotin carboxylase subunit of Escherichia coli acetyl-CoA carboxylase. J Biol Chem 267:855-863.
    • (1992) J Biol Chem , vol.267 , pp. 855-863
    • Li, S.J.1    Cronan, J.E.2
  • 89
    • 0026800929 scopus 로고
    • The dedB (usg) open reading frame of Escherichia coli encodes a subunit of acetyl-coenzyme A carboxylase
    • Li SJ, Rock CO, Cronan JE Jr. 1992. The dedB (usg) open reading frame of Escherichia coli encodes a subunit of acetyl-coenzyme A carboxylase. J Bacteriol 174:5755-5757.
    • (1992) J Bacteriol , vol.174 , pp. 5755-5757
    • Li, S.J.1    Rock, C.O.2    Cronan, J.E.3
  • 90
    • 0027389215 scopus 로고
    • Growth rate regulation of Escherichia coli acetyl coenzyme A carboxylase, which catalyzes the first committed step of lipid biosynthesis
    • Li SJ, Cronan JE Jr. 1993. Growth rate regulation of Escherichia coli acetyl coenzyme A carboxylase, which catalyzes the first committed step of lipid biosynthesis. J Bacteriol 175:332-340.
    • (1993) J Bacteriol , vol.175 , pp. 332-340
    • Li, S.J.1    Cronan, J.E.2
  • 91
    • 41449084503 scopus 로고    scopus 로고
    • Biotin sensing: universal influence of biotin status on transcription
    • Beckett D. 2007. Biotin sensing: universal influence of biotin status on transcription. Annu Rev Genet 41:443-464.
    • (2007) Annu Rev Genet , vol.41 , pp. 443-464
    • Beckett, D.1
  • 92
    • 0015935333 scopus 로고
    • Acetyl coenzyme A carboxylase. Proteolytic modification of biotin carboxyl carrier protein
    • Fall RR, Vagelos PR. 1973. Acetyl coenzyme A carboxylase. Proteolytic modification of biotin carboxyl carrier protein. J Biol Chem 248:2078-2088.
    • (1973) J Biol Chem , vol.248 , pp. 2078-2088
    • Fall, R.R.1    Vagelos, P.R.2
  • 93
    • 0035813096 scopus 로고    scopus 로고
    • The biotinyl domain of Escherichia coli acetyl-CoA carboxylase. Evidence that the "thumb" structure is essential and that the domain functions as a dimer
    • Cronan JE Jr. 2001. The biotinyl domain of Escherichia coli acetyl-CoA carboxylase. Evidence that the "thumb" structure is essential and that the domain functions as a dimer. J Biol Chem 276:37355-37364.
    • (2001) J Biol Chem , vol.276 , pp. 37355-37364
    • Cronan, J.E.1
  • 94
    • 0037077261 scopus 로고    scopus 로고
    • Stabilization of the biotinoyl domain of Escherichia coli acetyl-CoA carboxylase by interactions between the attached biotin and the protruding "thumb" structure
    • Solbiati J, Chapman-Smith A, Cronan JE Jr. 2002. Stabilization of the biotinoyl domain of Escherichia coli acetyl-CoA carboxylase by interactions between the attached biotin and the protruding "thumb" structure. J Biol Chem 277:21604-21609.
    • (2002) J Biol Chem , vol.277 , pp. 21604-21609
    • Solbiati, J.1    Chapman-Smith, A.2    Cronan, J.E.3
  • 95
    • 0033790516 scopus 로고    scopus 로고
    • Swinging arms and swinging domains in multifunctional enzymes: catalytic machines for multistep reactions
    • Perham RN. 2000. Swinging arms and swinging domains in multifunctional enzymes: catalytic machines for multistep reactions. Annu Rev Biochem 69:961-1004.
    • (2000) Annu Rev Biochem , vol.69 , pp. 961-1004
    • Perham, R.N.1
  • 96
    • 0036183336 scopus 로고    scopus 로고
    • Chemical and catalytic mechanisms of carboxyl transfer reactions in biotin-dependent enzymes
    • Attwood PV, Wallace JC. 2002. Chemical and catalytic mechanisms of carboxyl transfer reactions in biotin-dependent enzymes. Acc Chem Res 35:113-120.
    • (2002) Acc Chem Res , vol.35 , pp. 113-120
    • Attwood, P.V.1    Wallace, J.C.2
  • 97
    • 0038811689 scopus 로고    scopus 로고
    • The biotin enzyme family:conserved structural motifs and domain rearrangements
    • Jitrapakdee S, Wallace JC. 2003. The biotin enzyme family:conserved structural motifs and domain rearrangements. Curr Protein Pept Sci 4:217-229.
    • (2003) Curr Protein Pept Sci , vol.4 , pp. 217-229
    • Jitrapakdee, S.1    Wallace, J.C.2
  • 98
    • 33745200041 scopus 로고    scopus 로고
    • Is dimerization required for the catalytic activity of bacterial biotin carboxylase?
    • Shen Y, Chou CY, Chang GG, Tong L. 2006. Is dimerization required for the catalytic activity of bacterial biotin carboxylase? Mol. Cell 22:807-818.
    • (2006) Mol. Cell , vol.22 , pp. 807-818
    • Shen, Y.1    Chou, C.Y.2    Chang, G.G.3    Tong, L.4
  • 100
    • 0026589541 scopus 로고
    • Cloning and nucleotide sequence of the fabD gene encoding malonyl coenzyme A-acyl carrier protein transacylase of Escherichia coli
    • Magnuson K, Oh W, Larson TJ, Cronan JE Jr. 1992. Cloning and nucleotide sequence of the fabD gene encoding malonyl coenzyme A-acyl carrier protein transacylase of Escherichia coli. FEBS Lett 299:262-266.
    • (1992) FEBS Lett , vol.299 , pp. 262-266
    • Magnuson, K.1    Oh, W.2    Larson, T.J.3    Cronan, J.E.4
  • 101
    • 0026680582 scopus 로고
    • Cloning, nucleotide sequence, and expression of the Escherichia coli fabD gene, encoding malonyl coenzyme A-acyl carrier protein transacylase
    • Verwoert II, Verbree EC, van der Linden KH, Nijkamp HJ, Stuitje AR. 1992. Cloning, nucleotide sequence, and expression of the Escherichia coli fabD gene, encoding malonyl coenzyme A-acyl carrier protein transacylase. J Bacteriol 174:2851-2857.
    • (1992) J Bacteriol , vol.174 , pp. 2851-2857
    • Verwoert, I.I.1    Verbree, E.C.2    van der Linden, K.H.3    Nijkamp, H.J.4    Stuitje, A.R.5
  • 102
    • 33744460734 scopus 로고    scopus 로고
    • Mapping the active site of Escherichia coli malonyl-CoA-acyl carrier protein transacylase (FabD) by protein crystallography
    • Oefner C, Schulz H, D'Arcy A, Dale GE. 2006. Mapping the active site of Escherichia coli malonyl-CoA-acyl carrier protein transacylase (FabD) by protein crystallography. Acta Crystallogr D Biol Crystallogr 62:613-618.
    • (2006) Acta Crystallogr D Biol Crystallogr , vol.62 , pp. 613-618
    • Oefner, C.1    Schulz, H.2    D'Arcy, A.3    Dale, G.E.4
  • 103
    • 0029061966 scopus 로고
    • The Escherichia coli malonyl-CoA:acyl carrier protein transacylase at 1.5-Å resolution. Crystal structure of a fatty acid synthase component
    • Serre L, Verbree EC, Dauter Z, Stuitje AR, Derewenda ZS. 1995. The Escherichia coli malonyl-CoA:acyl carrier protein transacylase at 1.5-Å resolution. Crystal structure of a fatty acid synthase component. J Biol Chem 270:12961-12964.
    • (1995) J Biol Chem , vol.270 , pp. 12961-12964
    • Serre, L.1    Verbree, E.C.2    Dauter, Z.3    Stuitje, A.R.4    Derewenda, Z.S.5
  • 104
    • 0028271142 scopus 로고
    • Molecular characterization of an Escherichia coli mutant with a temperature-sensitive malonyl coenzyme A-acyl carrier protein transacylase
    • Verwoert II, Verhagen EF, van der Linden KH, Verbree EC, Nijkamp HJ, Stuitje AR. 1994. Molecular characterization of an Escherichia coli mutant with a temperature-sensitive malonyl coenzyme A-acyl carrier protein transacylase. FEBS Lett 348:311-316.
    • (1994) FEBS Lett , vol.348 , pp. 311-316
    • Verwoert, I.I.1    Verhagen, E.F.2    van der Linden, K.H.3    Verbree, E.C.4    Nijkamp, H.J.5    Stuitje, A.R.6
  • 107
    • 0031931702 scopus 로고    scopus 로고
    • Catalytic self-acylation of type II polyketide synthase acyl carrier proteins
    • Hitchman TS, Crosby J, Byrom KJ, Cox RJ, Simpson TJ. 1998. Catalytic self-acylation of type II polyketide synthase acyl carrier proteins. Chem Biol 5:35-47.
    • (1998) Chem Biol , vol.5 , pp. 35-47
    • Hitchman, T.S.1    Crosby, J.2    Byrom, K.J.3    Cox, R.J.4    Simpson, T.J.5
  • 108
    • 34447562562 scopus 로고    scopus 로고
    • Self-acylation properties of type II fatty acid biosynthesis acyl carrier protein
    • Misra A, Sharma SK, Surolia N, Surolia A. 2007. Self-acylation properties of type II fatty acid biosynthesis acyl carrier protein. Chem Biol 14:775-783.
    • (2007) Chem Biol , vol.14 , pp. 775-783
    • Misra, A.1    Sharma, S.K.2    Surolia, N.3    Surolia, A.4
  • 109
    • 0018841201 scopus 로고
    • Stoichiometry and stereochemistry of deuterium incorporated into fatty acids by cells of Escherichia coli grown on [methyl-2H3]acetate
    • White RH. 1980. Stoichiometry and stereochemistry of deuterium incorporated into fatty acids by cells of Escherichia coli grown on [methyl-2H3]acetate. Biochemistry 19:9-15.
    • (1980) Biochemistry , vol.19 , pp. 9-15
    • White, R.H.1
  • 110
    • 0023644886 scopus 로고
    • Acetoacetyl-acyl carrier protein synthase, a potential regulator of fatty acid biosynthesis in bacteria
    • Jackowski S, Rock CO. 1987. Acetoacetyl-acyl carrier protein synthase, a potential regulator of fatty acid biosynthesis in bacteria. J Biol Chem 262:7927-7931.
    • (1987) J Biol Chem , vol.262 , pp. 7927-7931
    • Jackowski, S.1    Rock, C.O.2
  • 111
    • 0026544037 scopus 로고
    • Overproduction of β-ketoacyl-acyl carrier protein synthase I imparts thiolactomycin resistance to Escherichia coli K-12
    • Tsay JT, Rock CO, Jackowski S. 1992. Overproduction of β-ketoacyl-acyl carrier protein synthase I imparts thiolactomycin resistance to Escherichia coli K-12. J Bacteriol 174:508-513.
    • (1992) J Bacteriol , vol.174 , pp. 508-513
    • Tsay, J.T.1    Rock, C.O.2    Jackowski, S.3
  • 112
    • 0015523037 scopus 로고
    • Acyl carrier protein. XV. Studies of β-ketoacyl-acyl carrier protein synthetase
    • Alberts AW, Bell RM, Vagelos PR. 1972. Acyl carrier protein. XV. Studies of β-ketoacyl-acyl carrier protein synthetase. J Biol Chem 247:3190-3198.
    • (1972) J Biol Chem , vol.247 , pp. 3190-3198
    • Alberts, A.W.1    Bell, R.M.2    Vagelos, P.R.3
  • 113
    • 0024287128 scopus 로고
    • Purification and characterization of [acyl-carrier-protein] acetyltransferase from Escherichia coli
    • Lowe PN, Rhodes S. 1988. Purification and characterization of [acyl-carrier-protein] acetyltransferase from Escherichia coli. Biochem J 250:789-796.
    • (1988) Biochem J , vol.250 , pp. 789-796
    • Lowe, P.N.1    Rhodes, S.2
  • 114
    • 0035797903 scopus 로고    scopus 로고
    • A Streptomyces collinus thiolase with novel acetyl-CoA:acyl carrier protein transacylase activity
    • Lobo S, Florova G, Reynolds KA. 2001. A Streptomyces collinus thiolase with novel acetyl-CoA:acyl carrier protein transacylase activity. Biochemistry 40:11955-11964.
    • (2001) Biochemistry , vol.40 , pp. 11955-11964
    • Lobo, S.1    Florova, G.2    Reynolds, K.A.3
  • 115
    • 0035928728 scopus 로고    scopus 로고
    • β-Ketoacyl-[acyl carrier protein] synthase I of Escherichia coli: aspects of the condensation mechanism revealed by analyses of mutations in the active site pocket
    • McGuire KA, Siggaard-Andersen M, Bangera MG, Olsen JG, von Wettstein-Knowles P. 2001. β-Ketoacyl-[acyl carrier protein] synthase I of Escherichia coli: aspects of the condensation mechanism revealed by analyses of mutations in the active site pocket. Biochemistry 40:9836-9845.
    • (2001) Biochemistry , vol.40 , pp. 9836-9845
    • McGuire, K.A.1    Siggaard-Andersen, M.2    Bangera, M.G.3    Olsen, J.G.4    von Wettstein-Knowles, P.5
  • 116
    • 0036233536 scopus 로고    scopus 로고
    • A missense mutation in the fabB β-ketoacyl-acyl carrier protein synthase I) gene confers thiolactomycin resistance to Escherichia coli
    • Jackowski S, Zhang YM, Price AC, White SW, Rock CO. 2002. A missense mutation in the fabB β-ketoacyl-acyl carrier protein synthase I) gene confers thiolactomycin resistance to Escherichia coli. Antimicrob Agents Chemother 46:1246-1252.
    • (2002) Antimicrob Agents Chemother , vol.46 , pp. 1246-1252
    • Jackowski, S.1    Zhang, Y.M.2    Price, A.C.3    White, S.W.4    Rock, C.O.5
  • 117
    • 0029045836 scopus 로고
    • Regulation of malonyl-CoA metabolism by acyl-acyl carrier protein and β-ketoacyl-acyl carrier protein synthases in Escherichia coli
    • Heath RJ, Rock CO. 1995. Regulation of malonyl-CoA metabolism by acyl-acyl carrier protein and β-ketoacyl-acyl carrier protein synthases in Escherichia coli. J Biol Chem 270:15531-15538.
    • (1995) J Biol Chem , vol.270 , pp. 15531-15538
    • Heath, R.J.1    Rock, C.O.2
  • 118
    • 0347065345 scopus 로고    scopus 로고
    • β-Ketoacyl-acyl carrier protein synthase III (FabH) is essential for bacterial fatty acid synthesis
    • Lai CY, Cronan JE. 2003. β-Ketoacyl-acyl carrier protein synthase III (FabH) is essential for bacterial fatty acid synthesis. J Biol Chem 278:51494-51503.
    • (2003) J Biol Chem , vol.278 , pp. 51494-51503
    • Lai, C.Y.1    Cronan, J.E.2
  • 119
    • 34447302085 scopus 로고    scopus 로고
    • Recent developments in naturally derived antimalarials: cryptolepine analogues
    • Wright CW. 2007. Recent developments in naturally derived antimalarials: cryptolepine analogues. J Pharm Pharmacol 59:899-904.
    • (2007) J Pharm Pharmacol , vol.59 , pp. 899-904
    • Wright, C.W.1
  • 120
    • 0016756653 scopus 로고
    • β-Ketoacyl-acyl carrier protein synthetase. Characterization of the acyl-enzyme intermediate
    • D'Agnolo G, Rosenfeld IS, Vagelos PR. 1975. β-Ketoacyl-acyl carrier protein synthetase. Characterization of the acyl-enzyme intermediate. J Biol Chem 250:5283-5288.
    • (1975) J Biol Chem , vol.250 , pp. 5283-5288
    • D'Agnolo, G.1    Rosenfeld, I.S.2    Vagelos, P.R.3
  • 121
    • 0028173383 scopus 로고
    • The fabJ-encoded β- ketoacyl-[acyl carrier protein] synthase IV from Escherichia coli is sensitive to cerulenin and specific for short-chain substrates
    • Siggaard-Andersen M, Wissenbach M, Chuck JA, Svendsen I, Olsen JG, von Wettstein-Knowles P. 1994. The fabJ-encoded β- ketoacyl-[acyl carrier protein] synthase IV from Escherichia coli is sensitive to cerulenin and specific for short-chain substrates. Proc Natl Acad Sci USA 91:11027-11031.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 11027-11031
    • Siggaard-Andersen, M.1    Wissenbach, M.2    Chuck, J.A.3    Svendsen, I.4    Olsen, J.G.5    von Wettstein-Knowles, P.6
  • 122
    • 0029043220 scopus 로고
    • The putative fabJ gene of Escherichia coli fatty acid synthesis is the fabF gene
    • Magnuson K, Carey MR, Cronan JE Jr. 1995. The putative fabJ gene of Escherichia coli fatty acid synthesis is the fabF gene. J Bacteriol 177:3593-3595.
    • (1995) J Bacteriol , vol.177 , pp. 3593-3595
    • Magnuson, K.1    Carey, M.R.2    Cronan, J.E.3
  • 123
    • 0036775842 scopus 로고    scopus 로고
    • The Claisen condensation in biology
    • Heath RJ, Rock CO. 2002. The Claisen condensation in biology. Nat Prod Rep 19:581-596.
    • (2002) Nat Prod Rep , vol.19 , pp. 581-596
    • Heath, R.J.1    Rock, C.O.2
  • 124
    • 0019275308 scopus 로고
    • Structural, enzymatic, and genetic studies of β-ketoacyl-acyl carrier protein synthases I and II of Escherichia coli
    • Garwin JL, Klages AL, Cronan JE Jr. 1980. Structural, enzymatic, and genetic studies of β-ketoacyl-acyl carrier protein synthases I and II of Escherichia coli. J Biol Chem 255:11949-11956.
    • (1980) J Biol Chem , vol.255 , pp. 11949-11956
    • Garwin, J.L.1    Klages, A.L.2    Cronan, J.E.3
  • 125
    • 0024146365 scopus 로고
    • β-Ketoacyl-ACP synthase I of Escherichia coli: nucleotide sequence of the fabB gene and identification of the cerulenin binding residue
    • Kauppinen S, Siggaard-Anderson M, van Wettstein-Knowles P. 1988. β-Ketoacyl-ACP synthase I of Escherichia coli: nucleotide sequence of the fabB gene and identification of the cerulenin binding residue. Carlsberg Res Commun 53:357-370.
    • (1988) Carlsberg Res Commun , vol.53 , pp. 357-370
    • Kauppinen, S.1    Siggaard-Anderson, M.2    van Wettstein-Knowles, P.3
  • 126
    • 0016734774 scopus 로고
    • Multiple forms of β-ketoacyl-acyl carrier protein synthetase in Escherichia coli
    • D'Agnolo G, Rosenfeld IS, Vagelos PR. 1975. Multiple forms of β-ketoacyl-acyl carrier protein synthetase in Escherichia coli. J Biol Chem 250:5289-5294.
    • (1975) J Biol Chem , vol.250 , pp. 5289-5294
    • D'Agnolo, G.1    Rosenfeld, I.S.2    Vagelos, P.R.3
  • 127
    • 0020646350 scopus 로고
    • Genetic and biochemical analyses of Escherichia coli mutants altered in the temperature-dependent regulation of membrane lipid composition
    • Ulrich AK, de Mendoza D, Garwin JL, Cronan JE Jr. 1983. Genetic and biochemical analyses of Escherichia coli mutants altered in the temperature-dependent regulation of membrane lipid composition. J Bacteriol 154:221-230.
    • (1983) J Bacteriol , vol.154 , pp. 221-230
    • Ulrich, A.K.1    de Mendoza, D.2    Garwin, J.L.3    Cronan, J.E.4
  • 128
    • 0343052737 scopus 로고    scopus 로고
    • Cloning of the fabF gene in an expression vector and in vitro characterization of recombinant fabF and fabB encoded enzymes from Escherichia coli
    • Edwards P, Nelsen JS, Metz JG, Dehesh K. 1997. Cloning of the fabF gene in an expression vector and in vitro characterization of recombinant fabF and fabB encoded enzymes from Escherichia coli. FEBS Lett 402:62-66.
    • (1997) FEBS Lett , vol.402 , pp. 62-66
    • Edwards, P.1    Nelsen, J.S.2    Metz, J.G.3    Dehesh, K.4
  • 129
    • 0014595487 scopus 로고
    • Evidence for two genes specifically involved in unsaturated fatty acid biosynthesis in Escherichia coli
    • Cronan JE Jr, Birge CH, Vagelos PR. 1969. Evidence for two genes specifically involved in unsaturated fatty acid biosynthesis in Escherichia coli. J Bacteriol 100:601-604.
    • (1969) J Bacteriol , vol.100 , pp. 601-604
    • Cronan, J.E.1    Birge, C.H.2    Vagelos, P.R.3
  • 130
    • 0018969670 scopus 로고
    • β-Ketoacyl-acyl carrier protein synthase II of Escherichia coli. Evidence for function in the thermal regulation of fatty acid synthesis
    • Garwin JL, Klages AL, Cronan JE Jr. 1980. β-Ketoacyl-acyl carrier protein synthase II of Escherichia coli. Evidence for function in the thermal regulation of fatty acid synthesis. J Biol Chem 255:3263-3265.
    • (1980) J Biol Chem , vol.255 , pp. 3263-3265
    • Garwin, J.L.1    Klages, A.L.2    Cronan, J.E.3
  • 131
    • 0021096466 scopus 로고
    • β-Hydroxydecanoyl thio ester dehydrase does not catalyze a rate-limiting step in Escherichia coli unsaturated fatty acid synthesis
    • Clark DP, DeMendoza D, Polacco ML, Cronan JE Jr. 1983. β-Hydroxydecanoyl thio ester dehydrase does not catalyze a rate-limiting step in Escherichia coli unsaturated fatty acid synthesis. Biochemistry 22:5897-5902.
    • (1983) Biochemistry , vol.22 , pp. 5897-5902
    • Clark, D.P.1    DeMendoza, D.2    Polacco, M.L.3    Cronan, J.E.4
  • 132
    • 0020531889 scopus 로고
    • Thermal regulation of membrane fluidity in Escherichia coli. Effects of overproduction of β-ketoacyl-acyl carrier protein synthase I
    • de Mendoza D, Klages Ulrich A, Cronan JE Jr. 1983. Thermal regulation of membrane fluidity in Escherichia coli. Effects of overproduction of β-ketoacyl-acyl carrier protein synthase I. J Biol Chem 258:2098-2101.
    • (1983) J Biol Chem , vol.258 , pp. 2098-2101
    • de Mendoza, D.1    Klages Ulrich, A.2    Cronan, J.E.3
  • 133
    • 0031783528 scopus 로고    scopus 로고
    • Overproduction of a functional fatty acid biosynthetic enzyme blocks fatty acid synthesis in Escherichia coli
    • Subrahmanyam S, Cronan JE Jr. 1998. Overproduction of a functional fatty acid biosynthetic enzyme blocks fatty acid synthesis in Escherichia coli. J Bacteriol 180:4596-4602.
    • (1998) J Bacteriol , vol.180 , pp. 4596-4602
    • Subrahmanyam, S.1    Cronan, J.E.2
  • 134
    • 0029941170 scopus 로고    scopus 로고
    • Polar allele duplication for transcriptional analysis of consecutive essential genes: application to a cluster of Escherichia coli fatty acid biosynthetic genes
    • Zhang Y, Cronan JE Jr. 1996. Polar allele duplication for transcriptional analysis of consecutive essential genes: application to a cluster of Escherichia coli fatty acid biosynthetic genes. J Bacteriol 178:3614-3620.
    • (1996) J Bacteriol , vol.178 , pp. 3614-3620
    • Zhang, Y.1    Cronan, J.E.2
  • 135
    • 0031801906 scopus 로고    scopus 로고
    • Transcriptional analysis of essential genes of the Escherichia coli fatty acid biosynthesis gene cluster by functional replacement with the analogous Salmonella typhimurium gene cluster
    • Zhang Y, Cronan JE Jr. 1998. Transcriptional analysis of essential genes of the Escherichia coli fatty acid biosynthesis gene cluster by functional replacement with the analogous Salmonella typhimurium gene cluster. J Bacteriol 180:3295-3303.
    • (1998) J Bacteriol , vol.180 , pp. 3295-3303
    • Zhang, Y.1    Cronan, J.E.2
  • 136
    • 1542286897 scopus 로고    scopus 로고
    • Isolation and characterization of β-ketoacyl-acyl carrier protein reductase (fabG) mutants of Escherichia coli and Salmonella enterica serovar Typhimurium
    • Lai CY, Cronan JE. 2004. Isolation and characterization of β-ketoacyl-acyl carrier protein reductase (fabG) mutants of Escherichia coli and Salmonella enterica serovar Typhimurium. J Bacteriol 186:1869-1878.
    • (2004) J Bacteriol , vol.186 , pp. 1869-1878
    • Lai, C.Y.1    Cronan, J.E.2
  • 137
    • 0014220972 scopus 로고
    • A β-hydroxydecanoyl-ACP dehydrase specific for saturated fatty acid biosynthesis in E. coli
    • Birge CH, Silbert DF, Vagelos PR. 1967. A β-hydroxydecanoyl-ACP dehydrase specific for saturated fatty acid biosynthesis in E. coli. Biochem Biophys Res Commun 29:808-814.
    • (1967) Biochem Biophys Res Commun , vol.29 , pp. 808-814
    • Birge, C.H.1    Silbert, D.F.2    Vagelos, P.R.3
  • 138
    • 0014407012 scopus 로고
    • Intermediate- and long-chain β-hydroxyacyl-ACP dehydrases from E. coli fatty acid synthetase
    • Mizugaki M, Swindell AC, Wakil SJ. 1968. Intermediate- and long-chain β-hydroxyacyl-ACP dehydrases from E. coli fatty acid synthetase. Biochem Biophys Res Commun 33:520-527.
    • (1968) Biochem Biophys Res Commun , vol.33 , pp. 520-527
    • Mizugaki, M.1    Swindell, A.C.2    Wakil, S.J.3
  • 139
    • 0029926496 scopus 로고    scopus 로고
    • Roles of the FabA and FabZ β- hydroxyacyl-acyl carrier protein dehydratases in Escherichia coli fatty acid biosynthesis
    • Heath RJ, Rock CO. 1996. Roles of the FabA and FabZ β- hydroxyacyl-acyl carrier protein dehydratases in Escherichia coli fatty acid biosynthesis. J Biol Chem 271:27795-27801.
    • (1996) J Biol Chem , vol.271 , pp. 27795-27801
    • Heath, R.J.1    Rock, C.O.2
  • 140
    • 0028584330 scopus 로고
    • An Escherichia coli gene (fabZ) encoding (3R)- hydroxymyristoyl acyl carrier protein dehydrase. Relation to fabA and suppression of mutations in lipid A biosynthesis
    • Mohan S, Kelly TM, Eveland SS, Raetz CR, Anderson MS. 1994. An Escherichia coli gene (fabZ) encoding (3R)- hydroxymyristoyl acyl carrier protein dehydrase. Relation to fabA and suppression of mutations in lipid A biosynthesis. J Biol Chem 269:32896-32903.
    • (1994) J Biol Chem , vol.269 , pp. 32896-32903
    • Mohan, S.1    Kelly, T.M.2    Eveland, S.S.3    Raetz, C.R.4    Anderson, M.S.5
  • 142
    • 4544303329 scopus 로고    scopus 로고
    • Functional replacement of the FabA and FabB proteins of Escherichia coli fatty acid synthesis by Enterococcus faecalis FabZ and FabF homologues
    • Wang H, Cronan JE. 2004. Functional replacement of the FabA and FabB proteins of Escherichia coli fatty acid synthesis by Enterococcus faecalis FabZ and FabF homologues. J Biol Chem 279:34489-34495.
    • (2004) J Biol Chem , vol.279 , pp. 34489-34495
    • Wang, H.1    Cronan, J.E.2
  • 143
    • 0014429312 scopus 로고
    • Studies on the mechanism of fatty acid synthesis. 18. Preparation and general properties of the enoyl acyl carrier protein reductases from Escherichia coli
    • Weeks G, Wakil SJ. 1968. Studies on the mechanism of fatty acid synthesis. 18. Preparation and general properties of the enoyl acyl carrier protein reductases from Escherichia coli. J Biol Chem 243:1180-1189.
    • (1968) J Biol Chem , vol.243 , pp. 1180-1189
    • Weeks, G.1    Wakil, S.J.2
  • 144
    • 0030431493 scopus 로고    scopus 로고
    • The enoyl-[acyl-carrier-protein] reductase (FabI) of Escherichia coli, which catalyzes a key regulatory step in fatty acid biosynthesis, accepts NADH and NADPH as cofactors and is inhibited by palmitoyl-CoA
    • Bergler H, Fuchsbichler S, Hogenauer G, Turnowsky F. 1996. The enoyl-[acyl-carrier-protein] reductase (FabI) of Escherichia coli, which catalyzes a key regulatory step in fatty acid biosynthesis, accepts NADH and NADPH as cofactors and is inhibited by palmitoyl-CoA. Eur J Biochem 242:689-694.
    • (1996) Eur J Biochem , vol.242 , pp. 689-694
    • Bergler, H.1    Fuchsbichler, S.2    Hogenauer, G.3    Turnowsky, F.4
  • 145
    • 0024331888 scopus 로고
    • envM genes of Salmonella typhimurium and Escherichia coli
    • Turnowsky F, Fuchs K, Jeschek C, Hogenauer G. 1989. envM genes of Salmonella typhimurium and Escherichia coli. J Bacteriol 171:6555-6565.
    • (1989) J Bacteriol , vol.171 , pp. 6555-6565
    • Turnowsky, F.1    Fuchs, K.2    Jeschek, C.3    Hogenauer, G.4
  • 146
    • 0028484071 scopus 로고
    • The use of a hybrid genetic system to study the functional relationship between prokaryotic and plant multi-enzyme fatty acid synthetase complexes
    • Kater MM, Koningstein GM, Nijkamp HJ, Stuitje AR. 1994. The use of a hybrid genetic system to study the functional relationship between prokaryotic and plant multi-enzyme fatty acid synthetase complexes. Plant Mol Biol 25:771-790.
    • (1994) Plant Mol Biol , vol.25 , pp. 771-790
    • Kater, M.M.1    Koningstein, G.M.2    Nijkamp, H.J.3    Stuitje, A.R.4
  • 148
    • 0032490937 scopus 로고    scopus 로고
    • Triclosan targets lipid synthesis
    • McMurry LM, Oethinger M, Levy SB. 1998. Triclosan targets lipid synthesis. Nature 394:531-532.
    • (1998) Nature , vol.394 , pp. 531-532
    • McMurry, L.M.1    Oethinger, M.2    Levy, S.B.3
  • 151
    • 0025353421 scopus 로고
    • Escherichia coli β-hydroxydecanoyl thioester dehydrase reacts with native C10 acyl-acyl-carrier proteins of plant and bacterial origin
    • Guerra DJ, Browse JA. 1990. Escherichia coli β-hydroxydecanoyl thioester dehydrase reacts with native C10 acyl-acyl-carrier proteins of plant and bacterial origin. Arch Biochem Biophys 280:336-345.
    • (1990) Arch Biochem Biophys , vol.280 , pp. 336-345
    • Guerra, D.J.1    Browse, J.A.2
  • 152
    • 0030584655 scopus 로고    scopus 로고
    • Structure of a dehydratase-isomerase from the bacterial pathway for biosynthesis of unsaturated fatty acids: two catalytic activities in one active site
    • Leesong M, Henderson BS, Gillig JR, Schwab JM, Smith JL. 1996. Structure of a dehydratase-isomerase from the bacterial pathway for biosynthesis of unsaturated fatty acids: two catalytic activities in one active site. Structure 4:253-264.
    • (1996) Structure , vol.4 , pp. 253-264
    • Leesong, M.1    Henderson, B.S.2    Gillig, J.R.3    Schwab, J.M.4    Smith, J.L.5
  • 153
    • 0014141616 scopus 로고
    • Fatty acid mutant of E. coli lacking a β-hydroxydecanoyl thioester dehydrase
    • Silbert DF, Vagelos PR. 1967. Fatty acid mutant of E. coli lacking a β-hydroxydecanoyl thioester dehydrase. Proc Natl Acad Sci USA 58:1579-1586.
    • (1967) Proc Natl Acad Sci USA , vol.58 , pp. 1579-1586
    • Silbert, D.F.1    Vagelos, P.R.2
  • 154
    • 0015935279 scopus 로고
    • An estimate of the minimum amount of unsaturated fatty acid required for growth of Escherichia coli
    • Cronan JE Jr, Gelmann EP. 1973. An estimate of the minimum amount of unsaturated fatty acid required for growth of Escherichia coli. J Biol Chem 248:1188-1195.
    • (1973) J Biol Chem , vol.248 , pp. 1188-1195
    • Cronan, J.E.1    Gelmann, E.P.2
  • 155
    • 0018826602 scopus 로고
    • Regulation of phospholipid biosynthesis in Escherichia coli. Cloning of the structural gene for the biosynthetic sn-glycerol-3- phosphate dehydrogenase
    • Clark D, Lightner V, Edgar R, Modrich P, Cronan JE Jr, Bell RM. 1980. Regulation of phospholipid biosynthesis in Escherichia coli. Cloning of the structural gene for the biosynthetic sn-glycerol-3- phosphate dehydrogenase. J Biol Chem 255:714-717.
    • (1980) J Biol Chem , vol.255 , pp. 714-717
    • Clark, D.1    Lightner, V.2    Edgar, R.3    Modrich, P.4    Cronan, J.E.5    Bell, R.M.6
  • 156
    • 0000088190 scopus 로고
    • Enzyme-catalyzed allylic rearrangements
    • Schwab J, Henderson J. 1990. Enzyme-catalyzed allylic rearrangements. Chem Rev 90:1203-1245.
    • (1990) Chem Rev , vol.90 , pp. 1203-1245
    • Schwab, J.1    Henderson, J.2
  • 157
    • 0023933734 scopus 로고
    • Derived amino acid sequence and identification of active site residues of Escherichia coli β-hydroxydecanoyl thioester dehydrase
    • Cronan JE Jr, Li WB, Coleman R, Narasimhan M, de Mendoza D, Schwab JM. 1988. Derived amino acid sequence and identification of active site residues of Escherichia coli β-hydroxydecanoyl thioester dehydrase. J Biol Chem 263:4641-4646.
    • (1988) J Biol Chem , vol.263 , pp. 4641-4646
    • Cronan, J.E.1    Li, W.B.2    Coleman, R.3    Narasimhan, M.4    de Mendoza, D.5    Schwab, J.M.6
  • 158
    • 33846259725 scopus 로고    scopus 로고
    • Coordinate expression of the acetyl coenzyme A carboxylase genes, accB and accC, is necessary for normal regulation of biotin synthesis in Escherichia coli
    • Abdel-Hamid AM, Cronan JE. 2007. Coordinate expression of the acetyl coenzyme A carboxylase genes, accB and accC, is necessary for normal regulation of biotin synthesis in Escherichia coli. J Bacteriol 189:369-376.
    • (2007) J Bacteriol , vol.189 , pp. 369-376
    • Abdel-Hamid, A.M.1    Cronan, J.E.2
  • 159
    • 1642576086 scopus 로고    scopus 로고
    • Expression of two Escherichia coli acetyl-CoA carboxylase subunits is autoregulated
    • James ES, Cronan JE. 2004. Expression of two Escherichia coli acetyl-CoA carboxylase subunits is autoregulated. J Biol Chem 279:2520-2527.
    • (2004) J Biol Chem , vol.279 , pp. 2520-2527
    • James, E.S.1    Cronan, J.E.2
  • 160
    • 0026499452 scopus 로고
    • The lethal phenotype caused by null mutations in the Escherichia coli htrB gene is suppressed by mutations in the accBC operon, encoding two subunits of acetyl coenzyme A carboxylase
    • Karow M, Fayet O, Georgopoulos C. 1992. The lethal phenotype caused by null mutations in the Escherichia coli htrB gene is suppressed by mutations in the accBC operon, encoding two subunits of acetyl coenzyme A carboxylase. J Bacteriol 174:7407-7418.
    • (1992) J Bacteriol , vol.174 , pp. 7407-7418
    • Karow, M.1    Fayet, O.2    Georgopoulos, C.3
  • 161
    • 0035157890 scopus 로고    scopus 로고
    • Escherichia coli FadR positively regulates transcription of the fabB fatty acid biosynthetic gene
    • Campbell JW, Cronan JE Jr. 2001. Escherichia coli FadR positively regulates transcription of the fabB fatty acid biosynthetic gene. J Bacteriol 183:5982-5990.
    • (2001) J Bacteriol , vol.183 , pp. 5982-5990
    • Campbell, J.W.1    Cronan, J.E.2
  • 162
    • 0026660312 scopus 로고
    • A new mechanism of transcriptional regulation: release of an activator triggered by small molecule binding
    • Henry MF, Cronan JE Jr. 1992. A new mechanism of transcriptional regulation: release of an activator triggered by small molecule binding. Cell 70:671-679.
    • (1992) Cell , vol.70 , pp. 671-679
    • Henry, M.F.1    Cronan, J.E.2
  • 163
    • 0026335805 scopus 로고
    • Escherichia coli transcription factor that both activates fatty acid synthesis and represses fatty acid degradation
    • Henry MF, Cronan JE Jr. 1991. Escherichia coli transcription factor that both activates fatty acid synthesis and represses fatty acid degradation. J Mol Biol 222:843-849.
    • (1991) J Mol Biol , vol.222 , pp. 843-849
    • Henry, M.F.1    Cronan, J.E.2
  • 164
    • 0020560953 scopus 로고
    • Role for fadR in unsaturated fatty acid biosynthesis in Escherichia coli
    • Nunn WD, Giffin K, Clark D, Cronan JE Jr. 1983. Role for fadR in unsaturated fatty acid biosynthesis in Escherichia coli. J Bacteriol 154:554-560.
    • (1983) J Bacteriol , vol.154 , pp. 554-560
    • Nunn, W.D.1    Giffin, K.2    Clark, D.3    Cronan, J.E.4
  • 165
    • 0027464211 scopus 로고
    • Regulation of transcription of genes required for fatty acid transport and unsaturated fatty acid biosynthesis in Escherichia coli by FadR
    • DiRusso CC, Metzger AK, Heimert TL. 1993. Regulation of transcription of genes required for fatty acid transport and unsaturated fatty acid biosynthesis in Escherichia coli by FadR. Mol Microbiol 7:311-322.
    • (1993) Mol Microbiol , vol.7 , pp. 311-322
    • DiRusso, C.C.1    Metzger, A.K.2    Heimert, T.L.3
  • 166
    • 0026003072 scopus 로고
    • Control site location and transcriptional regulation in Escherichia coli
    • Collado-Vides J, Magasanik B, Gralla JD. 1991. Control site location and transcriptional regulation in Escherichia coli. Microbiol Rev 55:371-394.
    • (1991) Microbiol Rev , vol.55 , pp. 371-394
    • Collado-Vides, J.1    Magasanik, B.2    Gralla, J.D.3
  • 167
    • 0026713687 scopus 로고
    • Characterization of FadR, a global transcriptional regulator of fatty acid metabolism in Escherichia coli. Interaction with the fadB promoter is prevented by long chain fatty acyl coenzyme A
    • DiRusso CC, Heimert TL, Metzger AK. 1992. Characterization of FadR, a global transcriptional regulator of fatty acid metabolism in Escherichia coli. Interaction with the fadB promoter is prevented by long chain fatty acyl coenzyme A. J Biol Chem 267:8685-8691.
    • (1992) J Biol Chem , vol.267 , pp. 8685-8691
    • DiRusso, C.C.1    Heimert, T.L.2    Metzger, A.K.3
  • 168
    • 0030692787 scopus 로고    scopus 로고
    • Characterization of the fatty acid-responsive transcription factor FadR. Biochemical and genetic analyses of the native conformation and functional domains
    • Raman N, Black PN, DiRusso CC. 1997. Characterization of the fatty acid-responsive transcription factor FadR. Biochemical and genetic analyses of the native conformation and functional domains. J Biol Chem 272:30645-30650.
    • (1997) J Biol Chem , vol.272 , pp. 30645-30650
    • Raman, N.1    Black, P.N.2    DiRusso, C.C.3
  • 169
    • 0028860254 scopus 로고
    • Analysis of acyl coenzyme A binding to the transcription factor FadR and identification of amino acid residues in the carboxyl terminus required for ligand binding
    • Raman N, DiRusso CC. 1995. Analysis of acyl coenzyme A binding to the transcription factor FadR and identification of amino acid residues in the carboxyl terminus required for ligand binding. J Biol Chem 270:1092-1097.
    • (1995) J Biol Chem , vol.270 , pp. 1092-1097
    • Raman, N.1    DiRusso, C.C.2
  • 170
    • 0035901537 scopus 로고    scopus 로고
    • The structural basis of acyl coenzyme A-dependent regulation of the transcription factor FadR
    • van Aalten DM, DiRusso CC, Knudsen J. 2001. The structural basis of acyl coenzyme A-dependent regulation of the transcription factor FadR. EMBO J 20:2041-2050.
    • (2001) EMBO J , vol.20 , pp. 2041-2050
    • van Aalten, D.M.1    DiRusso, C.C.2    Knudsen, J.3
  • 171
    • 0034597011 scopus 로고    scopus 로고
    • Crystal structure of FadR, a fatty acid-responsive transcription factor with a novel acyl coenzyme A-binding fold
    • van Aalten DM, DiRusso CC, Knudsen J, Wierenga RK. 2000. Crystal structure of FadR, a fatty acid-responsive transcription factor with a novel acyl coenzyme A-binding fold. EMBO J 19:5167-5177.
    • (2000) EMBO J , vol.19 , pp. 5167-5177
    • van Aalten, D.M.1    DiRusso, C.C.2    Knudsen, J.3    Wierenga, R.K.4
  • 172
    • 0035907285 scopus 로고    scopus 로고
    • The FadR. DNA complex. Transcriptional control of fatty acid metabolism in Escherichia coli
    • Xu Y, Heath RJ, Li Z, Rock CO, White SW. 2001. The FadR. DNA complex. Transcriptional control of fatty acid metabolism in Escherichia coli. J Biol Chem 276:17373-17379.
    • (2001) J Biol Chem , vol.276 , pp. 17373-17379
    • Xu, Y.1    Heath, R.J.2    Li, Z.3    Rock, C.O.4    White, S.W.5
  • 174
    • 0037013190 scopus 로고    scopus 로고
    • The FabR (YijC) transcription factor regulates unsaturated fatty acid biosynthesis in Escherichia coli
    • Zhang YM, Marrakchi H, Rock CO. 2002. The FabR (YijC) transcription factor regulates unsaturated fatty acid biosynthesis in Escherichia coli. J Biol Chem 277:15558-15565.
    • (2002) J Biol Chem , vol.277 , pp. 15558-15565
    • Zhang, Y.M.1    Marrakchi, H.2    Rock, C.O.3
  • 175
    • 33846610096 scopus 로고    scopus 로고
    • Identification of amino acid residues involved in substrate specificity of plant acyl-ACP thioesterases using a bioinformatics-guided approach
    • Mayer KM, Shanklin J. 2007. Identification of amino acid residues involved in substrate specificity of plant acyl-ACP thioesterases using a bioinformatics-guided approach. BMC Plant Biol 7:1.
    • (2007) BMC Plant Biol , vol.7 , pp. 1
    • Mayer, K.M.1    Shanklin, J.2
  • 176
    • 0028149560 scopus 로고
    • Alteration of the specificity and regulation of fatty acid synthesis of Escherichia coli by expression of a plant medium-chain acyl-acyl carrier protein thioesterase
    • Voelker TA, Davies HM. 1994. Alteration of the specificity and regulation of fatty acid synthesis of Escherichia coli by expression of a plant medium-chain acyl-acyl carrier protein thioesterase. J Bacteriol 176:7320-7327.
    • (1994) J Bacteriol , vol.176 , pp. 7320-7327
    • Voelker, T.A.1    Davies, H.M.2
  • 177
    • 0018171197 scopus 로고
    • Thioesterases I and II of Escherichia coli. Hydrolysis of native acyl-acyl carrier protein thioesters
    • Spencer AK, Greenspan AD, Cronan JE Jr. 1978. Thioesterases I and II of Escherichia coli. Hydrolysis of native acyl-acyl carrier protein thioesters. J Biol Chem 253:5922-5926.
    • (1978) J Biol Chem , vol.253 , pp. 5922-5926
    • Spencer, A.K.1    Greenspan, A.D.2    Cronan, J.E.3
  • 178
    • 0014409277 scopus 로고
    • Studies on the mechanism of fatty acid synthesis. XIX. Preparation and general properties of palmityl thioesterase
    • Barnes EM Jr, Wakil SJ. 1968. Studies on the mechanism of fatty acid synthesis. XIX. Preparation and general properties of palmityl thioesterase. J Biol Chem 243:2955-2962.
    • (1968) J Biol Chem , vol.243 , pp. 2955-2962
    • Barnes, E.M.1    Wakil, S.J.2
  • 179
    • 0027255719 scopus 로고
    • Escherichia coli thioesterase I, molecular cloning and sequencing of the structural gene and identification as a periplasmic enzyme
    • Cho H, Cronan JE Jr. 1993. Escherichia coli thioesterase I, molecular cloning and sequencing of the structural gene and identification as a periplasmic enzyme. J Biol Chem 268:9238-9245.
    • (1993) J Biol Chem , vol.268 , pp. 9238-9245
    • Cho, H.1    Cronan, J.E.2
  • 180
    • 0028960890 scopus 로고
    • Defective export of a periplasmic enzyme disrupts regulation of fatty acid synthesis
    • Cho H, Cronan JE Jr. 1995. Defective export of a periplasmic enzyme disrupts regulation of fatty acid synthesis. J Biol Chem 270:4216-4219.
    • (1995) J Biol Chem , vol.270 , pp. 4216-4219
    • Cho, H.1    Cronan, J.E.2
  • 181
    • 0033046667 scopus 로고    scopus 로고
    • Production of medium-chain-length poly(3-hydroxyalkanoates) from gluconate by recombinant Escherichia coli
    • Klinke S, Ren Q, Witholt B, Kessler B. 1999. Production of medium-chain-length poly(3-hydroxyalkanoates) from gluconate by recombinant Escherichia coli. Appl Environ Microbiol 65:540-548.
    • (1999) Appl Environ Microbiol , vol.65 , pp. 540-548
    • Klinke, S.1    Ren, Q.2    Witholt, B.3    Kessler, B.4
  • 182
    • 0031054314 scopus 로고    scopus 로고
    • In vivo evidence that acyl coenzyme A regulates DNA binding by the Escherichia coli FadR global transcription factor
    • Cronan JE Jr. 1997. In vivo evidence that acyl coenzyme A regulates DNA binding by the Escherichia coli FadR global transcription factor. J Bacteriol 179:1819-1823.
    • (1997) J Bacteriol , vol.179 , pp. 1819-1823
    • Cronan, J.E.1
  • 183
    • 0028176615 scopus 로고
    • "Protease I" of Escherichia coli functions as a thioesterase in vivo
    • Cho H, Cronan JE Jr. 1994. "Protease I" of Escherichia coli functions as a thioesterase in vivo. J Bacteriol 176:1793-1795.
    • (1994) J Bacteriol , vol.176 , pp. 1793-1795
    • Cho, H.1    Cronan, J.E.2
  • 184
    • 0027461466 scopus 로고
    • Molecular cloning, sequencing, and mapping of the gene encoding protease I and characterization of proteinase and proteinase- defective Escherichia coli mutants
    • Ichihara S, Matsubara Y, Kato C, Akasaka K, Mizushima S. 1993. Molecular cloning, sequencing, and mapping of the gene encoding protease I and characterization of proteinase and proteinase- defective Escherichia coli mutants. J Bacteriol 175:1032-1037.
    • (1993) J Bacteriol , vol.175 , pp. 1032-1037
    • Ichihara, S.1    Matsubara, Y.2    Kato, C.3    Akasaka, K.4    Mizushima, S.5
  • 187
    • 0029758922 scopus 로고    scopus 로고
    • Conversion of serine-114 to cysteine-114 and the role of the active site nucleophile in acyl transfer by myristoyl-ACP thioesterase from Vibrio harveyi
    • Li J, Szittner R, Derewenda ZS, Meighen EA. 1996. Conversion of serine-114 to cysteine-114 and the role of the active site nucleophile in acyl transfer by myristoyl-ACP thioesterase from Vibrio harveyi. Biochemistry 35:9967-9973.
    • (1996) Biochemistry , vol.35 , pp. 9967-9973
    • Li, J.1    Szittner, R.2    Derewenda, Z.S.3    Meighen, E.A.4
  • 188
    • 0032839515 scopus 로고    scopus 로고
    • The Escherichia coli pldC gene encoding lysophospholipase L(1) is identical to the apeA and tesA genes encoding protease I and thioesterase I, respectively
    • Karasawa K, Yokoyama K, Setaka M, Nojima S. 1999. The Escherichia coli pldC gene encoding lysophospholipase L(1) is identical to the apeA and tesA genes encoding protease I and thioesterase I, respectively. J Biochem (Tokyo) 126:445-448.
    • (1999) J Biochem (Tokyo) , vol.126 , pp. 445-448
    • Karasawa, K.1    Yokoyama, K.2    Setaka, M.3    Nojima, S.4
  • 189
    • 0016835997 scopus 로고
    • Lysophospholipase of Escherichia coli
    • Doi O, Nojima S. 1975. Lysophospholipase of Escherichia coli. J Biol Chem 250:5208-5214.
    • (1975) J Biol Chem , vol.250 , pp. 5208-5214
    • Doi, O.1    Nojima, S.2
  • 190
    • 0038723702 scopus 로고    scopus 로고
    • Crystal structure of Escherichia coli thioesterase I/protease I/lysophospholipase L1: consensus sequence blocks constitute the catalytic center of SGNHhydrolases through a conserved hydrogen bond network
    • Lo YC, Lin SC, Shaw JF, Liaw YC. 2003. Crystal structure of Escherichia coli thioesterase I/protease I/lysophospholipase L1: consensus sequence blocks constitute the catalytic center of SGNHhydrolases through a conserved hydrogen bond network. J Mol Biol 330:539-551.
    • (2003) J Mol Biol , vol.330 , pp. 539-551
    • Lo, Y.C.1    Lin, S.C.2    Shaw, J.F.3    Liaw, Y.C.4
  • 191
    • 33745542346 scopus 로고    scopus 로고
    • Functional role of catalytic triad and oxyanion hole-forming residues on enzyme activity of Escherichia coli thioesterase I/protease I/phospholipase L1
    • Lee LC, Lee YL, Leu RJ, Shaw JF. 2006. Functional role of catalytic triad and oxyanion hole-forming residues on enzyme activity of Escherichia coli thioesterase I/protease I/phospholipase L1. Biochem J 397:69-76.
    • (2006) Biochem J , vol.397 , pp. 69-76
    • Lee, L.C.1    Lee, Y.L.2    Leu, R.J.3    Shaw, J.F.4
  • 192
    • 34547459487 scopus 로고    scopus 로고
    • Enhanced preference for pi-bond containing substrates is correlated to Pro110 in the substrate- binding tunnel of Escherichia coli thioesterase I/protease I/lysophospholipase L(1)
    • Lee LC, Liaw YC, Lee YL, Shaw JF. 2007. Enhanced preference for pi-bond containing substrates is correlated to Pro110 in the substrate- binding tunnel of Escherichia coli thioesterase I/protease I/lysophospholipase L(1). Biochim Biophys Acta 1774:959-967.
    • (2007) Biochim Biophys Acta , vol.1774 , pp. 959-967
    • Lee, L.C.1    Liaw, Y.C.2    Lee, Y.L.3    Shaw, J.F.4
  • 193
    • 0038164679 scopus 로고    scopus 로고
    • Sequential structural changes of Escherichia coli thioesterase/protease I in the serial formation of Michaelis and tetrahedral complexes with diethyl p-nitrophenyl phosphate
    • Tyukhtenko SI, Litvinchuk AV, Chang CF, Lo YC, Lee SJ, Shaw JF, Liaw YC, Huang TH. 2003. Sequential structural changes of Escherichia coli thioesterase/protease I in the serial formation of Michaelis and tetrahedral complexes with diethyl p-nitrophenyl phosphate. Biochemistry 42:8289-8297.
    • (2003) Biochemistry , vol.42 , pp. 8289-8297
    • Tyukhtenko, S.I.1    Litvinchuk, A.V.2    Chang, C.F.3    Lo, Y.C.4    Lee, S.J.5    Shaw, J.F.6    Liaw, Y.C.7    Huang, T.H.8
  • 194
    • 0015523017 scopus 로고
    • Purification and properties of fatty acyl thioesterase I from Escherichia coli
    • Bonner WM, Bloch K. 1972. Purification and properties of fatty acyl thioesterase I from Escherichia coli. J Biol Chem 247:3123-3133.
    • (1972) J Biol Chem , vol.247 , pp. 3123-3133
    • Bonner, W.M.1    Bloch, K.2
  • 195
    • 0022455531 scopus 로고
    • Genetic and biochemical characterization of an Escherichia coli K-12 mutant deficient in acyl-coenzyme A thioesterase II
    • Narasimhan ML, Lampi JL, Cronan JE Jr. 1986. Genetic and biochemical characterization of an Escherichia coli K-12 mutant deficient in acyl-coenzyme A thioesterase II. J Bacteriol 165:911-917.
    • (1986) J Bacteriol , vol.165 , pp. 911-917
    • Narasimhan, M.L.1    Lampi, J.L.2    Cronan, J.E.3
  • 196
    • 19244382596 scopus 로고    scopus 로고
    • Mutation of a conserved residue (D123) required for oligomerization of human immunodeficiency virus type 1 Nef protein abolishes interaction with human thioesterase and results in impairment of Nef biological functions
    • Liu LX, Heveker N, Fackler OT, Arold S, Le Gall S, Janvier K, Peterlin BM, Dumas C, Schwartz O, Benichou S, Benarous R. 2000. Mutation of a conserved residue (D123) required for oligomerization of human immunodeficiency virus type 1 Nef protein abolishes interaction with human thioesterase and results in impairment of Nef biological functions. J Virol 74:5310-5319.
    • (2000) J Virol , vol.74 , pp. 5310-5319
    • Liu, L.X.1    Heveker, N.2    Fackler, O.T.3    Arold, S.4    Le Gall, S.5    Janvier, K.6    Peterlin, B.M.7    Dumas, C.8    Schwartz, O.9    Benichou, S.10    Benarous, R.11
  • 197
    • 0030920271 scopus 로고    scopus 로고
    • Binding of HIV-1 Nef to a novel thioesterase enzyme correlates with Nef-mediated CD4 down-regulation
    • Liu LX, Margottin F, Le Gall S, Schwartz O, Selig L, Benarous R, Benichou S. 1997. Binding of HIV-1 Nef to a novel thioesterase enzyme correlates with Nef-mediated CD4 down-regulation. J Biol Chem 272:13779-13785.
    • (1997) J Biol Chem , vol.272 , pp. 13779-13785
    • Liu, L.X.1    Margottin, F.2    Le Gall, S.3    Schwartz, O.4    Selig, L.5    Benarous, R.6    Benichou, S.7
  • 198
    • 0033936807 scopus 로고    scopus 로고
    • Crystal structure of the Escherichia coli thioesterase II, a homolog of the human Nef binding enzyme
    • Li J, Derewenda U, Dauter Z, Smith S, Derewenda ZS. 2000. Crystal structure of the Escherichia coli thioesterase II, a homolog of the human Nef binding enzyme. Nat Struct Biol 7:555-559.
    • (2000) Nat Struct Biol , vol.7 , pp. 555-559
    • Li, J.1    Derewenda, U.2    Dauter, Z.3    Smith, S.4    Derewenda, Z.S.5
  • 199
    • 3242770756 scopus 로고    scopus 로고
    • Thioesterase II of Escherichia coli plays an important role in 3- hydroxydecanoic acid production
    • Zheng Z, Gong Q, Liu T, Deng Y, Chen JC, Chen GQ. 2004. Thioesterase II of Escherichia coli plays an important role in 3- hydroxydecanoic acid production. Appl Environ Microbiol 70:3807-3813.
    • (2004) Appl Environ Microbiol , vol.70 , pp. 3807-3813
    • Zheng, Z.1    Gong, Q.2    Liu, T.3    Deng, Y.4    Chen, J.C.5    Chen, G.Q.6
  • 200
    • 0014409506 scopus 로고
    • Catalysis of water oxygen and of acetate incorporation into fatty acids by Escherichia coli fatty acid synthetase
    • Kaplan A, Boyer PD. 1968. Catalysis of water oxygen and of acetate incorporation into fatty acids by Escherichia coli fatty acid synthetase. J Biol Chem 243:4077-4082.
    • (1968) J Biol Chem , vol.243 , pp. 4077-4082
    • Kaplan, A.1    Boyer, P.D.2
  • 201
    • 0019295718 scopus 로고
    • Biosynthetic control of the natural abundance of carbon 13 at specific positions within fatty acids in Escherichia coli. Evidence regarding the coupling of fatty acid and phospholipid synthesis
    • Monson KD, Hayes JM. 1980. Biosynthetic control of the natural abundance of carbon 13 at specific positions within fatty acids in Escherichia coli. Evidence regarding the coupling of fatty acid and phospholipid synthesis. J Biol Chem 255:11435-11441.
    • (1980) J Biol Chem , vol.255 , pp. 11435-11441
    • Monson, K.D.1    Hayes, J.M.2
  • 202
    • 0020641705 scopus 로고
    • Periplasmic glycerophosphodiester phosphodiesterase of Escherichia coli, a new enzyme of the glp regulon
    • Larson T, Ehrmann M, Boos W. 1883. Periplasmic glycerophosphodiester phosphodiesterase of Escherichia coli, a new enzyme of the glp regulon. J Biol Chem 258:5428-5432.
    • (1883) J Biol Chem , vol.258 , pp. 5428-5432
    • Larson, T.1    Ehrmann, M.2    Boos, W.3
  • 203
    • 0028032946 scopus 로고
    • Guanosine tetraphosphate inhibition of fatty acid and phospholipid synthesis in Escherichia coli is relieved by overexpression of glycerol-3-phosphate acyltransferase (plsB)
    • Heath RJ, Jackowski S, Rock CO. 1994. Guanosine tetraphosphate inhibition of fatty acid and phospholipid synthesis in Escherichia coli is relieved by overexpression of glycerol-3-phosphate acyltransferase (plsB). J Biol Chem 269:26584-26590.
    • (1994) J Biol Chem , vol.269 , pp. 26584-26590
    • Heath, R.J.1    Jackowski, S.2    Rock, C.O.3
  • 204
    • 0015322320 scopus 로고
    • Control of fatty acid synthesis in bacteria
    • Mindich L. 1972. Control of fatty acid synthesis in bacteria. J Bacteriol 110:96-102.
    • (1972) J Bacteriol , vol.110 , pp. 96-102
    • Mindich, L.1
  • 205
    • 0016702792 scopus 로고
    • Regulation of membrane lipid synthesis in Escherichia coli. Accumulation of free fatty acids of abnormal length during inhibition of phospholipid synthesis
    • Cronan JE Jr, Weisberg LJ, Allen RG. 1975. Regulation of membrane lipid synthesis in Escherichia coli. Accumulation of free fatty acids of abnormal length during inhibition of phospholipid synthesis. J Biol Chem 250:5835-5840.
    • (1975) J Biol Chem , vol.250 , pp. 5835-5840
    • Cronan, J.E.1    Weisberg, L.J.2    Allen, R.G.3
  • 206
    • 0023141067 scopus 로고
    • Fatty acid metabolism in sn-glycerol-3-phosphate acyltransferase (plsB) mutants
    • Cooper CL, Jackowski S, Rock CO. 1987. Fatty acid metabolism in sn-glycerol-3-phosphate acyltransferase (plsB) mutants. J Bacteriol 169:605-611.
    • (1987) J Bacteriol , vol.169 , pp. 605-611
    • Cooper, C.L.1    Jackowski, S.2    Rock, C.O.3
  • 207
    • 0017655173 scopus 로고
    • Regulation of fatty acid synthesis during the cessation of phospholipid biosynthesis in Escherichia coli
    • Nunn WD, Kelly DL, Stumfall MY. 1977. Regulation of fatty acid synthesis during the cessation of phospholipid biosynthesis in Escherichia coli. J Bacteriol 132:526-531.
    • (1977) J Bacteriol , vol.132 , pp. 526-531
    • Nunn, W.D.1    Kelly, D.L.2    Stumfall, M.Y.3
  • 208
    • 84959051704 scopus 로고
    • Composition phospholipidique de mutants thermosensibles d'Escherichia coli K 12
    • Barbin A, Peypoux F, Michel G. 1970. Composition phospholipidique de mutants thermosensibles d'Escherichia coli K 12. Biochim Biophys Acta 218:453-462.
    • (1970) Biochim Biophys Acta , vol.218 , pp. 453-462
    • Barbin, A.1    Peypoux, F.2    Michel, G.3
  • 209
    • 0014294940 scopus 로고
    • Phospholipid alterations during growth of Escherichia coli
    • Cronan JE Jr. 1968. Phospholipid alterations during growth of Escherichia coli. J Bacteriol 95:2054-2061.
    • (1968) J Bacteriol , vol.95 , pp. 2054-2061
    • Cronan, J.E.1
  • 210
    • 0028821432 scopus 로고
    • Cloning and expression in Escherichia coli of a novel thioesterase from Arabidopsis thaliana specific for long-chain acyl-acyl carrier proteins
    • Dormann P, Voelker TA, Ohlrogge JB. 1995. Cloning and expression in Escherichia coli of a novel thioesterase from Arabidopsis thaliana specific for long-chain acyl-acyl carrier proteins. Arch Biochem Biophys 316:612-618.
    • (1995) Arch Biochem Biophys , vol.316 , pp. 612-618
    • Dormann, P.1    Voelker, T.A.2    Ohlrogge, J.B.3
  • 211
    • 0015040624 scopus 로고
    • Fatty acid degradation in Escherichia coli. An inducible system for the uptake of fatty acids and further characterization of old mutants
    • Klein K, Steinberg R, Fiethen B, Overath P. 1971. Fatty acid degradation in Escherichia coli. An inducible system for the uptake of fatty acids and further characterization of old mutants. Eur J Biochem 19:442-450.
    • (1971) Eur J Biochem , vol.19 , pp. 442-450
    • Klein, K.1    Steinberg, R.2    Fiethen, B.3    Overath, P.4
  • 212
    • 4444335028 scopus 로고    scopus 로고
    • The Escherichia coli fadK (ydiD) gene encodes an anaerobically regulated short chain acyl-CoA synthetase
    • Morgan-Kiss RM, Cronan JE. 2004. The Escherichia coli fadK (ydiD) gene encodes an anaerobically regulated short chain acyl-CoA synthetase. J Biol Chem 279:37324-37333.
    • (2004) J Biol Chem , vol.279 , pp. 37324-37333
    • Morgan-Kiss, R.M.1    Cronan, J.E.2
  • 213
    • 17544367317 scopus 로고    scopus 로고
    • Inhibition of β-ketoacyl-acyl carrier protein synthase III (FabH) by acyl-acyl carrier protein in Escherichia col
    • Heath RJ, Rock CO. 1996. Inhibition of β-ketoacyl-acyl carrier protein synthase III (FabH) by acyl-acyl carrier protein in Escherichia col. J Biol Chem 271:10996-11000.
    • (1996) J Biol Chem , vol.271 , pp. 10996-11000
    • Heath, R.J.1    Rock, C.O.2
  • 214
    • 0030033704 scopus 로고    scopus 로고
    • Regulation of fatty acid elongation and initiation by acyl-acyl carrier protein in Escherichia coli
    • Heath RJ, Rock CO. 1996. Regulation of fatty acid elongation and initiation by acyl-acyl carrier protein in Escherichia coli. J Biol Chem 271:1833-1836.
    • (1996) J Biol Chem , vol.271 , pp. 1833-1836
    • Heath, R.J.1    Rock, C.O.2
  • 215
    • 0000421938 scopus 로고
    • Effect of temperature on the composition of fatty acids in Escherichia coli
    • Marr AG, Ingraham JL. 1962. Effect of temperature on the composition of fatty acids in Escherichia coli. J Bacteriol 84:1260-1267.
    • (1962) J Bacteriol , vol.84 , pp. 1260-1267
    • Marr, A.G.1    Ingraham, J.L.2
  • 216
    • 0018860548 scopus 로고
    • Thermal modulation of fatty acid synthesis in Escherichia coli does not involve de novo enzyme synthesis
    • Garwin JL, Cronan JE Jr. 1980. Thermal modulation of fatty acid synthesis in Escherichia coli does not involve de novo enzyme synthesis. J Bacteriol 141:1457-1459.
    • (1980) J Bacteriol , vol.141 , pp. 1457-1459
    • Garwin, J.L.1    Cronan, J.E.2
  • 217
    • 0020372996 scopus 로고
    • Overproduction of cis-vaccenic acid and altered temperature control of fatty acid synthesis in a mutant of Escherichia coli
    • de Mendoza D, Garwin JL, Cronan JE Jr. 1982. Overproduction of cis-vaccenic acid and altered temperature control of fatty acid synthesis in a mutant of Escherichia coli. J Bacteriol 151:1608-1611.
    • (1982) J Bacteriol , vol.151 , pp. 1608-1611
    • de Mendoza, D.1    Garwin, J.L.2    Cronan, J.E.3
  • 218
    • 0026775039 scopus 로고
    • Isolation and characterization of the β-ketoacyl-acyl carrier protein synthase III gene (fabH) from Escherichia coli K-12
    • Tsay JT, Oh W, Larson TJ, Jackowski S, Rock CO. 1992. Isolation and characterization of the β-ketoacyl-acyl carrier protein synthase III gene (fabH) from Escherichia coli K-12. J Biol Chem 267:6807-6814.
    • (1992) J Biol Chem , vol.267 , pp. 6807-6814
    • Tsay, J.T.1    Oh, W.2    Larson, T.J.3    Jackowski, S.4    Rock, C.O.5
  • 219
    • 0014686318 scopus 로고
    • A mutant of Escherichia coli defective in phosphatidic acid synthesis
    • Kito M, Lubin M, Pizer LI. 1969. A mutant of Escherichia coli defective in phosphatidic acid synthesis. Biochem Biophys Res Commun 34:454-458.
    • (1969) Biochem Biophys Res Commun , vol.34 , pp. 454-458
    • Kito, M.1    Lubin, M.2    Pizer, L.I.3
  • 220
    • 0014483640 scopus 로고
    • Phosphatidic acid synthesis in Escherichia coli
    • Kito M, Pizer LI. 1969. Phosphatidic acid synthesis in Escherichia coli. J Bacteriol 97:1321-1327.
    • (1969) J Bacteriol , vol.97 , pp. 1321-1327
    • Kito, M.1    Pizer, L.I.2
  • 221
    • 0014690601 scopus 로고
    • Purification and regulatory properties of the biosynthetic L-glycerol 3-phosphate dehydrogenase from Escherichia coli
    • Kito M, Pizer LI. 1969. Purification and regulatory properties of the biosynthetic L-glycerol 3-phosphate dehydrogenase from Escherichia coli. J Biol Chem 244:3316-3323.
    • (1969) J Biol Chem , vol.244 , pp. 3316-3323
    • Kito, M.1    Pizer, L.I.2
  • 222
    • 0016235686 scopus 로고
    • Mutants of Escherichia coli defective in membrane phospholipid synthesis: mapping of sn-glycerol 3-phosphate acyltransferase Km mutants
    • Cronan JE Jr, Bell RM. 1974. Mutants of Escherichia coli defective in membrane phospholipid synthesis: mapping of sn-glycerol 3-phosphate acyltransferase Km mutants. J Bacteriol 120:227-233.
    • (1974) J Bacteriol , vol.120 , pp. 227-233
    • Cronan, J.E.1    Bell, R.M.2
  • 223
    • 0016747352 scopus 로고
    • Mutants of Escherichia coli defective in membrane phospholipid synthesis. Phenotypic suppression of sn-glycerol-3-phosphate acyltransferase Km mutants by loss of feedback inhibition of the biosynthetic sn-glycerol-3-phosphate dehydrogenase
    • Bell RM, Cronan JE Jr. 1975. Mutants of Escherichia coli defective in membrane phospholipid synthesis. Phenotypic suppression of sn-glycerol-3-phosphate acyltransferase Km mutants by loss of feedback inhibition of the biosynthetic sn-glycerol-3-phosphate dehydrogenase. J Biol Chem 250:7153-7158.
    • (1975) J Biol Chem , vol.250 , pp. 7153-7158
    • Bell, R.M.1    Cronan, J.E.2
  • 224
    • 0019218027 scopus 로고
    • The positional distribution of fatty acids in Escherichia coli phospholipids is not regulated by sn-glycerol 3-phosphate levels
    • Goelz SE, Cronan JE Jr. 1980. The positional distribution of fatty acids in Escherichia coli phospholipids is not regulated by sn-glycerol 3-phosphate levels. J Bacteriol 144:462-464.
    • (1980) J Bacteriol , vol.144 , pp. 462-464
    • Goelz, S.E.1    Cronan, J.E.2
  • 225
    • 0016747351 scopus 로고
    • Mutants of Escherichia coli defective in membrane phospholipid synthesis. Properties of wild type and Km defective sn-glycerol-3-phosphate acyltransferase activities
    • Bell RM. 1975. Mutants of Escherichia coli defective in membrane phospholipid synthesis. Properties of wild type and Km defective sn-glycerol-3-phosphate acyltransferase activities. J Biol Chem 250:7147-7152.
    • (1975) J Biol Chem , vol.250 , pp. 7147-7152
    • Bell, R.M.1
  • 226
    • 0031941001 scopus 로고    scopus 로고
    • A conserved histidine is essential for glycerolipid acyltransferase catalysis
    • Heath RJ, Rock CO. 1998. A conserved histidine is essential for glycerolipid acyltransferase catalysis. J Bacteriol 180:1425-1430.
    • (1998) J Bacteriol , vol.180 , pp. 1425-1430
    • Heath, R.J.1    Rock, C.O.2
  • 227
    • 0021686501 scopus 로고
    • sn-Glycerol-3-phosphate auxotrophy of plsB strains of Escherichia coli: evidence that a second mutation, plsX, is required
    • Larson TJ, Ludtke DN, Bell RM. 1984. sn-Glycerol-3-phosphate auxotrophy of plsB strains of Escherichia coli: evidence that a second mutation, plsX, is required. J Bacteriol 160:711-717.
    • (1984) J Bacteriol , vol.160 , pp. 711-717
    • Larson, T.J.1    Ludtke, D.N.2    Bell, R.M.3
  • 228
    • 33747887074 scopus 로고    scopus 로고
    • Acyl-phosphates initiate membrane phospholipid synthesis in Grampositive pathogens
    • Lu YJ, Zhang YM, Grimes KD, Qi J, Lee RE, Rock CO. 2006. Acyl-phosphates initiate membrane phospholipid synthesis in Grampositive pathogens. Mol Cell 23:765-772.
    • (2006) Mol Cell , vol.23 , pp. 765-772
    • Lu, Y.J.1    Zhang, Y.M.2    Grimes, K.D.3    Qi, J.4    Lee, R.E.5    Rock, C.O.6
  • 229
    • 34548058048 scopus 로고    scopus 로고
    • Involvement of the YneS/YgiH and PlsX proteins in phospholipid biosynthesis in both Bacillus subtilis and Escherichia coli
    • Yoshimura M, Oshima T, Ogasawara N. 2007. Involvement of the YneS/YgiH and PlsX proteins in phospholipid biosynthesis in both Bacillus subtilis and Escherichia coli. BMC Microbiol 7:69.
    • (2007) BMC Microbiol , vol.7 , pp. 69
    • Yoshimura, M.1    Oshima, T.2    Ogasawara, N.3
  • 230
    • 0033031797 scopus 로고    scopus 로고
    • A missense mutation accounts for the defect in the glycerol-3-phosphate acyltransferase expressed in the plsB26 mutant
    • Heath RJ, Rock CO. 1999. A missense mutation accounts for the defect in the glycerol-3-phosphate acyltransferase expressed in the plsB26 mutant. J Bacteriol 181:1944-1946.
    • (1999) J Bacteriol , vol.181 , pp. 1944-1946
    • Heath, R.J.1    Rock, C.O.2
  • 231
    • 0017713566 scopus 로고
    • Mechanism of the apparent regulation of Escherichia coli unsaturated fatty acid synthesis by exogenous oleic acid
    • Polacco ML, Cronan JE Jr. 1977. Mechanism of the apparent regulation of Escherichia coli unsaturated fatty acid synthesis by exogenous oleic acid. J Biol Chem 252:5488-5490.
    • (1977) J Biol Chem , vol.252 , pp. 5488-5490
    • Polacco, M.L.1    Cronan, J.E.2
  • 232
    • 0025131925 scopus 로고
    • Characterization of Escherichia coli cells deficient in 1-acyl-sn-glycerol-3-phosphate acyltransferase activity
    • Coleman J. 1990. Characterization of Escherichia coli cells deficient in 1-acyl-sn-glycerol-3-phosphate acyltransferase activity. J Biol Chem 265:17215-17221.
    • (1990) J Biol Chem , vol.265 , pp. 17215-17221
    • Coleman, J.1
  • 233
    • 0026548077 scopus 로고
    • Characterization of the Escherichia coli gene for 1-acyl-sn-glycerol-3-phosphate acyltransferase (plsC)
    • Coleman J. 1992. Characterization of the Escherichia coli gene for 1-acyl-sn-glycerol-3-phosphate acyltransferase (plsC). Mol Gen Genet 232:295-303.
    • (1992) Mol Gen Genet , vol.232 , pp. 295-303
    • Coleman, J.1
  • 234
    • 0028519115 scopus 로고
    • Isolation and characterization of a maize cDNA that complements a 1-acyl sn-glycerol-3-phosphate acyltransferase mutant of Escherichia coli and encodes a protein which has similarities to other acyltransferases
    • Brown AP, Coleman J, Tommey AM, Watson MD, Slabas AR. 1994. Isolation and characterization of a maize cDNA that complements a 1-acyl sn-glycerol-3-phosphate acyltransferase mutant of Escherichia coli and encodes a protein which has similarities to other acyltransferases. Plant Mol Biol 26:211-223.
    • (1994) Plant Mol Biol , vol.26 , pp. 211-223
    • Brown, A.P.1    Coleman, J.2    Tommey, A.M.3    Watson, M.D.4    Slabas, A.R.5
  • 235
    • 0029153622 scopus 로고
    • A plant acyltransferase involved in triacylglycerol biosynthesis complements an Escherichia coli sn-1-acylglycerol-3-phosphate acyltransferase mutant
    • Hanke C, Wolter FP, Coleman J, Peterek G, Frentzen M. 1995. A plant acyltransferase involved in triacylglycerol biosynthesis complements an Escherichia coli sn-1-acylglycerol-3-phosphate acyltransferase mutant. Eur J Biochem 232:806-810.
    • (1995) Eur J Biochem , vol.232 , pp. 806-810
    • Hanke, C.1    Wolter, F.P.2    Coleman, J.3    Peterek, G.4    Frentzen, M.5
  • 237
    • 0030670712 scopus 로고    scopus 로고
    • A gene (plsD) from Clostridium butyricum that functionally substitutes for the sn-glycerol-3-phosphate acyltransferase gene (plsB) of Escherichia coli
    • Heath RJ, Goldfine H, Rock CO. 1997. A gene (plsD) from Clostridium butyricum that functionally substitutes for the sn-glycerol-3-phosphate acyltransferase gene (plsB) of Escherichia coli. J Bacteriol 179:7257-7263.
    • (1997) J Bacteriol , vol.179 , pp. 7257-7263
    • Heath, R.J.1    Goldfine, H.2    Rock, C.O.3
  • 238
    • 0024110267 scopus 로고
    • Membrane-bound phosphatases in Escherichia coli:sequence of the pgpB gene and dual subcellular localization of the pgpB product
    • Icho T. 1988. Membrane-bound phosphatases in Escherichia coli:sequence of the pgpB gene and dual subcellular localization of the pgpB product. J Bacteriol 170:5117-5124.
    • (1988) J Bacteriol , vol.170 , pp. 5117-5124
    • Icho, T.1
  • 239
    • 0019431621 scopus 로고
    • Phospholipid synthesis in Escherichia coli. Characteristics of fatty acid transfer from acylacyl carrier protein to sn-glycerol 3-phosphate
    • Rock CO, Goelz SE, Cronan JE Jr. 1981. Phospholipid synthesis in Escherichia coli. Characteristics of fatty acid transfer from acylacyl carrier protein to sn-glycerol 3-phosphate. J Biol Chem 256:736-742.
    • (1981) J Biol Chem , vol.256 , pp. 736-742
    • Rock, C.O.1    Goelz, S.E.2    Cronan, J.E.3
  • 240
    • 0014358261 scopus 로고
    • Cytidine triphosphate: phosphatidic acid cytidyltransferase in Escherichia coli
    • Carter JR Jr. 1968. Cytidine triphosphate: phosphatidic acid cytidyltransferase in Escherichia coli. J Lipid Res 9:748-754.
    • (1968) J Lipid Res , vol.9 , pp. 748-754
    • Carter, J.R.1
  • 241
    • 0001590175 scopus 로고
    • Metabolism and function of bacterial lipids. II. biosynthesis of phospholipids in Escherichia coli
    • Kanfer J, Kennedy EP. 1964. Metabolism and function of bacterial lipids. II. biosynthesis of phospholipids in Escherichia coli. J Biol Chem 239:1720-1726.
    • (1964) J Biol Chem , vol.239 , pp. 1720-1726
    • Kanfer, J.1    Kennedy, E.P.2
  • 242
    • 0015608814 scopus 로고
    • Characterization of the cardiolipin synthetase activity of Escherichia coli envelopes
    • Tunaitis E, Cronan JE Jr. 1973. Characterization of the cardiolipin synthetase activity of Escherichia coli envelopes. Arch Biochem Biophys 155:420-427.
    • (1973) Arch Biochem Biophys , vol.155 , pp. 420-427
    • Tunaitis, E.1    Cronan, J.E.2
  • 243
    • 0015919182 scopus 로고
    • Function of cytidine diphosphatediglyceride and deoxycytidine diphosphate-diglyceride in the biogenesis of membrane lipids in Escherichia coli
    • Raetz CR, Kennedy EP. 1973. Function of cytidine diphosphatediglyceride and deoxycytidine diphosphate-diglyceride in the biogenesis of membrane lipids in Escherichia coli. J Biol Chem 248:1098-1105.
    • (1973) J Biol Chem , vol.248 , pp. 1098-1105
    • Raetz, C.R.1    Kennedy, E.P.2
  • 244
    • 0031552991 scopus 로고    scopus 로고
    • CDP-diacylglycerol synthase of microorganisms
    • Dowhan W. 1997. CDP-diacylglycerol synthase of microorganisms. Biochim Biophys Acta 1348:157-165.
    • (1997) Biochim Biophys Acta , vol.1348 , pp. 157-165
    • Dowhan, W.1
  • 245
    • 0018825019 scopus 로고
    • Phosphatidic acid accumulation in the membranes of Escherichia coli mutants defective in CDP-diglyceride synthetase
    • Ganong BR, Leonard JM, Raetz CR. 1980. Phosphatidic acid accumulation in the membranes of Escherichia coli mutants defective in CDP-diglyceride synthetase. J Biol Chem 255:1623-1629.
    • (1980) J Biol Chem , vol.255 , pp. 1623-1629
    • Ganong, B.R.1    Leonard, J.M.2    Raetz, C.R.3
  • 246
    • 0020028720 scopus 로고
    • Massive accumulation of phosphatidic acid in conditionally lethal CDP-diglyceride synthetase mutants and cytidine auxotrophs of Escherichia coli
    • Ganong BR, Raetz CR. 1982. Massive accumulation of phosphatidic acid in conditionally lethal CDP-diglyceride synthetase mutants and cytidine auxotrophs of Escherichia coli. J Biol Chem 257:389-394.
    • (1982) J Biol Chem , vol.257 , pp. 389-394
    • Ganong, B.R.1    Raetz, C.R.2
  • 247
    • 0020660617 scopus 로고
    • pH-sensitive CDP-diglyceride synthetase mutants of Escherichia coli: phenotypic suppression by mutations at a second site
    • Ganong BR, Raetz CR. 1983. pH-sensitive CDP-diglyceride synthetase mutants of Escherichia coli: phenotypic suppression by mutations at a second site. J Bacteriol 153:731-738.
    • (1983) J Bacteriol , vol.153 , pp. 731-738
    • Ganong, B.R.1    Raetz, C.R.2
  • 248
    • 1542465944 scopus 로고    scopus 로고
    • Molecular and cell biology of phosphatidylserine and phosphatidylethanolamine metabolism
    • Vance JE. 2003. Molecular and cell biology of phosphatidylserine and phosphatidylethanolamine metabolism. Prog Nucleic Acid Res Mol Biol 75:69-111.
    • (2003) Prog Nucleic Acid Res Mol Biol , vol.75 , pp. 69-111
    • Vance, J.E.1
  • 249
    • 0018890180 scopus 로고
    • Investigations on the association of phosphatidylserine synthase with the ribosomal component from Escherichia coli
    • Louie K, Dowhan W. 1980. Investigations on the association of phosphatidylserine synthase with the ribosomal component from Escherichia coli. J Biol Chem 255:1124-1127.
    • (1980) J Biol Chem , vol.255 , pp. 1124-1127
    • Louie, K.1    Dowhan, W.2
  • 250
    • 4544365682 scopus 로고    scopus 로고
    • Lipid dependence and activity control of phosphatidylserine synthase from Escherichia coli
    • Linde K, Gröbner G, Rilfors L. 2004. Lipid dependence and activity control of phosphatidylserine synthase from Escherichia coli. FEBS Lett 575:77-80.
    • (2004) FEBS Lett , vol.575 , pp. 77-80
    • Linde, K.1    Gröbner, G.2    Rilfors, L.3
  • 251
    • 0022444435 scopus 로고
    • Substrate-induced membrane association of phosphatidylserine synthase from Escherichia coli
    • Louie K, Chen YC, Dowhan W. 1986. Substrate-induced membrane association of phosphatidylserine synthase from Escherichia coli. J Bacteriol 165:805-812.
    • (1986) J Bacteriol , vol.165 , pp. 805-812
    • Louie, K.1    Chen, Y.C.2    Dowhan, W.3
  • 252
    • 0032913497 scopus 로고    scopus 로고
    • Reconstituted phosphatidylserine synthase from Escherichia coli is activated by anionic phospholipids and micelleforming amphiphiles
    • Rilfors L, Niemi A, Haraldsson S, Edwards K, Andersson AS, Dowhan W. 1999. Reconstituted phosphatidylserine synthase from Escherichia coli is activated by anionic phospholipids and micelleforming amphiphiles. Biochim Biophys Acta 1438:281-294.
    • (1999) Biochim Biophys Acta , vol.1438 , pp. 281-294
    • Rilfors, L.1    Niemi, A.2    Haraldsson, S.3    Edwards, K.4    Andersson, A.S.5    Dowhan, W.6
  • 253
    • 0023668239 scopus 로고
    • Phospholipids chiral at phosphorus. Steric course of the reactions catalyzed by phosphatidylserine synthase from Escherichia coli and yeast
    • Raetz CR, Carman GM, Dowhan W, Jiang RT, Waszkuc W, Loffredo W, Tsai MD. 1987. Phospholipids chiral at phosphorus. Steric course of the reactions catalyzed by phosphatidylserine synthase from Escherichia coli and yeast. Biochemistry 26:4022-4027.
    • (1987) Biochemistry , vol.26 , pp. 4022-4027
    • Raetz, C.R.1    Carman, G.M.2    Dowhan, W.3    Jiang, R.T.4    Waszkuc, W.5    Loffredo, W.6    Tsai, M.D.7
  • 254
    • 0017836977 scopus 로고
    • Identification of bound pyruvate essential for the activity of phosphatidylserine decarboxylase of Escherichia coli
    • Satre M, Kennedy EP. 1978. Identification of bound pyruvate essential for the activity of phosphatidylserine decarboxylase of Escherichia coli. J Biol Chem 253:479-483.
    • (1978) J Biol Chem , vol.253 , pp. 479-483
    • Satre, M.1    Kennedy, E.P.2
  • 255
    • 0026519860 scopus 로고
    • Phosphatidylserine decarboxylase from Escherichia coli
    • Dowhan W, Li QX. 1992. Phosphatidylserine decarboxylase from Escherichia coli. Methods Enzymol 209:348-359.
    • (1992) Methods Enzymol , vol.209 , pp. 348-359
    • Dowhan, W.1    Li, Q.X.2
  • 256
    • 0025253340 scopus 로고
    • Studies on the mechanism of formation of the pyruvate prosthetic group of phosphatidylserine decarboxylase from Escherichia coli
    • Li QX, Dowhan W. 1990. Studies on the mechanism of formation of the pyruvate prosthetic group of phosphatidylserine decarboxylase from Escherichia coli. J Biol Chem 265:4111-4115.
    • (1990) J Biol Chem , vol.265 , pp. 4111-4115
    • Li, Q.X.1    Dowhan, W.2
  • 257
    • 0016785971 scopus 로고
    • Biogenesis of membrane lipids:mutants of Escherichia coli with temperature-sensitive phosphatidylserine decarboxylase
    • Hawrot E, Kennedy EP. 1975. Biogenesis of membrane lipids:mutants of Escherichia coli with temperature-sensitive phosphatidylserine decarboxylase. Proc Natl Acad Sci USA 72:1112-1116.
    • (1975) Proc Natl Acad Sci USA , vol.72 , pp. 1112-1116
    • Hawrot, E.1    Kennedy, E.P.2
  • 258
    • 0017147105 scopus 로고
    • Conditional lethal phosphatidylserine decarboxylase mutants of Escherichia coli. Mapping of the structural gene for phosphatidylserine decarboxylase
    • Hawrot E, Kennedy EP. 1976. Conditional lethal phosphatidylserine decarboxylase mutants of Escherichia coli. Mapping of the structural gene for phosphatidylserine decarboxylase. Mol Gen Genet 148:271-279.
    • (1976) Mol Gen Genet , vol.148 , pp. 271-279
    • Hawrot, E.1    Kennedy, E.P.2
  • 259
    • 0018122198 scopus 로고
    • Phospholipid composition and membrane function in phosphatidylserine decarboxylase mutants of Escherichia coli
    • Hawrot E, Kennedy EP. 1978. Phospholipid composition and membrane function in phosphatidylserine decarboxylase mutants of Escherichia coli. J Biol Chem 253:8213-8220.
    • (1978) J Biol Chem , vol.253 , pp. 8213-8220
    • Hawrot, E.1    Kennedy, E.P.2
  • 260
    • 0018786086 scopus 로고
    • Increased synthesis of phosphatidylserine decarboxylase in a strain of Escherichia coli bearing a hybrid plasmid. Altered association of enzyme with the membrane
    • Tyhach RJ, Hawrot E, Satre M, Kennedy EP. 1979. Increased synthesis of phosphatidylserine decarboxylase in a strain of Escherichia coli bearing a hybrid plasmid. Altered association of enzyme with the membrane. J Biol Chem 254:627-633.
    • (1979) J Biol Chem , vol.254 , pp. 627-633
    • Tyhach, R.J.1    Hawrot, E.2    Satre, M.3    Kennedy, E.P.4
  • 261
    • 0026416875 scopus 로고
    • Sequence and inactivation of the pss gene of Escherichia coli. Phosphatidylethanolamine may not be essential for cell viability
    • DeChavigny A, Heacock PN, Dowhan W. 1991. Sequence and inactivation of the pss gene of Escherichia coli. Phosphatidylethanolamine may not be essential for cell viability. J Biol Chem 266:10710.
    • (1991) J Biol Chem , vol.266 , pp. 10710
    • DeChavigny, A.1    Heacock, P.N.2    Dowhan, W.3
  • 262
    • 7044264920 scopus 로고    scopus 로고
    • Diversity and versatility of lipid-protein interactions revealed by molecular genetic approaches
    • Dowhan W, Mileykovskaya E, Bogdanov M. 2004. Diversity and versatility of lipid-protein interactions revealed by molecular genetic approaches. Biochim Biophys Acta 1666:19-39.
    • (2004) Biochim Biophys Acta , vol.1666 , pp. 19-39
    • Dowhan, W.1    Mileykovskaya, E.2    Bogdanov, M.3
  • 264
    • 0017043386 scopus 로고
    • Activation of long chain fatty acids with acyl carrier protein: demonstration of a new enzyme, acyl-acyl carrier protein synthetase, in Escherichia coli
    • Ray TK, Cronan JE Jr. 1976. Activation of long chain fatty acids with acyl carrier protein: demonstration of a new enzyme, acyl-acyl carrier protein synthetase, in Escherichia coli. Proc Natl Acad Sci USA 73:4374-4378.
    • (1976) Proc Natl Acad Sci USA , vol.73 , pp. 4374-4378
    • Ray, T.K.1    Cronan, J.E.2
  • 265
    • 0024551559 scopus 로고
    • 2-Acylglycerolphosphoethanolamine acyltransferase/acyl-acyl carrier protein synthetase is a membrane-associated acyl carrier protein binding protein
    • Cooper CL, Hsu L, Jackowski S, Rock CO. 1989. 2-Acylglycerolphosphoethanolamine acyltransferase/acyl-acyl carrier protein synthetase is a membrane-associated acyl carrier protein binding protein. J Biol Chem 264:7384-7389.
    • (1989) J Biol Chem , vol.264 , pp. 7384-7389
    • Cooper, C.L.1    Hsu, L.2    Jackowski, S.3    Rock, C.O.4
  • 266
    • 0018291891 scopus 로고
    • Solubilization, purification, and salt activation of acyl-acyl carrier protein synthetase from Escherichia coli
    • Rock CO, Cronan JE Jr. 1979. Solubilization, purification, and salt activation of acyl-acyl carrier protein synthetase from Escherichia coli. J Biol Chem 254:7116-7122.
    • (1979) J Biol Chem , vol.254 , pp. 7116-7122
    • Rock, C.O.1    Cronan, J.E.2
  • 267
    • 0022351664 scopus 로고
    • Pathways for the incorporation of exogenous fatty acids into phosphatidylethanolamine in Escherichia coli
    • Rock CO, Jackowski S. 1985. Pathways for the incorporation of exogenous fatty acids into phosphatidylethanolamine in Escherichia coli. J Biol Chem 260:12720-12724.
    • (1985) J Biol Chem , vol.260 , pp. 12720-12724
    • Rock, C.O.1    Jackowski, S.2
  • 268
    • 0034048280 scopus 로고    scopus 로고
    • Overexpression and purification of the Escherichia coli inner membrane enzyme acyl-acyl carrier protein synthase in an active form
    • Shanklin J. 2000. Overexpression and purification of the Escherichia coli inner membrane enzyme acyl-acyl carrier protein synthase in an active form. Protein Expr Purif 18:355-360.
    • (2000) Protein Expr Purif , vol.18 , pp. 355-360
    • Shanklin, J.1
  • 269
    • 0025900050 scopus 로고
    • Isolation and characterization of Escherichia coli K-12 mutants lacking both 2-acylglycerophosphoethanolamine acyltransferase and acyl-acyl carrier protein synthetase activity
    • Hsu L, Jackowski S, Rock CO. 1991. Isolation and characterization of Escherichia coli K-12 mutants lacking both 2-acylglycerophosphoethanolamine acyltransferase and acyl-acyl carrier protein synthetase activity. J Biol Chem 266:13783-13788.
    • (1991) J Biol Chem , vol.266 , pp. 13783-13788
    • Hsu, L.1    Jackowski, S.2    Rock, C.O.3
  • 270
    • 0026604494 scopus 로고
    • 2-Acylglycerophosphoethanolamine acyltransferase/acyl-[acyl-carrier- protein] synthetase from Escherichia coli
    • Jackowski S, Hsu L, Rock CO. 1992. 2-Acylglycerophosphoethanolamine acyltransferase/acyl-[acyl-carrier- protein] synthetase from Escherichia coli. Methods Enzymol 209:111-117.
    • (1992) Methods Enzymol , vol.209 , pp. 111-117
    • Jackowski, S.1    Hsu, L.2    Rock, C.O.3
  • 271
    • 0026588599 scopus 로고
    • Phosphatidylglycerophosphate synthase from Escherichia coli
    • Dowhan W. 1992. Phosphatidylglycerophosphate synthase from Escherichia coli. Methods Enzymol 209:313-321.
    • (1992) Methods Enzymol , vol.209 , pp. 313-321
    • Dowhan, W.1
  • 272
    • 0016372507 scopus 로고
    • The inhibition of phosphatidylglycerol synthesis in Escherichia coli by 3,4-dihydroxybutyl-1- phosphonate
    • Shopsis CS, Engel R, Tropp BE. 1974. The inhibition of phosphatidylglycerol synthesis in Escherichia coli by 3,4-dihydroxybutyl-1- phosphonate. J Biol Chem 249:2473-2477.
    • (1974) J Biol Chem , vol.249 , pp. 2473-2477
    • Shopsis, C.S.1    Engel, R.2    Tropp, B.E.3
  • 273
    • 0026480566 scopus 로고
    • The phosphonic acid analog of phosphatidylglycerol phosphate: influence on Escherichia coli growth and physiology
    • Ke L, Engel R, Tropp BE. 1992. The phosphonic acid analog of phosphatidylglycerol phosphate: influence on Escherichia coli growth and physiology. Biochim Biophys Acta 1128:250-257.
    • (1992) Biochim Biophys Acta , vol.1128 , pp. 250-257
    • Ke, L.1    Engel, R.2    Tropp, B.E.3
  • 274
    • 0023665097 scopus 로고
    • Construction of a lethal mutation in the synthesis of the major acidic phospholipids of Escherichia coli
    • Heacock PN, Dowhan W. 1987. Construction of a lethal mutation in the synthesis of the major acidic phospholipids of Escherichia coli. J Biol Chem 262:13044-13049.
    • (1987) J Biol Chem , vol.262 , pp. 13044-13049
    • Heacock, P.N.1    Dowhan, W.2
  • 275
    • 36048999506 scopus 로고    scopus 로고
    • Hyperexpression of the osmB gene in an acidic phospholipid- deficient Escherichia coli mutant
    • Nagahama H, Oshima T, Mori H, Matsumoto K, Hara H. 2007. Hyperexpression of the osmB gene in an acidic phospholipid- deficient Escherichia coli mutant. J Gen Appl Microbiol 53:143-151.
    • (2007) J Gen Appl Microbiol , vol.53 , pp. 143-151
    • Nagahama, H.1    Oshima, T.2    Mori, H.3    Matsumoto, K.4    Hara, H.5
  • 276
    • 33745224099 scopus 로고    scopus 로고
    • RcsA-dependent and -independent growth defects caused by the activated Rcs phosphorelay system in the Escherichia coli pgsA null mutant
    • Nagahama H, Sakamoto Y, Matsumoto K, Hara H. 2006. RcsA-dependent and -independent growth defects caused by the activated Rcs phosphorelay system in the Escherichia coli pgsA null mutant. J Gen Appl Microbiol 52:91-98.
    • (2006) J Gen Appl Microbiol , vol.52 , pp. 91-98
    • Nagahama, H.1    Sakamoto, Y.2    Matsumoto, K.3    Hara, H.4
  • 277
    • 0029828862 scopus 로고    scopus 로고
    • The Escherichia coli pgpB gene encodes for a diacylglycerol pyrophosphate phosphatase activity
    • Dillon DA, Wu WI, Riedel B, Wissing JB, Dowhan W, Carman GM. 1996. The Escherichia coli pgpB gene encodes for a diacylglycerol pyrophosphate phosphatase activity. J Biol Chem 271:30548-30553.
    • (1996) J Biol Chem , vol.271 , pp. 30548-30553
    • Dillon, D.A.1    Wu, W.I.2    Riedel, B.3    Wissing, J.B.4    Dowhan, W.5    Carman, G.M.6
  • 278
    • 0026534373 scopus 로고
    • Phosphatidylglycerophosphate phosphatase from Escherichia coli
    • Dowhan W, Funk CR. 1992. Phosphatidylglycerophosphate phosphatase from Escherichia coli. Methods Enzymol 209:224-230.
    • (1992) Methods Enzymol , vol.209 , pp. 224-230
    • Dowhan, W.1    Funk, C.R.2
  • 279
    • 0026597155 scopus 로고
    • The pgpA and pgpB genes of Escherichia coli are not essential: evidence for a third phosphatidylglycerophosphate phosphatase
    • Funk CR, Zimniak L, Dowhan W. 1992. The pgpA and pgpB genes of Escherichia coli are not essential: evidence for a third phosphatidylglycerophosphate phosphatase. J Bacteriol 174:205-213.
    • (1992) J Bacteriol , vol.174 , pp. 205-213
    • Funk, C.R.1    Zimniak, L.2    Dowhan, W.3
  • 280
    • 21444450859 scopus 로고    scopus 로고
    • Identification of multiple genes encoding membrane proteins with undecaprenyl pyrophosphate phosphatase (UppP) activity in Escherichia coli
    • El Ghachi M, Derbise A, Bouhss A, Mengin-Lecreulx D. 2005. Identification of multiple genes encoding membrane proteins with undecaprenyl pyrophosphate phosphatase (UppP) activity in Escherichia coli. J Biol Chem 280:18689-18695.
    • (2005) J Biol Chem , vol.280 , pp. 18689-18695
    • El Ghachi, M.1    Derbise, A.2    Bouhss, A.3    Mengin-Lecreulx, D.4
  • 281
    • 0023955825 scopus 로고
    • Disruption of the Escherichia coli cls gene responsible for cardiolipin synthesis
    • Nishijima S, Asami Y, Uetake N, Yamagoe S, Ohta A, Shibuya I. 1988. Disruption of the Escherichia coli cls gene responsible for cardiolipin synthesis. J Bacteriol 170:775-780.
    • (1988) J Bacteriol , vol.170 , pp. 775-780
    • Nishijima, S.1    Asami, Y.2    Uetake, N.3    Yamagoe, S.4    Ohta, A.5    Shibuya, I.6
  • 282
    • 0031552876 scopus 로고    scopus 로고
    • Cardiolipin synthase from Escherichia coli
    • Tropp BE. 1997. Cardiolipin synthase from Escherichia coli. Biochim Biophys Acta 1348:192-200.
    • (1997) Biochim Biophys Acta , vol.1348 , pp. 192-200
    • Tropp, B.E.1
  • 283
    • 0015302026 scopus 로고
    • Mechanism of the enzymatic synthesis of cardiolipin in Escherichia coli
    • Hirschberg CB, Kennedy EP. 1972. Mechanism of the enzymatic synthesis of cardiolipin in Escherichia coli. Proc Natl Acad Sci USA 69:648-651.
    • (1972) Proc Natl Acad Sci USA , vol.69 , pp. 648-651
    • Hirschberg, C.B.1    Kennedy, E.P.2
  • 284
    • 0017821432 scopus 로고
    • Function of phospholipids in Escherichia coli. Characterization of a mutant deficient in cardiolipin synthesis
    • Pluschke G, Hirota Y, Overath P. 1978. Function of phospholipids in Escherichia coli. Characterization of a mutant deficient in cardiolipin synthesis. J Biol Chem 253:5048-5055.
    • (1978) J Biol Chem , vol.253 , pp. 5048-5055
    • Pluschke, G.1    Hirota, Y.2    Overath, P.3
  • 285
    • 0021992333 scopus 로고
    • Alteration of phospholipid composition by combined defects in phosphatidylserine and cardiolipin synthases and physiological consequences in Escherichia coli
    • Shibuya I, Miyazaki C, Ohta A. 1985. Alteration of phospholipid composition by combined defects in phosphatidylserine and cardiolipin synthases and physiological consequences in Escherichia coli. J Bacteriol 161:1086-1092.
    • (1985) J Bacteriol , vol.161 , pp. 1086-1092
    • Shibuya, I.1    Miyazaki, C.2    Ohta, A.3
  • 286
    • 0027133440 scopus 로고
    • Active increase in cardiolipin synthesis in the stationary growth phase and its physiological significance in Escherichia coli
    • Hiraoka S, Matsuzaki H, Shibuya I. 1993. Active increase in cardiolipin synthesis in the stationary growth phase and its physiological significance in Escherichia coli. FEBS Lett 336:221-224.
    • (1993) FEBS Lett , vol.336 , pp. 221-224
    • Hiraoka, S.1    Matsuzaki, H.2    Shibuya, I.3
  • 288
    • 0033970689 scopus 로고    scopus 로고
    • A second Escherichia coli protein with CL synthase activity
    • Guo D, Tropp BE. 2000. A second Escherichia coli protein with CL synthase activity. Biochim Biophys Acta 1483:263-274.
    • (2000) Biochim Biophys Acta , vol.1483 , pp. 263-274
    • Guo, D.1    Tropp, B.E.2
  • 289
    • 0021929888 scopus 로고
    • Biosynthesis of novel acidic phospholipid analogs in Escherichia coli
    • Shibuya I, Yamagoe S, Miyazaki C, Matsuzaki H, Ohta A. 1985. Biosynthesis of novel acidic phospholipid analogs in Escherichia coli. J Bacteriol 161:473-477.
    • (1985) J Bacteriol , vol.161 , pp. 473-477
    • Shibuya, I.1    Yamagoe, S.2    Miyazaki, C.3    Matsuzaki, H.4    Ohta, A.5
  • 290
    • 0031457094 scopus 로고    scopus 로고
    • Cyclopropane ring formation in membrane lipids of bacteria
    • Grogan DW, Cronan JE Jr. 1997. Cyclopropane ring formation in membrane lipids of bacteria. Microbiol Mol Biol Rev 61:429-441.
    • (1997) Microbiol Mol Biol Rev , vol.61 , pp. 429-441
    • Grogan, D.W.1    Cronan, J.E.2
  • 291
    • 0033054689 scopus 로고    scopus 로고
    • Membrane cyclopropane fatty acid content is a major factor in acid resistance of Escherichia coli
    • Chang YY, Cronan JE Jr. 1999. Membrane cyclopropane fatty acid content is a major factor in acid resistance of Escherichia coli. Mol Microbiol 33:249-259.
    • (1999) Mol Microbiol , vol.33 , pp. 249-259
    • Chang, Y.Y.1    Cronan, J.E.2
  • 292
    • 0022647889 scopus 로고
    • Characterization of Escherichia coli mutants completely defective in synthesis of cyclopropane fatty acids
    • Grogan DW, Cronan JE Jr. 1986. Characterization of Escherichia coli mutants completely defective in synthesis of cyclopropane fatty acids. J Bacteriol 166:872-877.
    • (1986) J Bacteriol , vol.166 , pp. 872-877
    • Grogan, D.W.1    Cronan, J.E.2
  • 293
    • 13444288319 scopus 로고    scopus 로고
    • The formation of cyclopropane fatty acids in Salmonella enterica serovar Typhimurium
    • Kim BH, Kim S, Kim HG, Lee J, Lee IS, Park YK. 2005. The formation of cyclopropane fatty acids in Salmonella enterica serovar Typhimurium. Microbiology 151:209-218.
    • (2005) Microbiology , vol.151 , pp. 209-218
    • Kim, B.H.1    Kim, S.2    Kim, H.G.3    Lee, J.4    Lee, I.S.5    Park, Y.K.6
  • 294
    • 0026447153 scopus 로고
    • Cyclopropane fatty acid synthase of Escherichia coli: deduced amino acid sequence, purification, and studies of the enzyme active site
    • Wang AY, Grogan DW, Cronan JE Jr. 1992. Cyclopropane fatty acid synthase of Escherichia coli: deduced amino acid sequence, purification, and studies of the enzyme active site. Biochemistry 31:11020-11028.
    • (1992) Biochemistry , vol.31 , pp. 11020-11028
    • Wang, A.Y.1    Grogan, D.W.2    Cronan, J.E.3
  • 295
    • 11244252157 scopus 로고    scopus 로고
    • Escherichia coli cyclopropane fatty acid synthase
    • Courtois F, Guerard C, Thomas X, Ploux O. 2004. Escherichia coli cyclopropane fatty acid synthase. Eur J Biochem 271:4769-4778.
    • (2004) Eur J Biochem , vol.271 , pp. 4769-4778
    • Courtois, F.1    Guerard, C.2    Thomas, X.3    Ploux, O.4
  • 296
    • 6344243372 scopus 로고    scopus 로고
    • Isotope and elemental effects indicate a rate-limiting methyl transfer as the initial step in the reaction catalyzed by Escherichia coli cyclopropane fatty acid synthase
    • Iwig DF, Grippe AT, McIntyre TA, Booker SJ. 2004. Isotope and elemental effects indicate a rate-limiting methyl transfer as the initial step in the reaction catalyzed by Escherichia coli cyclopropane fatty acid synthase. Biochemistry 43:13510-13524.
    • (2004) Biochemistry , vol.43 , pp. 13510-13524
    • Iwig, D.F.1    Grippe, A.T.2    McIntyre, T.A.3    Booker, S.J.4
  • 297
    • 0028227365 scopus 로고
    • The growth phase-dependent synthesis of cyclopropane fatty acids in Escherichia coli is the result of an RpoS(KatF)-dependent promoter plus enzyme instability
    • Wang AY, Cronan JE Jr. 1994. The growth phase-dependent synthesis of cyclopropane fatty acids in Escherichia coli is the result of an RpoS(KatF)-dependent promoter plus enzyme instability. Mol Microbiol 11:1009-1017.
    • (1994) Mol Microbiol , vol.11 , pp. 1009-1017
    • Wang, A.Y.1    Cronan, J.E.2
  • 298
    • 0033927364 scopus 로고    scopus 로고
    • Metabolic instability of Escherichia coli cyclopropane fatty acid synthase is due to RpoHdependent proteolysis
    • Chang YY, Eichel J, Cronan JE Jr. 2000. Metabolic instability of Escherichia coli cyclopropane fatty acid synthase is due to RpoHdependent proteolysis. J Bacteriol 182:4288-4294.
    • (2000) J Bacteriol , vol.182 , pp. 4288-4294
    • Chang, Y.Y.1    Eichel, J.2    Cronan, J.E.3
  • 299
    • 33747794608 scopus 로고    scopus 로고
    • Identification of new inhibitors of Escherichia coli cyclopropane fatty acid synthase using a colorimetric assay
    • Guianvarc'h D, Drujon T, Leang TE, Courtois F, Ploux O. 2006. Identification of new inhibitors of Escherichia coli cyclopropane fatty acid synthase using a colorimetric assay. Biochim Biophys Acta 1764:1381-1388.
    • (2006) Biochim Biophys Acta , vol.1764 , pp. 1381-1388
    • Guianvarc'h, D.1    Drujon, T.2    Leang, T.E.3    Courtois, F.4    Ploux, O.5
  • 300
    • 26644465065 scopus 로고    scopus 로고
    • Escherichia coli cyclopropane fatty acid synthase: is a bound bicarbonate ion the active-site base?
    • Courtois F, Ploux O. 2005. Escherichia coli cyclopropane fatty acid synthase: is a bound bicarbonate ion the active-site base? Biochemistry 44:13583-13590.
    • (2005) Biochemistry , vol.44 , pp. 13583-13590
    • Courtois, F.1    Ploux, O.2
  • 301
    • 23944435441 scopus 로고    scopus 로고
    • The activity of Escherichia coli cyclopropane fatty acid synthase depends on the presence of bicarbonate
    • Iwig DF, Uchida A, Stromberg JA, Booker SJ. 2005. The activity of Escherichia coli cyclopropane fatty acid synthase depends on the presence of bicarbonate. J Am Chem Soc 127:11612-11613.
    • (2005) J Am Chem Soc , vol.127 , pp. 11612-11613
    • Iwig, D.F.1    Uchida, A.2    Stromberg, J.A.3    Booker, S.J.4
  • 304
    • 2942718769 scopus 로고    scopus 로고
    • Identification and characterization of the first class of potent bacterial acetyl-CoA carboxylase inhibitors with antibacterial activity
    • Freiberg C, Brunner NA, Schiffer G, Lampe T, Pohlmann J, Brands M, Raabe M, Habich D, Ziegelbauer K. 2004. Identification and characterization of the first class of potent bacterial acetyl-CoA carboxylase inhibitors with antibacterial activity. J Biol Chem 279:26066-26073.
    • (2004) J Biol Chem , vol.279 , pp. 26066-26073
    • Freiberg, C.1    Brunner, N.A.2    Schiffer, G.3    Lampe, T.4    Pohlmann, J.5    Brands, M.6    Raabe, M.7    Habich, D.8    Ziegelbauer, K.9
  • 306
    • 0027483921 scopus 로고
    • spoT-dependent accumulation of guanosine tetraphosphate in response to fatty acid starvation in Escherichia coli
    • Seyfzadeh M, Keener J, Nomura M. 1993. spoT-dependent accumulation of guanosine tetraphosphate in response to fatty acid starvation in Escherichia coli. Proc Natl Acad Sci USA 90:11004-11008.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 11004-11008
    • Seyfzadeh, M.1    Keener, J.2    Nomura, M.3
  • 307
    • 33750479525 scopus 로고    scopus 로고
    • Acyl carrier protein/SpoT interaction, the switch linking SpoT-dependent stress response to fatty acid metabolism
    • Battesti A, Bouveret E. 2006. Acyl carrier protein/SpoT interaction, the switch linking SpoT-dependent stress response to fatty acid metabolism. Mol Microbiol 62:1048-1063.
    • (2006) Mol Microbiol , vol.62 , pp. 1048-1063
    • Battesti, A.1    Bouveret, E.2
  • 308
    • 0024564710 scopus 로고
    • Acetoacetyl-acyl carrier protein synthase. A target for the antibiotic thiolactomycin
    • Jackowski S, Murphy CM, Cronan JE Jr, Rock CO. 1989. Acetoacetyl-acyl carrier protein synthase. A target for the antibiotic thiolactomycin. J Biol Chem 264:7624-7629.
    • (1989) J Biol Chem , vol.264 , pp. 7624-7629
    • Jackowski, S.1    Murphy, C.M.2    Cronan, J.E.3    Rock, C.O.4
  • 309
    • 0037051944 scopus 로고    scopus 로고
    • The YbgC protein encoded by the ybgC gene of the tol-pal gene cluster of Haemophilus influenzae catalyzes acyl-coenzyme A thioester hydrolysis
    • Zhuang Z, Song F, Martin BM, Dunaway-Mariano D. 2002. The YbgC protein encoded by the ybgC gene of the tol-pal gene cluster of Haemophilus influenzae catalyzes acyl-coenzyme A thioester hydrolysis. FEBS Lett 516:161-163.
    • (2002) FEBS Lett , vol.516 , pp. 161-163
    • Zhuang, Z.1    Song, F.2    Martin, B.M.3    Dunaway-Mariano, D.4
  • 311
    • 33746284201 scopus 로고    scopus 로고
    • Toxoplasma gondii scavenges host-derived lipoic acid despite its de novo synthesis in the apicoplast
    • Crawford MJ, Thomsen-Zieger N, Ray M, Schachtner J, Roos DS, Seeber F. 2006. Toxoplasma gondii scavenges host-derived lipoic acid despite its de novo synthesis in the apicoplast. EMBO J 25:3214-3222.
    • (2006) EMBO J , vol.25 , pp. 3214-3222
    • Crawford, M.J.1    Thomsen-Zieger, N.2    Ray, M.3    Schachtner, J.4    Roos, D.S.5    Seeber, F.6
  • 312
    • 23844532238 scopus 로고    scopus 로고
    • The plant-type ferredoxin-NADP+ reductase/ferredoxin redox system as a possible drug target against apicomplexan human parasites
    • Seeber F, Aliverti A, Zanetti G. 2005. The plant-type ferredoxin-NADP+ reductase/ferredoxin redox system as a possible drug target against apicomplexan human parasites. Curr Pharm Des 11:3159-3172.
    • (2005) Curr Pharm Des , vol.11 , pp. 3159-3172
    • Seeber, F.1    Aliverti, A.2    Zanetti, G.3
  • 313
    • 0038304827 scopus 로고    scopus 로고
    • Apicomplexan parasites contain a single lipoic acid synthase located in the plastid
    • Thomsen-Zieger N, Schachtner J, Seeber F. 2003. Apicomplexan parasites contain a single lipoic acid synthase located in the plastid. FEBS Lett 547:80-86.
    • (2003) FEBS Lett , vol.547 , pp. 80-86
    • Thomsen-Zieger, N.1    Schachtner, J.2    Seeber, F.3
  • 315
    • 0037160079 scopus 로고    scopus 로고
    • A new mechanism for anaerobic unsaturated fatty acid formation in Streptococcus pneumoniae
    • Marrakchi H, Choi KH, Rock CO. 2002. A new mechanism for anaerobic unsaturated fatty acid formation in Streptococcus pneumoniae. J Biol Chem 277:44809-44816.
    • (2002) J Biol Chem , vol.277 , pp. 44809-44816
    • Marrakchi, H.1    Choi, K.H.2    Rock, C.O.3
  • 316
    • 35448940589 scopus 로고    scopus 로고
    • A Pseudomonas aeruginosa transcription factor that senses fatty acid structure
    • Zhang YM, Zhu K, Frank MW, Rock CO. 2007. A Pseudomonas aeruginosa transcription factor that senses fatty acid structure. Mol Microbiol 66:622-632.
    • (2007) Mol Microbiol , vol.66 , pp. 622-632
    • Zhang, Y.M.1    Zhu, K.2    Frank, M.W.3    Rock, C.O.4
  • 317
    • 38349161956 scopus 로고    scopus 로고
    • Vibrio cholerae FabV defines a new class of enoyl-acyl carrier protein reductase
    • Massengo-Tiasse RP, Cronan JE. 2008. Vibrio cholerae FabV defines a new class of enoyl-acyl carrier protein reductase. J Biol Chem 283:1308-1316.
    • (2008) J Biol Chem , vol.283 , pp. 1308-1316
    • Massengo-Tiasse, R.P.1    Cronan, J.E.2
  • 318
    • 12344300344 scopus 로고    scopus 로고
    • The reductase steps of the type II fatty acid synthase as antimicrobial targets
    • Zhang YM, Lu YJ, Rock CO. 2004. The reductase steps of the type II fatty acid synthase as antimicrobial targets. Lipids 39:1055-1060.
    • (2004) Lipids , vol.39 , pp. 1055-1060
    • Zhang, Y.M.1    Lu, Y.J.2    Rock, C.O.3
  • 319
    • 0034644010 scopus 로고    scopus 로고
    • A triclosan-resistant bacterial enzyme
    • Heath RJ, Rock CO. 2000. A triclosan-resistant bacterial enzyme. Nature 406:145-146.
    • (2000) Nature , vol.406 , pp. 145-146
    • Heath, R.J.1    Rock, C.O.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.