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Volumn 35, Issue 3, 2011, Pages 475-497

Fatty acid biosynthesis in actinomycetes

Author keywords

Acyl CoA carboxylase; Corynebacterium; Lipid biosynthesis; Lipid homeostasis; Mycobacterium; Streptomyces

Indexed keywords

ACCD5 PROTEIN; ACYL COENZYME A CARBOXYLASE; ACYL COENZYME A CARBOXYLASE INHIBITOR; ANDRIMID; ANTIBIOTIC AGENT; ANTIMYCOBACTERIAL AGENT; BACTERIAL PROTEIN; BIOTIN; BIOTIN CARBOXYLASE; CARBOXYLASE; ENZYME INHIBITOR; FATTY ACID; FATTY ACID SYNTHASE; FATTY ACID SYNTHASE 1; FATTY ACID SYNTHASE 2; HERBICIDE; LIPID; MALONYL COENZYME A; MOIRAMIDE B; NCI 172033; NCI 65828; PCCB PROTEIN; PHOSPHOLIPID; PROTEIN FABD; PROTEIN FABH; TUBERCULOSTATIC AGENT; UNCLASSIFIED DRUG;

EID: 79953306224     PISSN: 01686445     EISSN: 15746976     Source Type: Journal    
DOI: 10.1111/j.1574-6976.2010.00259.x     Document Type: Review
Times cited : (140)

References (156)
  • 1
    • 0014552288 scopus 로고
    • Acetyl CoA carboxylase, II. Demonstration of biotin-protein and biotin carboxylase subunits
    • Alberts AW, Nervi AM & Vagelos PR (1969) Acetyl CoA carboxylase, II. Demonstration of biotin-protein and biotin carboxylase subunits. P Natl Acad Sci USA 63: 1319-1326.
    • (1969) P Natl Acad Sci USA , vol.63 , pp. 1319-1326
    • Alberts, A.W.1    Nervi, A.M.2    Vagelos, P.R.3
  • 2
    • 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
  • 3
    • 0141676629 scopus 로고    scopus 로고
    • The process of structure-based drug design
    • Anderson AC (2003) The process of structure-based drug design. Chem Biol 10: 787-797.
    • (2003) Chem Biol , vol.10 , pp. 787-797
    • Anderson, A.C.1
  • 5
    • 77957224172 scopus 로고    scopus 로고
    • FasR, a novel class of transcriptional regulator, governs the activation of fatty acid biosynthesis genes in Streptomyces coelicolor
    • Arabolaza A, D'Angelo M, Comba S & Gramajo H (2010a) FasR, a novel class of transcriptional regulator, governs the activation of fatty acid biosynthesis genes in Streptomyces coelicolor. Mol Microbiol 78: 47-63.
    • (2010) Mol Microbiol , vol.78 , pp. 47-63
    • Arabolaza, A.1    D'Angelo, M.2    Comba, S.3    Gramajo, H.4
  • 7
    • 61449089528 scopus 로고    scopus 로고
    • Phthiocerol dimycocerosates of M. tuberculosis participate in macrophage invasion by inducing changes in the organization of plasma membrane lipids
    • Astarie-Dequeker C, Le Guyader L, Malaga W, Seaphanh FK, Chalut C, Lopez A & Guilhot C (2009) Phthiocerol dimycocerosates of M. tuberculosis participate in macrophage invasion by inducing changes in the organization of plasma membrane lipids. PLoS Pathog 5: e1000289.
    • (2009) PLoS Pathog , vol.5
    • Astarie-Dequeker, C.1    Le Guyader, L.2    Malaga, W.3    Seaphanh, F.K.4    Chalut, C.5    Lopez, A.6    Guilhot, C.7
  • 8
    • 0029646091 scopus 로고
    • Structure of the biotinyl domain of acetyl-coenzyme A carboxylase determined by MAD phasing
    • Athappilly FK & Hendrickson WA (1995) Structure of the biotinyl domain of acetyl-coenzyme A carboxylase determined by MAD phasing. Structure 3: 1407-1419.
    • (1995) Structure , vol.3 , pp. 1407-1419
    • Athappilly, F.K.1    Hendrickson, W.A.2
  • 11
    • 27744492218 scopus 로고    scopus 로고
    • Conditional depletion of KasA, a key enzyme of mycolic acid biosynthesis, leads to mycobacterial cell lysis
    • Bhatt A, Kremer L, Dai AZ, Sacchettini JC & Jacobs WR Jr (2005) Conditional depletion of KasA, a key enzyme of mycolic acid biosynthesis, leads to mycobacterial cell lysis. J Bacteriol 187: 7596-7606.
    • (2005) J Bacteriol , vol.187 , pp. 7596-7606
    • Bhatt, A.1    Kremer, L.2    Dai, A.Z.3    Sacchettini, J.C.4    Jacobs Jr, W.R.5
  • 12
    • 34247572374 scopus 로고    scopus 로고
    • Deletion of kasB in Mycobacterium tuberculosis causes loss of acid-fastness and subclinical latent tuberculosis in immunocompetent mice
    • Bhatt A, Fujiwara N, Bhatt K et al. (2007) Deletion of kasB in Mycobacterium tuberculosis causes loss of acid-fastness and subclinical latent tuberculosis in immunocompetent mice. P Natl Acad Sci USA 104: 5157-5162.
    • (2007) P Natl Acad Sci USA , vol.104 , pp. 5157-5162
    • Bhatt, A.1    Fujiwara, N.2    Bhatt, K.3
  • 13
    • 32344447009 scopus 로고    scopus 로고
    • The structure of the carboxyltransferase component of acetyl-coA carboxylase reveals a zinc-binding motif unique to the bacterial enzyme
    • Bilder P, Lightle S, Bainbridge G et al. (2006) The structure of the carboxyltransferase component of acetyl-coA carboxylase reveals a zinc-binding motif unique to the bacterial enzyme. Biochemistry 45: 1712-1722.
    • (2006) Biochemistry , vol.45 , pp. 1712-1722
    • Bilder, P.1    Lightle, S.2    Bainbridge, G.3
  • 14
    • 0032563087 scopus 로고    scopus 로고
    • Overexpression and kinetic characterization of the carboxyltransferase component of acetyl-CoA carboxylase
    • Blanchard CZ & Waldrop GL (1998) Overexpression and kinetic characterization of the carboxyltransferase component of acetyl-CoA carboxylase. J Biol Chem 273: 19140-19145.
    • (1998) J Biol Chem , vol.273 , pp. 19140-19145
    • Blanchard, C.Z.1    Waldrop, G.L.2
  • 15
    • 0033590108 scopus 로고    scopus 로고
    • Inhibition of biotin carboxylase by a reaction intermediate analog: implications for the kinetic mechanism
    • Blanchard CZ, Amspacher D, Strongin R & Waldrop GL (1999a) Inhibition of biotin carboxylase by a reaction intermediate analog: implications for the kinetic mechanism. Biochem Bioph Res Co 266: 466-471.
    • (1999) Biochem Bioph Res Co , vol.266 , pp. 466-471
    • Blanchard, C.Z.1    Amspacher, D.2    Strongin, R.3    Waldrop, G.L.4
  • 16
    • 0033527641 scopus 로고    scopus 로고
    • The biotin domain peptide from the biotin carboxyl carrier protein of Escherichia coli acetyl-CoA carboxylase causes a marked increase in the catalytic efficiency of biotin carboxylase and carboxyltransferase relative to free biotin
    • Blanchard CZ, Chapman-Smith A, Wallace JC & Waldrop GL (1999b) The biotin domain peptide from the biotin carboxyl carrier protein of Escherichia coli acetyl-CoA carboxylase causes a marked increase in the catalytic efficiency of biotin carboxylase and carboxyltransferase relative to free biotin. J Biol Chem 274: 31767-31769.
    • (1999) J Biol Chem , vol.274 , pp. 31767-31769
    • Blanchard, C.Z.1    Chapman-Smith, A.2    Wallace, J.C.3    Waldrop, G.L.4
  • 17
    • 0017354918 scopus 로고
    • Control mechanisms in the synthesis of saturated fatty acids
    • Bloch K & Vance D (1977) Control mechanisms in the synthesis of saturated fatty acids. Annu Rev Biochem 46: 263-298.
    • (1977) Annu Rev Biochem , vol.46 , pp. 263-298
    • Bloch, K.1    Vance, D.2
  • 18
    • 0029913390 scopus 로고    scopus 로고
    • Propionyl-CoA carboxylase from Streptomyces coelicolor A3(2): cloning of the gene encoding the biotin-containing subunit
    • Bramwell H, Hunter IS, Coggins JR & Nimmo HG (1996) Propionyl-CoA carboxylase from Streptomyces coelicolor A3(2): cloning of the gene encoding the biotin-containing subunit. Microbiology 142: 649-655.
    • (1996) Microbiology , vol.142 , pp. 649-655
    • Bramwell, H.1    Hunter, I.S.2    Coggins, J.R.3    Nimmo, H.G.4
  • 19
    • 0037844364 scopus 로고    scopus 로고
    • Structure, function, and biogenesis of the cell wall of Mycobacterium tuberculosis
    • Brennan PJ (2003) Structure, function, and biogenesis of the cell wall of Mycobacterium tuberculosis. Tuberculosis (Edinb) 83: 91-97.
    • (2003) Tuberculosis (Edinb) , vol.83 , pp. 91-97
    • Brennan, P.J.1
  • 20
    • 25444463559 scopus 로고    scopus 로고
    • Probing the mechanism of the Mycobacterium tuberculosis beta-ketoacyl-acyl carrier protein synthase III mtFabH: factors influencing catalysis and substrate specificity
    • Brown AK, Sridharan S, Kremer L, Lindenberg S, Dover LG, Sacchettini JC & Besra GS (2005) Probing the mechanism of the Mycobacterium tuberculosis beta-ketoacyl-acyl carrier protein synthase III mtFabH: factors influencing catalysis and substrate specificity. J Biol Chem 280: 32539-32547.
    • (2005) J Biol Chem , vol.280 , pp. 32539-32547
    • Brown, A.K.1    Sridharan, S.2    Kremer, L.3    Lindenberg, S.4    Dover, L.G.5    Sacchettini, J.C.6    Besra, G.S.7
  • 21
    • 0000812428 scopus 로고    scopus 로고
    • Identification of a virulence gene cluster of Mycobacterium tuberculosis by signature-tagged transposon mutagenesis
    • Camacho LR, Ensergueix D, Perez E, Gicquel B & Guilhot C (1999) Identification of a virulence gene cluster of Mycobacterium tuberculosis by signature-tagged transposon mutagenesis. Mol Microbiol 34: 257-267.
    • (1999) Mol Microbiol , vol.34 , pp. 257-267
    • Camacho, L.R.1    Ensergueix, D.2    Perez, E.3    Gicquel, B.4    Guilhot, C.5
  • 22
    • 0002838747 scopus 로고    scopus 로고
    • The mycelial life-style of Streptomyces coelicolor A3(2) and its relatives
    • (Shapiro J & Dworkin M, eds) - Oxford University Press, Oxford.
    • Chater K & Losick R (1997) The mycelial life-style of Streptomyces coelicolor A3(2) and its relatives. Bacteria as Multicellular Organisms (Shapiro J & Dworkin M, eds), pp. 149-182. Oxford University Press, Oxford.
    • (1997) Bacteria as Multicellular Organisms , pp. 149-182
    • Chater, K.1    Losick, R.2
  • 23
    • 27944507949 scopus 로고    scopus 로고
    • ChemDB: a public database of small molecules and related chemoinformatics resources
    • Chen J, Swamidass SJ, Dou Y, Bruand J & Baldi P (2005) ChemDB: a public database of small molecules and related chemoinformatics resources. Bioinformatics 21: 4133-4139.
    • (2005) Bioinformatics , vol.21 , pp. 4133-4139
    • Chen, J.1    Swamidass, S.J.2    Dou, Y.3    Bruand, J.4    Baldi, P.5
  • 24
    • 0036299101 scopus 로고    scopus 로고
    • Crystal structure of MabA from Mycobacterium tuberculosis, a reductase involved in long-chain fatty acid biosynthesis
    • Cohen-Gonsaud M, Ducasse S, Hoh F, Zerbib D, Labesse G & Quemard A (2002) Crystal structure of MabA from Mycobacterium tuberculosis, a reductase involved in long-chain fatty acid biosynthesis. J Mol Biol 320: 249-261.
    • (2002) J Mol Biol , vol.320 , pp. 249-261
    • Cohen-Gonsaud, M.1    Ducasse, S.2    Hoh, F.3    Zerbib, D.4    Labesse, G.5    Quemard, A.6
  • 25
    • 0032508046 scopus 로고    scopus 로고
    • Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence
    • Cole ST, Brosch R, Parkhill J et al. (1998) Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence. Nature 393: 537-544.
    • (1998) Nature , vol.393 , pp. 537-544
    • Cole, S.T.1    Brosch, R.2    Parkhill, J.3
  • 26
    • 0020463232 scopus 로고
    • Fatty acid composition of some mycolic acid-containing coryneform bacteria
    • Collins MD, Goodfellow M & Minnikin DE (1982) Fatty acid composition of some mycolic acid-containing coryneform bacteria. J Gen Microbiol 128: 2503-2509.
    • (1982) J Gen Microbiol , vol.128 , pp. 2503-2509
    • Collins, M.D.1    Goodfellow, M.2    Minnikin, D.E.3
  • 27
    • 0033523971 scopus 로고    scopus 로고
    • Complex lipid determines tissue-specific replication of Mycobacterium tuberculosis in mice
    • Cox JS, Chen B, McNeil M & Jacobs WR Jr (1999) Complex lipid determines tissue-specific replication of Mycobacterium tuberculosis in mice. Nature 402: 79-83.
    • (1999) Nature , vol.402 , pp. 79-83
    • Cox, J.S.1    Chen, B.2    McNeil, M.3    Jacobs Jr, W.R.4
  • 28
    • 0035813096 scopus 로고    scopus 로고
    • The biotinyl domain of Escherichia coli acetyl-CoA carboxylase. Evidence that the 'thumb' structure id 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 id 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 Jr, J.E.1
  • 30
    • 0001517649 scopus 로고    scopus 로고
    • Biosynthesis of membrane lipids
    • Böck A, Curtiss R III, Kaper J, Karp P, Neidhardt F, Nyström T, Slauch J, Squires C & Ussery D, eds), Chapter 3.6.4. ASM Press, Washington, DC.
    • Cronan JE & Rock CO (2008) Biosynthesis of membrane lipids. EcoSal, Escherichia coli and Salmonella: Cellular and Molecular Biology (Böck A, Curtiss R III, Kaper J, Karp P, Neidhardt F, Nyström T, Slauch J, Squires C & Ussery D, eds), Chapter 3.6.4. ASM Press, Washington, DC.
    • (2008) EcoSal, Escherichia coli and Salmonella: Cellular and Molecular Biology
    • Cronan, J.E.1    Rock, C.O.2
  • 31
    • 0031815062 scopus 로고    scopus 로고
    • FadR, transcriptional co-ordination of metabolic expediency
    • Cronan JE Jr & Subrahmanyam S (1998) FadR, transcriptional co-ordination of metabolic expediency. Mol Microbiol 29: 937-943.
    • (1998) Mol Microbiol , vol.29 , pp. 937-943
    • Cronan Jr, J.E.1    Subrahmanyam, S.2
  • 32
    • 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 Jr, J.E.1    Waldrop, G.L.2
  • 33
    • 0032452982 scopus 로고    scopus 로고
    • The envelope layers of mycobacteria with reference to their pathogenicity
    • Daffe M & Draper P (1998) The envelope layers of mycobacteria with reference to their pathogenicity. Adv Microb Physiol 39: 131-203.
    • (1998) Adv Microb Physiol , vol.39 , pp. 131-203
    • Daffe, M.1    Draper, P.2
  • 34
    • 68949182472 scopus 로고    scopus 로고
    • The global architecture of the mycobacteria cell envelope
    • Daffe M & Reyrat JM, eds) - ASM Press, Washington, DC.
    • Daffe M (2008) The global architecture of the mycobacteria cell envelope. The Mycobacterial Cell Envelope (Daffe M & Reyrat JM, eds), pp. 3-12. ASM Press, Washington, DC.
    • (2008) The Mycobacterial Cell Envelope , pp. 3-12
    • Daffe, M.1
  • 35
    • 3242750587 scopus 로고    scopus 로고
    • Induction of a novel class of diacylglycerol acyltransferases and triacylglycerol accumulation in Mycobacterium tuberculosis as it goes into a dormancy-like state in culture
    • Daniel J, Deb C, Dubey VS, Sirakova TD, Abomoelak B, Morbidoni HR & Kolattukudy PE (2004) Induction of a novel class of diacylglycerol acyltransferases and triacylglycerol accumulation in Mycobacterium tuberculosis as it goes into a dormancy-like state in culture. J Bacteriol 186: 5017-5030.
    • (2004) J Bacteriol , vol.186 , pp. 5017-5030
    • Daniel, J.1    Deb, C.2    Dubey, V.S.3    Sirakova, T.D.4    Abomoelak, B.5    Morbidoni, H.R.6    Kolattukudy, P.E.7
  • 36
    • 33846632320 scopus 로고    scopus 로고
    • AccD6, a member of the Fas II locus, is a functional carboxyltransferase subunit of the acyl-coenzyme A carboxylase in Mycobacterium tuberculosis
    • Daniel J, Oh TJ, Lee CM & Kolattukudy PE (2007) AccD6, a member of the Fas II locus, is a functional carboxyltransferase subunit of the acyl-coenzyme A carboxylase in Mycobacterium tuberculosis. J Bacteriol 189: 911-917.
    • (2007) J Bacteriol , vol.189 , pp. 911-917
    • Daniel, J.1    Oh, T.J.2    Lee, C.M.3    Kolattukudy, P.E.4
  • 37
    • 0022578265 scopus 로고
    • Structure, biosynthesis, and physicochemical properties of archaebacterial lipids
    • De Rosa M, Gambacorta A & Gliozzi A (1986) Structure, biosynthesis, and physicochemical properties of archaebacterial lipids. Microbiol Rev 50: 70-80.
    • (1986) Microbiol Rev , vol.50 , pp. 70-80
    • De Rosa, M.1    Gambacorta, A.2    Gliozzi, A.3
  • 38
    • 0037163047 scopus 로고    scopus 로고
    • Kinetic and structural analysis of a new group of acyl-CoA carboxylases found in Streptomyces coelicolor A3(2)
    • Diacovich L, Peiru S, Kurth D, Rodriguez E, Podesta F, Khosla C & Gramajo H (2002) Kinetic and structural analysis of a new group of acyl-CoA carboxylases found in Streptomyces coelicolor A3(2). J Biol Chem 277: 31228-31236.
    • (2002) J Biol Chem , vol.277 , pp. 31228-31236
    • Diacovich, L.1    Peiru, S.2    Kurth, D.3    Rodriguez, E.4    Podesta, F.5    Khosla, C.6    Gramajo, H.7
  • 39
    • 8344220571 scopus 로고    scopus 로고
    • Crystal structure of the beta-subunit of acyl-CoA carboxylase: structure-based engineering of substrate specificity
    • Diacovich L, Mitchell DL, Pham H, Gago G, Melgar MM, Khosla C, Gramajo H & Tsai SC (2004) Crystal structure of the beta-subunit of acyl-CoA carboxylase: structure-based engineering of substrate specificity. Biochemistry 43: 14027-14036.
    • (2004) Biochemistry , vol.43 , pp. 14027-14036
    • Diacovich, L.1    Mitchell, D.L.2    Pham, H.3    Gago, G.4    Melgar, M.M.5    Khosla, C.6    Gramajo, H.7    Tsai, S.C.8
  • 40
    • 0031983015 scopus 로고    scopus 로고
    • The fats of Escherichia coli during infancy and old age: regulation by global regulators, alarmones and lipid intermediates
    • DiRusso CC & Nystrom T (1998) The fats of Escherichia coli during infancy and old age: regulation by global regulators, alarmones and lipid intermediates. Mol Microbiol 27: 1-8.
    • (1998) Mol Microbiol , vol.27 , pp. 1-8
    • DiRusso, C.C.1    Nystrom, T.2
  • 41
    • 0015864097 scopus 로고
    • Acetyl-CoA and propionyl-CoA carboxylation by Mycobacterium phlei. Partial purification and some properties of the enzyme
    • Erfle JD (1973) Acetyl-CoA and propionyl-CoA carboxylation by Mycobacterium phlei. Partial purification and some properties of the enzyme. Biochim Biophys Acta 316: 143-155.
    • (1973) Biochim Biophys Acta , vol.316 , pp. 143-155
    • Erfle, J.D.1
  • 42
    • 0037143585 scopus 로고    scopus 로고
    • Enzymes involved in fatty acid and polyketide biosynthesis in Streptomyces glaucescens: role of FabH and FabD and their acyl carrier protein specificity
    • Florova G, Kazanina G & Reynolds KA (2002) Enzymes involved in fatty acid and polyketide biosynthesis in Streptomyces glaucescens: role of FabH and FabD and their acyl carrier protein specificity. Biochemistry 41: 10462-10471.
    • (2002) Biochemistry , vol.41 , pp. 10462-10471
    • Florova, G.1    Kazanina, G.2    Reynolds, K.A.3
  • 43
    • 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
  • 44
    • 30744470169 scopus 로고    scopus 로고
    • Biochemical and structural characterization of an essential acyl coenzyme A carboxylase from Mycobacterium tuberculosis
    • Gago G, Kurth D, Diacovich L, Tsai SC & Gramajo H (2006) Biochemical and structural characterization of an essential acyl coenzyme A carboxylase from Mycobacterium tuberculosis. J Bacteriol 188: 477-486.
    • (2006) J Bacteriol , vol.188 , pp. 477-486
    • Gago, G.1    Kurth, D.2    Diacovich, L.3    Tsai, S.C.4    Gramajo, H.5
  • 45
    • 7244242397 scopus 로고    scopus 로고
    • Acyl-CoA carboxylases (accD2 and accD3), together with a unique polyketide synthase (Cg-pks), are key to mycolic acid biosynthesis in Corynebacterianeae such as Corynebacterium glutamicum and Mycobacterium tuberculosis
    • Gande R, Gibson KJ, Brown AK, Krumbach K, Dover LG, Sahm H, Shioyama S, Oikawa T, Besra GS & Eggeling L (2004) Acyl-CoA carboxylases (accD2 and accD3), together with a unique polyketide synthase (Cg-pks), are key to mycolic acid biosynthesis in Corynebacterianeae such as Corynebacterium glutamicum and Mycobacterium tuberculosis. J Biol Chem 279: 44847-44857.
    • (2004) J Biol Chem , vol.279 , pp. 44847-44857
    • Gande, R.1    Gibson, K.J.2    Brown, A.K.3    Krumbach, K.4    Dover, L.G.5    Sahm, H.6    Shioyama, S.7    Oikawa, T.8    Besra, G.S.9    Eggeling, L.10
  • 46
    • 34447529329 scopus 로고    scopus 로고
    • The two carboxylases of Corynebacterium glutamicum essential for fatty acid and mycolic acid synthesis
    • Gande R, Dover LG, Krumbach K, Besra GS, Sahm H, Oikawa T & Eggeling L (2007) The two carboxylases of Corynebacterium glutamicum essential for fatty acid and mycolic acid synthesis. J Bacteriol 189: 5257-5264.
    • (2007) J Bacteriol , vol.189 , pp. 5257-5264
    • Gande, R.1    Dover, L.G.2    Krumbach, K.3    Besra, G.S.4    Sahm, H.5    Oikawa, T.6    Eggeling, L.7
  • 47
    • 0141677776 scopus 로고    scopus 로고
    • Requirement for kasB in Mycobacterium mycolic acid biosynthesis, cell wall impermeability and intracellular survival: implications for therapy
    • Gao LY, Laval F, Lawson EH, Groger RK, Woodruff A, Morisaki JH, Cox JS, Daffe M & Brown EJ (2003) Requirement for kasB in Mycobacterium mycolic acid biosynthesis, cell wall impermeability and intracellular survival: implications for therapy. Mol Microbiol 49: 1547-1563.
    • (2003) Mol Microbiol , vol.49 , pp. 1547-1563
    • Gao, L.Y.1    Laval, F.2    Lawson, E.H.3    Groger, R.K.4    Woodruff, A.5    Morisaki, J.H.6    Cox, J.S.7    Daffe, M.8    Brown, E.J.9
  • 48
    • 34249070268 scopus 로고    scopus 로고
    • The key role of the mycolic acid content in the functionality of the cell wall permeability barrier in Corynebacterineae
    • Gebhardt H, Meniche X, Tropis M, Kramer R, Daffe M & Morbach S (2007) The key role of the mycolic acid content in the functionality of the cell wall permeability barrier in Corynebacterineae. Microbiology 153: 1424-1434.
    • (2007) Microbiology , vol.153 , pp. 1424-1434
    • Gebhardt, H.1    Meniche, X.2    Tropis, M.3    Kramer, R.4    Daffe, M.5    Morbach, S.6
  • 49
    • 36549060587 scopus 로고    scopus 로고
    • Versatility of polyketide synthases in generating metabolic diversity
    • Gokhale RS, Sankaranarayanan R & Mohanty D (2007a) Versatility of polyketide synthases in generating metabolic diversity. Curr Opin Struc Biol 17: 736-743.
    • (2007) Curr Opin Struc Biol , vol.17 , pp. 736-743
    • Gokhale, R.S.1    Sankaranarayanan, R.2    Mohanty, D.3
  • 50
    • 33947662068 scopus 로고    scopus 로고
    • Versatile polyketide enzymatic machinery for the biosynthesis of complex mycobacterial lipids
    • Gokhale RS, Saxena P, Chopra T & Mohanty D (2007b) Versatile polyketide enzymatic machinery for the biosynthesis of complex mycobacterial lipids. Nat Prod Rep 24: 267-277.
    • (2007) Nat Prod Rep , vol.24 , pp. 267-277
    • Gokhale, R.S.1    Saxena, P.2    Chopra, T.3    Mohanty, D.4
  • 51
    • 0014670912 scopus 로고
    • Acyl carrier protein. 13. Beta-ketoacyl acyl carrier protein synthetase from Escherichia coli
    • Greenspan MD, Alberts AW & Vagelos PR (1969) Acyl carrier protein. 13. Beta-ketoacyl acyl carrier protein synthetase from Escherichia coli. J Biol Chem 244: 6477-6485.
    • (1969) J Biol Chem , vol.244 , pp. 6477-6485
    • Greenspan, M.D.1    Alberts, A.W.2    Vagelos, P.R.3
  • 52
    • 0027955944 scopus 로고
    • Herbicides inhibiting acetyl-CoA carboxylase
    • Gronwald JW (1994) Herbicides inhibiting acetyl-CoA carboxylase. Biochem Soc T 22: 616-621.
    • (1994) Biochem Soc T , vol.22 , pp. 616-621
    • Gronwald, J.W.1
  • 53
    • 0020442441 scopus 로고
    • The subunit structure and function of the propionyl coenzyme A carboxylase of Mycobacterium smegmatis
    • Haase FC, Henrikson KP, Treble DH & Allen SH (1982) The subunit structure and function of the propionyl coenzyme A carboxylase of Mycobacterium smegmatis. J Biol Chem 257: 11994-11999.
    • (1982) J Biol Chem , vol.257 , pp. 11994-11999
    • Haase, F.C.1    Henrikson, K.P.2    Treble, D.H.3    Allen, S.H.4
  • 54
    • 0038581162 scopus 로고    scopus 로고
    • Transcarboxylase 12S crystal structure: hexamer assembly and substrate binding to a multienzyme core
    • Hall PR, Wang YF, Rivera-Hainaj RE, Zheng X, Pustai-Carey M, Carey PR & Yee VC (2003) Transcarboxylase 12S crystal structure: hexamer assembly and substrate binding to a multienzyme core. EMBO J 22: 2334-2347.
    • (2003) EMBO J , vol.22 , pp. 2334-2347
    • Hall, P.R.1    Wang, Y.F.2    Rivera-Hainaj, R.E.3    Zheng, X.4    Pustai-Carey, M.5    Carey, P.R.6    Yee, V.C.7
  • 55
    • 0031751326 scopus 로고    scopus 로고
    • Characterization of beta-ketoacyl-acyl carrier protein synthase III from Streptomyces glaucescens and its role in initiation of fatty acid biosynthesis
    • Han L, Lobo S & Reynolds KA (1998) Characterization of beta-ketoacyl-acyl carrier protein synthase III from Streptomyces glaucescens and its role in initiation of fatty acid biosynthesis. J Bacteriol 180: 4481-4486.
    • (1998) J Bacteriol , vol.180 , pp. 4481-4486
    • Han, L.1    Lobo, S.2    Reynolds, K.A.3
  • 56
    • 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
  • 57
    • 0018786920 scopus 로고
    • Purification and subunit structure of propionyl coenzyme A carboxylase of Mycobacterium smegmatis
    • Henrikson KP & Allen SH (1979) Purification and subunit structure of propionyl coenzyme A carboxylase of Mycobacterium smegmatis. J Biol Chem 254: 5888-5891.
    • (1979) J Biol Chem , vol.254 , pp. 5888-5891
    • Henrikson, K.P.1    Allen, S.H.2
  • 58
    • 69249202590 scopus 로고    scopus 로고
    • The biosynthetic logic of polyketide diversity
    • Hertweck C (2009) The biosynthetic logic of polyketide diversity. Angew Chem Int Edit 48: 4688-4716.
    • (2009) Angew Chem Int Edit , vol.48 , pp. 4688-4716
    • Hertweck, C.1
  • 59
    • 0035113799 scopus 로고    scopus 로고
    • The crotonase superfamily: divergently related enzymes that catalyze different reactions involving acyl coenzyme a thioesters
    • Holden HM, Benning MM, Haller T & Gerlt JA (2001) The crotonase superfamily: divergently related enzymes that catalyze different reactions involving acyl coenzyme a thioesters. Accounts Chem Res 34: 145-157.
    • (2001) Accounts Chem Res , vol.34 , pp. 145-157
    • Holden, H.M.1    Benning, M.M.2    Haller, T.3    Gerlt, J.A.4
  • 60
    • 0024982049 scopus 로고
    • Antibiotics: opportunities for genetic manipulation
    • Hopwood DA (1989) Antibiotics: opportunities for genetic manipulation. Philos T Roy Soc B 324: 549-562.
    • (1989) Philos T Roy Soc B , vol.324 , pp. 549-562
    • Hopwood, D.A.1
  • 61
    • 31044455479 scopus 로고    scopus 로고
    • Purification and characterization of the Mycobacterium tuberculosis FabD2, a novel malonyl-CoA: AcpM transacylase of fatty acid synthase
    • Huang YS, Ge J, Zhang HM, Lei JQ, Zhang XL & Wang HH (2006) Purification and characterization of the Mycobacterium tuberculosis FabD2, a novel malonyl-CoA: AcpM transacylase of fatty acid synthase. Protein Expres Purif 45: 393-399.
    • (2006) Protein Expres Purif , vol.45 , pp. 393-399
    • Huang, Y.S.1    Ge, J.2    Zhang, H.M.3    Lei, J.Q.4    Zhang, X.L.5    Wang, H.H.6
  • 62
    • 0020352076 scopus 로고
    • Isolation and characterization of an acyl-coenzyme A carboxylase from an erythromycin-producing Streptomyces erythreus
    • Hunaiti AR & Kolattukudy PE (1982) Isolation and characterization of an acyl-coenzyme A carboxylase from an erythromycin-producing Streptomyces erythreus. Arch Biochem Biophys 216: 362-371.
    • (1982) Arch Biochem Biophys , vol.216 , pp. 362-371
    • Hunaiti, A.R.1    Kolattukudy, P.E.2
  • 63
    • 0035839589 scopus 로고    scopus 로고
    • Function of Escherichia coli biotin carboxylase requires catalytic activity of both subunits of the homodimer
    • Janiyani K, Bordelon T, Waldrop GL & Cronan JE Jr (2001) Function of Escherichia coli biotin carboxylase requires catalytic activity of both subunits of the homodimer. J Biol Chem 276: 29864-29870.
    • (2001) J Biol Chem , vol.276 , pp. 29864-29870
    • Janiyani, K.1    Bordelon, T.2    Waldrop, G.L.3    Cronan Jr, J.E.4
  • 64
    • 12444259324 scopus 로고    scopus 로고
    • The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its impact on the production of l-aspartate-derived amino acids and vitamins
    • Kalinowski J, Bathe B, Bartels D et al. (2003) The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its impact on the production of l-aspartate-derived amino acids and vitamins. J Biotechnol 104: 5-25.
    • (2003) J Biotechnol , vol.104 , pp. 5-25
    • Kalinowski, J.1    Bathe, B.2    Bartels, D.3
  • 65
    • 0025890074 scopus 로고
    • Iso- and anteiso-fatty acids in bacteria: biosynthesis, function, and taxonomic significance
    • Kaneda T (1991) Iso- and anteiso-fatty acids in bacteria: biosynthesis, function, and taxonomic significance. Microbiol Rev 55: 288-302.
    • (1991) Microbiol Rev , vol.55 , pp. 288-302
    • Kaneda, T.1
  • 66
    • 0026659794 scopus 로고
    • Purification and characterization of an unusually large fatty acid synthase from Mycobacterium tuberculosis var. bovis BCG
    • Kikuchi S, Rainwater DL & Kolattukudy PE (1992) Purification and characterization of an unusually large fatty acid synthase from Mycobacterium tuberculosis var. bovis BCG. Arch Biochem Biophys 295: 318-326.
    • (1992) Arch Biochem Biophys , vol.295 , pp. 318-326
    • Kikuchi, S.1    Rainwater, D.L.2    Kolattukudy, P.E.3
  • 67
    • 0031691012 scopus 로고    scopus 로고
    • Propionyl-CoA carboxylase of Myxococcus xanthus: catalytic properties and function in developing cells
    • Kimura Y, Kojyo T, Kimura I & Sato M (1998) Propionyl-CoA carboxylase of Myxococcus xanthus: catalytic properties and function in developing cells. Arch Microbiol 170: 179-184.
    • (1998) Arch Microbiol , vol.170 , pp. 179-184
    • Kimura, Y.1    Kojyo, T.2    Kimura, I.3    Sato, M.4
  • 68
    • 0028075219 scopus 로고
    • Systems and mechanisms of amino acid uptake and excretion in prokaryotes
    • Kramer R (1994) Systems and mechanisms of amino acid uptake and excretion in prokaryotes. Arch Microbiol 162: 1-13.
    • (1994) Arch Microbiol , vol.162 , pp. 1-13
    • Kramer, R.1
  • 69
    • 0034595879 scopus 로고    scopus 로고
    • Thiolactomycin and related analogues as novel anti-mycobacterial agents targeting KasA and KasB condensing enzymes in Mycobacterium tuberculosis
    • Kremer L, Douglas JD, Baulard AR et al. (2000) Thiolactomycin and related analogues as novel anti-mycobacterial agents targeting KasA and KasB condensing enzymes in Mycobacterium tuberculosis. J Biol Chem 275: 16857-16864.
    • (2000) J Biol Chem , vol.275 , pp. 16857-16864
    • Kremer, L.1    Douglas, J.D.2    Baulard, A.R.3
  • 70
    • 0035958944 scopus 로고    scopus 로고
    • Biochemical characterization of acyl carrier protein (AcpM) and malonyl-CoA: AcpM transacylase (mtFabD), two major components of Mycobacterium tuberculosis fatty acid synthase II
    • Kremer L, Nampoothiri KM, Lesjean S, Dover LG, Graham S, Betts J, Brennan PJ, Minnikin DE, Locht C & Besra GS (2001) Biochemical characterization of acyl carrier protein (AcpM) and malonyl-CoA: AcpM transacylase (mtFabD), two major components of Mycobacterium tuberculosis fatty acid synthase II. J Biol Chem 276: 27967-27974.
    • (2001) J Biol Chem , vol.276 , pp. 27967-27974
    • Kremer, L.1    Nampoothiri, K.M.2    Lesjean, S.3    Dover, L.G.4    Graham, S.5    Betts, J.6    Brennan, P.J.7    Minnikin, D.E.8    Locht, C.9    Besra, G.S.10
  • 73
    • 4544282847 scopus 로고
    • The biochemical function of biotin, VI. Chemical structure of the carboxylated active site of propionyl carboxylase
    • Lane MD & Lynen F (1963) The biochemical function of biotin, VI. Chemical structure of the carboxylated active site of propionyl carboxylase. P Natl Acad Sci USA 49: 379-385.
    • (1963) P Natl Acad Sci USA , vol.49 , pp. 379-385
    • Lane, M.D.1    Lynen, F.2
  • 75
    • 0036296417 scopus 로고    scopus 로고
    • A bisubstrate analog inhibitor of the carboxyltransferase component of acetyl-CoA carboxylase
    • Levert KL & Waldrop GL (2002) A bisubstrate analog inhibitor of the carboxyltransferase component of acetyl-CoA carboxylase. Biochem Bioph Res Co 291: 1213-1217.
    • (2002) Biochem Bioph Res Co , vol.291 , pp. 1213-1217
    • Levert, K.L.1    Waldrop, G.L.2
  • 76
    • 0034636083 scopus 로고    scopus 로고
    • Do cysteine 230 and lysine 238 of biotin carboxylase play a role in the activation of biotin?
    • Levert KL, Lloyd RB & Waldrop GL (2000) Do cysteine 230 and lysine 238 of biotin carboxylase play a role in the activation of biotin? Biochemistry 39: 4122-4128.
    • (2000) Biochemistry , vol.39 , pp. 4122-4128
    • Levert, K.L.1    Lloyd, R.B.2    Waldrop, G.L.3
  • 77
    • 18944390942 scopus 로고    scopus 로고
    • Alteration of the fatty acid profile of Streptomyces coelicolor by replacement of the initiation enzyme 3-ketoacyl acyl carrier protein synthase III (FabH)
    • Li Y, Florova G & Reynolds KA (2005) Alteration of the fatty acid profile of Streptomyces coelicolor by replacement of the initiation enzyme 3-ketoacyl acyl carrier protein synthase III (FabH). J Bacteriol 187: 3795-3799.
    • (2005) J Bacteriol , vol.187 , pp. 3795-3799
    • Li, Y.1    Florova, G.2    Reynolds, K.A.3
  • 79
    • 0029862802 scopus 로고    scopus 로고
    • Mycolic acid structure determines the fluidity of the mycobacterial cell wall
    • Liu J, Barry CE III, Besra GS & Nikaido H (1996) Mycolic acid structure determines the fluidity of the mycobacterial cell wall. J Biol Chem 271: 29545-29551.
    • (1996) J Biol Chem , vol.271 , pp. 29545-29551
    • Liu, J.1    Barry III, C.E.2    Besra, G.S.3    Nikaido, H.4
  • 80
    • 33645051218 scopus 로고    scopus 로고
    • Transcriptional regulation of fatty acid biosynthesis in Streptococcus pneumoniae
    • Lu YJ & Rock CO (2006) Transcriptional regulation of fatty acid biosynthesis in Streptococcus pneumoniae. Mol Microbiol 59: 551-566.
    • (2006) Mol Microbiol , vol.59 , pp. 551-566
    • Lu, Y.J.1    Rock, C.O.2
  • 81
    • 0018556771 scopus 로고
    • New experiments of biotin enzymes
    • Lynen F (1979) New experiments of biotin enzymes. CRC Crit Rev Biochem 7: 103-119.
    • (1979) CRC Crit Rev Biochem , vol.7 , pp. 103-119
    • Lynen, F.1
  • 82
    • 0019164234 scopus 로고
    • On the structure of fatty acid synthetase of yeast
    • Lynen F (1980) On the structure of fatty acid synthetase of yeast. Eur J Biochem 112: 431-442.
    • (1980) Eur J Biochem , vol.112 , pp. 431-442
    • Lynen, F.1
  • 84
    • 34247145507 scopus 로고    scopus 로고
    • Organization and function of the YsiA regulon of Bacillus subtilis involved in fatty acid degradation
    • Matsuoka H, Hirooka K & Fujita Y (2007) Organization and function of the YsiA regulon of Bacillus subtilis involved in fatty acid degradation. J Biol Chem 282: 5180-5194.
    • (2007) J Biol Chem , vol.282 , pp. 5180-5194
    • Matsuoka, H.1    Hirooka, K.2    Fujita, Y.3
  • 85
    • 0019099305 scopus 로고
    • Lipid composition in the classification and identification of acid-fast bacteria
    • Minnikin DE & Goodfellow M (1980) Lipid composition in the classification and identification of acid-fast bacteria. Soc Appl Bacteriol Symp Ser 8: 189-256.
    • (1980) Soc Appl Bacteriol Symp Ser , vol.8 , pp. 189-256
    • Minnikin, D.E.1    Goodfellow, M.2
  • 86
    • 0036015838 scopus 로고    scopus 로고
    • The methyl-branched fortifications of Mycobacterium tuberculosis
    • Minnikin DE, Kremer L, Dover LG & Besra GS (2002) The methyl-branched fortifications of Mycobacterium tuberculosis. Chem Biol 9: 545-553.
    • (2002) Chem Biol , vol.9 , pp. 545-553
    • Minnikin, D.E.1    Kremer, L.2    Dover, L.G.3    Besra, G.S.4
  • 87
    • 33749570515 scopus 로고    scopus 로고
    • The condensing activities of the Mycobacterium tuberculosis type II fatty acid synthase are differentially regulated by phosphorylation
    • Molle V, Brown AK, Besra GS, Cozzone AJ & Kremer L (2006) The condensing activities of the Mycobacterium tuberculosis type II fatty acid synthase are differentially regulated by phosphorylation. J Biol Chem 281: 30094-30103.
    • (2006) J Biol Chem , vol.281 , pp. 30094-30103
    • Molle, V.1    Brown, A.K.2    Besra, G.S.3    Cozzone, A.J.4    Kremer, L.5
  • 88
    • 0017654536 scopus 로고
    • Fatty acid synthetase activity in Mycobacterium smegmatis. Characterization of the acyl carrier protein-dependent elongating system
    • Odriozola JM, Ramos JA & Bloch K (1977) Fatty acid synthetase activity in Mycobacterium smegmatis. Characterization of the acyl carrier protein-dependent elongating system. Biochim Biophys Acta 488: 207-217.
    • (1977) Biochim Biophys Acta , vol.488 , pp. 207-217
    • Odriozola, J.M.1    Ramos, J.A.2    Bloch, K.3
  • 89
    • 33645239314 scopus 로고    scopus 로고
    • Identification and characterization of Rv3281 as a novel subunit of a biotin-dependent acyl-CoA carboxylase in Mycobacterium tuberculosis H37Rv
    • Oh TJ, Daniel J, Kim HJ, Sirakova TD & Kolattukudy PE (2006) Identification and characterization of Rv3281 as a novel subunit of a biotin-dependent acyl-CoA carboxylase in Mycobacterium tuberculosis H37Rv. J Biol Chem 281: 3899-3908.
    • (2006) J Biol Chem , vol.281 , pp. 3899-3908
    • Oh, T.J.1    Daniel, J.2    Kim, H.J.3    Sirakova, T.D.4    Kolattukudy, P.E.5
  • 92
    • 35348978364 scopus 로고    scopus 로고
    • Product-regulation mechanisms for fatty acid biosynthesis catalyzed by Mycobacterium smegmatis FAS I
    • Papaioannou N, Cheon HS, Lian Y & Kishi Y (2007) Product-regulation mechanisms for fatty acid biosynthesis catalyzed by Mycobacterium smegmatis FAS I. Chembiochem 8: 1775-1780.
    • (2007) Chembiochem , vol.8 , pp. 1775-1780
    • Papaioannou, N.1    Cheon, H.S.2    Lian, Y.3    Kishi, Y.4
  • 93
    • 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
  • 94
    • 0017385010 scopus 로고
    • Mycobacterium smegmatis fatty acid synthetase. Long chain transacylase chain length specificity
    • Peterson DO & Bloch K (1977) Mycobacterium smegmatis fatty acid synthetase. Long chain transacylase chain length specificity. J Biol Chem 252: 5735-5739.
    • (1977) J Biol Chem , vol.252 , pp. 5735-5739
    • Peterson, D.O.1    Bloch, K.2
  • 96
    • 15744389881 scopus 로고    scopus 로고
    • The acyl-AMP ligase FadD32 and AccD4-containing acyl-CoA carboxylase are required for the synthesis of mycolic acids and essential for mycobacterial growth: identification of the carboxylation product and determination of the acyl-CoA carboxylase components
    • Portevin D, Sousa-D'Auria C, Montrozier H, Houssin C, Stella A, Laneelle MA, Bardou F, Guilhot C & Daffe M (2005) The acyl-AMP ligase FadD32 and AccD4-containing acyl-CoA carboxylase are required for the synthesis of mycolic acids and essential for mycobacterial growth: identification of the carboxylation product and determination of the acyl-CoA carboxylase components. J Biol Chem 280: 8862-8874.
    • (2005) J Biol Chem , vol.280 , pp. 8862-8874
    • Portevin, D.1    Sousa-D'Auria, C.2    Montrozier, H.3    Houssin, C.4    Stella, A.5    Laneelle, M.A.6    Bardou, F.7    Guilhot, C.8    Daffe, M.9
  • 97
    • 0014010711 scopus 로고
    • Studies on the mechanism of fatty acid synthesis. 13. The role of beta-hydroxy acids in the synthesis of palmitate and cis vaccenate by the Escherichia coli enzyme system
    • Pugh EL, Sauer F, Waite M, Toomey RE & Wakil SJ (1966) Studies on the mechanism of fatty acid synthesis. 13. The role of beta-hydroxy acids in the synthesis of palmitate and cis vaccenate by the Escherichia coli enzyme system. J Biol Chem 241: 2635-2643.
    • (1966) J Biol Chem , vol.241 , pp. 2635-2643
    • Pugh, E.L.1    Sauer, F.2    Waite, M.3    Toomey, R.E.4    Wakil, S.J.5
  • 98
    • 23644436692 scopus 로고    scopus 로고
    • Crystal structure and substrate specificity of the beta-ketoacyl-acyl carrier protein synthase III (FabH) from Staphylococcus aureus
    • Qiu X, Choudhry AE, Janson CA, Grooms M, Daines RA, Lonsdale JT & Khandekar SS (2005) Crystal structure and substrate specificity of the beta-ketoacyl-acyl carrier protein synthase III (FabH) from Staphylococcus aureus. Protein Sci 14: 2087-2094.
    • (2005) Protein Sci , vol.14 , pp. 2087-2094
    • Qiu, X.1    Choudhry, A.E.2    Janson, C.A.3    Grooms, M.4    Daines, R.A.5    Lonsdale, J.T.6    Khandekar, S.S.7
  • 101
    • 0032101861 scopus 로고    scopus 로고
    • Biosynthesis of fatty acids and related metabolites
    • Rawlings BJ (1998) Biosynthesis of fatty acids and related metabolites. Nat Prod Rep 15: 275-308.
    • (1998) Nat Prod Rep , vol.15 , pp. 275-308
    • Rawlings, B.J.1
  • 102
    • 0000041171 scopus 로고    scopus 로고
    • High resolution solution structure of the 1.3S subunit of transcarboxylase from Propionibacterium shermanii
    • Reddy DV, Shenoy BC, Carey PR & Sonnichsen FD (2000) High resolution solution structure of the 1.3S subunit of transcarboxylase from Propionibacterium shermanii. Biochemistry 39: 2509-2516.
    • (2000) Biochemistry , vol.39 , pp. 2509-2516
    • Reddy, D.V.1    Shenoy, B.C.2    Carey, P.R.3    Sonnichsen, F.D.4
  • 103
    • 0029059472 scopus 로고
    • Purification of a malonyltransferase from Streptomyces coelicolor A3(2) and analysis of its genetic determinant
    • Revill WP, Bibb MJ & Hopwood DA (1995) Purification of a malonyltransferase from Streptomyces coelicolor A3(2) and analysis of its genetic determinant. J Bacteriol 177: 3946-3952.
    • (1995) J Bacteriol , vol.177 , pp. 3946-3952
    • Revill, W.P.1    Bibb, M.J.2    Hopwood, D.A.3
  • 104
    • 0029841660 scopus 로고    scopus 로고
    • Relationships between fatty acid and polyketide synthases from Streptomyces coelicolor A3(2): characterization of the fatty acid synthase acyl carrier protein
    • Revill WP, Bibb MJ & Hopwood DA (1996) Relationships between fatty acid and polyketide synthases from Streptomyces coelicolor A3(2): characterization of the fatty acid synthase acyl carrier protein. J Bacteriol 178: 5660-5667.
    • (1996) J Bacteriol , vol.178 , pp. 5660-5667
    • Revill, W.P.1    Bibb, M.J.2    Hopwood, D.A.3
  • 105
    • 0035025631 scopus 로고    scopus 로고
    • Beta-ketoacyl acyl carrier protein synthase III (FabH) is essential for fatty acid biosynthesis in Streptomyces coelicolor A3(2)
    • Revill WP, Bibb MJ, Scheu AK, Kieser HJ & Hopwood DA (2001) Beta-ketoacyl acyl carrier protein synthase III (FabH) is essential for fatty acid biosynthesis in Streptomyces coelicolor A3(2). J Bacteriol 183: 3526-3530.
    • (2001) J Bacteriol , vol.183 , pp. 3526-3530
    • Revill, W.P.1    Bibb, M.J.2    Scheu, A.K.3    Kieser, H.J.4    Hopwood, D.A.5
  • 106
    • 0033586767 scopus 로고    scopus 로고
    • Solution structures of apo and holo biotinyl domains from acetyl coenzyme A carboxylase of Escherichia coli determined by triple-resonance nuclear magnetic resonance spectroscopy
    • Roberts EL, Shu N, Howard MJ, Broadhurst RW, Chapman-Smith A, Wallace JC, Morris T, Cronan JE Jr & Perham RN (1999) Solution structures of apo and holo biotinyl domains from acetyl coenzyme A carboxylase of Escherichia coli determined by triple-resonance nuclear magnetic resonance spectroscopy. Biochemistry 38: 5045-5053.
    • (1999) Biochemistry , vol.38 , pp. 5045-5053
    • Roberts, E.L.1    Shu, N.2    Howard, M.J.3    Broadhurst, R.W.4    Chapman-Smith, A.5    Wallace, J.C.6    Morris, T.7    Cronan Jr, J.E.8    Perham, R.N.9
  • 107
    • 84882460199 scopus 로고    scopus 로고
    • Fatty acid and phospholipid metabolism in prokaryotes
    • Dennis EV & Jean EV, eds) - Elsevier, Amsterdam.
    • Rock CO (2008) Fatty acid and phospholipid metabolism in prokaryotes. Biochemistry of Lipids, Lipoproteins and Membranes (Dennis EV & Jean EV, eds), pp. 59-96. Elsevier, Amsterdam.
    • (2008) Biochemistry of Lipids, Lipoproteins and Membranes , pp. 59-96
    • Rock, C.O.1
  • 108
    • 0030581109 scopus 로고    scopus 로고
    • Escherichia coli as a model for the regulation of dissociable (type II) fatty acid biosynthesis
    • Rock CO & Cronan JE (1996) Escherichia coli as a model for the regulation of dissociable (type II) fatty acid biosynthesis. Biochim Biophys Acta 1302: 1-16.
    • (1996) Biochim Biophys Acta , vol.1302 , pp. 1-16
    • Rock, C.O.1    Cronan, J.E.2
  • 109
    • 0032746921 scopus 로고    scopus 로고
    • Genetic and biochemical characterization of the alpha and beta components of a propionyl-CoA carboxylase complex of Streptomyces coelicolor A3(2)
    • Rodriguez E & Gramajo H (1999) Genetic and biochemical characterization of the alpha and beta components of a propionyl-CoA carboxylase complex of Streptomyces coelicolor A3(2). Microbiology 145: 3109-3119.
    • (1999) Microbiology , vol.145 , pp. 3109-3119
    • Rodriguez, E.1    Gramajo, H.2
  • 110
    • 0035458437 scopus 로고    scopus 로고
    • Role of an essential acyl coenzyme A carboxylase in the primary and secondary metabolism of Streptomyces coelicolor A3(2)
    • Rodriguez E, Banchio C, Diacovich L, Bibb MJ & Gramajo H (2001) Role of an essential acyl coenzyme A carboxylase in the primary and secondary metabolism of Streptomyces coelicolor A3(2). Appl Environ Microb 67: 4166-4176.
    • (2001) Appl Environ Microb , vol.67 , pp. 4166-4176
    • Rodriguez, E.1    Banchio, C.2    Diacovich, L.3    Bibb, M.J.4    Gramajo, H.5
  • 112
    • 40049090679 scopus 로고    scopus 로고
    • Probing reactivity and substrate specificity of both subunits of the dimeric Mycobacterium tuberculosis FabH using alkyl-CoA disulfide inhibitors and acyl-CoA substrates
    • Sachdeva S, Musayev F, Alhamadsheh MM, Neel Scarsdale J, Tonie Wright H & Reynolds KA (2008) Probing reactivity and substrate specificity of both subunits of the dimeric Mycobacterium tuberculosis FabH using alkyl-CoA disulfide inhibitors and acyl-CoA substrates. Bioorg Chem 36: 85-90.
    • (2008) Bioorg Chem , vol.36 , pp. 85-90
    • Sachdeva, S.1    Musayev, F.2    Alhamadsheh, M.M.3    Neel Scarsdale, J.4    Tonie Wright, H.5    Reynolds, K.A.6
  • 114
    • 0242268400 scopus 로고    scopus 로고
    • Genetic requirements for mycobacterial survival during infection
    • Sassetti CM & Rubin EJ (2003) Genetic requirements for mycobacterial survival during infection. P Natl Acad Sci USA 100: 12989-12994.
    • (2003) P Natl Acad Sci USA , vol.100 , pp. 12989-12994
    • Sassetti, C.M.1    Rubin, E.J.2
  • 115
    • 0035940515 scopus 로고    scopus 로고
    • Comprehensive identification of conditionally essential genes in mycobacteria
    • Sassetti CM, Boyd DH & Rubin EJ (2001) Comprehensive identification of conditionally essential genes in mycobacteria. P Natl Acad Sci USA 98: 12712-12717.
    • (2001) P Natl Acad Sci USA , vol.98 , pp. 12712-12717
    • Sassetti, C.M.1    Boyd, D.H.2    Rubin, E.J.3
  • 116
    • 0035827542 scopus 로고    scopus 로고
    • Crystal structure of the Mycobacterium tuberculosis beta-ketoacyl-acyl carrier protein synthase III
    • Scarsdale JN, Kazanina G, He X, Reynolds KA & Wright HT (2001) Crystal structure of the Mycobacterium tuberculosis beta-ketoacyl-acyl carrier protein synthase III. J Biol Chem 276: 20516-20522.
    • (2001) J Biol Chem , vol.276 , pp. 20516-20522
    • Scarsdale, J.N.1    Kazanina, G.2    He, X.3    Reynolds, K.A.4    Wright, H.T.5
  • 117
    • 0035861550 scopus 로고    scopus 로고
    • Purification and biochemical characterization of the Mycobacterium tuberculosis beta-ketoacyl-acyl carrier protein synthases KasA and KasB
    • Schaeffer ML, Agnihotri G, Volker C, Kallender H, Brennan PJ & Lonsdale JT (2001) Purification and biochemical characterization of the Mycobacterium tuberculosis beta-ketoacyl-acyl carrier protein synthases KasA and KasB. J Biol Chem 276: 47029-47037.
    • (2001) J Biol Chem , vol.276 , pp. 47029-47037
    • Schaeffer, M.L.1    Agnihotri, G.2    Volker, C.3    Kallender, H.4    Brennan, P.J.5    Lonsdale, J.T.6
  • 118
    • 0029787239 scopus 로고    scopus 로고
    • Disruption of the gene encoding the acyl-CoA-binding protein (ACB1) perturbs acyl-CoA metabolism in Saccharomyces cerevisiae
    • Schjerling CK, Hummel R, Hansen JK, Borsting C, Mikkelsen JM, Kristiansen K & Knudsen J (1996) Disruption of the gene encoding the acyl-CoA-binding protein (ACB1) perturbs acyl-CoA metabolism in Saccharomyces cerevisiae. J Biol Chem 271: 22514-22521.
    • (1996) J Biol Chem , vol.271 , pp. 22514-22521
    • Schjerling, C.K.1    Hummel, R.2    Hansen, J.K.3    Borsting, C.4    Mikkelsen, J.M.5    Kristiansen, K.6    Knudsen, J.7
  • 119
    • 42049114662 scopus 로고    scopus 로고
    • Regulation of type II fatty acid synthase in Gram-positive bacteria
    • Schujman GE & de Mendoza D (2008) Regulation of type II fatty acid synthase in Gram-positive bacteria. Curr Opin Microbiol 11: 148-152.
    • (2008) Curr Opin Microbiol , vol.11 , pp. 148-152
    • Schujman, G.E.1    de Mendoza, D.2
  • 120
    • 0037992415 scopus 로고    scopus 로고
    • FapR, a bacterial transcription factor involved in global regulation of membrane lipid biosynthesis
    • Schujman GE, Paoletti L, Grossman AD & de Mendoza D (2003) FapR, a bacterial transcription factor involved in global regulation of membrane lipid biosynthesis. Dev Cell 4: 663-672.
    • (2003) Dev Cell , vol.4 , pp. 663-672
    • Schujman, G.E.1    Paoletti, L.2    Grossman, A.D.3    de Mendoza, D.4
  • 122
    • 4544275674 scopus 로고    scopus 로고
    • Microbial type I fatty acid synthases (FAS): major players in a network of cellular FAS systems
    • Schweizer E & Hofmann J (2004) Microbial type I fatty acid synthases (FAS): major players in a network of cellular FAS systems. Microbiol Mol Biol R 68: 501-517.
    • (2004) Microbiol Mol Biol R , vol.68 , pp. 501-517
    • Schweizer, E.1    Hofmann, J.2
  • 123
    • 10944226843 scopus 로고    scopus 로고
    • A mechanism for the potent inhibition of eukaryotic acetyl-coenzyme A carboxylase by soraphen A, a macrocyclic polyketide natural product
    • Shen Y, Volrath SL, Weatherly SC, Elich TD & Tong L (2004) A mechanism for the potent inhibition of eukaryotic acetyl-coenzyme A carboxylase by soraphen A, a macrocyclic polyketide natural product. Mol Cell 16: 881-891.
    • (2004) Mol Cell , vol.16 , pp. 881-891
    • Shen, Y.1    Volrath, S.L.2    Weatherly, S.C.3    Elich, T.D.4    Tong, L.5
  • 124
    • 0035907336 scopus 로고    scopus 로고
    • The Mycobacterium tuberculosis pks2 gene encodes the synthase for the hepta- and octamethyl-branched fatty acids required for sulfolipid synthesis
    • Sirakova TD, Thirumala AK, Dubey VS, Sprecher H & Kolattukudy PE (2001) The Mycobacterium tuberculosis pks2 gene encodes the synthase for the hepta- and octamethyl-branched fatty acids required for sulfolipid synthesis. J Biol Chem 276: 16833-16839.
    • (2001) J Biol Chem , vol.276 , pp. 16833-16839
    • Sirakova, T.D.1    Thirumala, A.K.2    Dubey, V.S.3    Sprecher, H.4    Kolattukudy, P.E.5
  • 125
    • 0036448224 scopus 로고    scopus 로고
    • The role of KasA and KasB in the biosynthesis of meromycolic acids and isoniazid resistance in Mycobacterium tuberculosis
    • (Edinb)
    • Slayden RA & Barry CE III (2002) The role of KasA and KasB in the biosynthesis of meromycolic acids and isoniazid resistance in Mycobacterium tuberculosis. Tuberculosis (Edinb) 82: 149-160.
    • (2002) Tuberculosis , vol.82 , pp. 149-160
    • Slayden, R.A.1    Barry III, C.E.2
  • 126
    • 51149101636 scopus 로고    scopus 로고
    • Biochemistry. An enzyme assembly line
    • Smith JL & Sherman DH (2008) Biochemistry. An enzyme assembly line. Science 321: 1304-1305.
    • (2008) Science , vol.321 , pp. 1304-1305
    • Smith, J.L.1    Sherman, D.H.2
  • 127
    • 33845212858 scopus 로고    scopus 로고
    • Type III polyketide synthase beta-ketoacyl-ACP starter unit and ethylmalonyl-CoA extender unit selectivity discovered by Streptomyces coelicolor genome mining
    • Song L, Barona-Gomez F, Corre C, Xiang L, Udwary DW, Austin MB, Noel JP, Moore BS & Challis GL (2006) Type III polyketide synthase beta-ketoacyl-ACP starter unit and ethylmalonyl-CoA extender unit selectivity discovered by Streptomyces coelicolor genome mining. J Am Chem Soc 128: 14754-14755.
    • (2006) J Am Chem Soc , vol.128 , pp. 14754-14755
    • Song, L.1    Barona-Gomez, F.2    Corre, C.3    Xiang, L.4    Udwary, D.W.5    Austin, M.B.6    Noel, J.P.7    Moore, B.S.8    Challis, G.L.9
  • 128
    • 0024398149 scopus 로고
    • Protein phosphorylation and regulation of adaptive responses in bacteria
    • Stock JB, Ninfa AJ & Stock AM (1989) Protein phosphorylation and regulation of adaptive responses in bacteria. Microbiol Rev 53: 450-490.
    • (1989) Microbiol Rev , vol.53 , pp. 450-490
    • Stock, J.B.1    Ninfa, A.J.2    Stock, A.M.3
  • 129
    • 0029743606 scopus 로고    scopus 로고
    • Identification and functional differentiation of two type I fatty acid synthases in Brevibacterium ammoniagenes
    • Stuible HP, Wagner C, Andreou I, Huter G, Haselmann J & Schweizer E (1996) Identification and functional differentiation of two type I fatty acid synthases in Brevibacterium ammoniagenes. J Bacteriol 178: 4787-4793.
    • (1996) J Bacteriol , vol.178 , pp. 4787-4793
    • Stuible, H.P.1    Wagner, C.2    Andreou, I.3    Huter, G.4    Haselmann, J.5    Schweizer, E.6
  • 130
    • 0029125339 scopus 로고
    • Malonyl-coenzyme A: acyl carrier protein acyltransferase of Streptomyces glaucescens: a possible link between fatty acid and polyketide biosynthesis
    • Summers RG, Ali A, Shen B, Wessel WA & Hutchinson CR (1995) Malonyl-coenzyme A: acyl carrier protein acyltransferase of Streptomyces glaucescens: a possible link between fatty acid and polyketide biosynthesis. Biochemistry 34: 9389-9402.
    • (1995) Biochemistry , vol.34 , pp. 9389-9402
    • Summers, R.G.1    Ali, A.2    Shen, B.3    Wessel, W.A.4    Hutchinson, C.R.5
  • 131
    • 66149108701 scopus 로고    scopus 로고
    • Influence relevance voting: an accurate and interpretable virtual high throughput screening method
    • Swamidass SJ, Azencott CA, Lin TW, Gramajo H, Tsai SC & Baldi P (2009) Influence relevance voting: an accurate and interpretable virtual high throughput screening method. J Chem Inf Model 49: 756-766.
    • (2009) J Chem Inf Model , vol.49 , pp. 756-766
    • Swamidass, S.J.1    Azencott, C.A.2    Lin, T.W.3    Gramajo, H.4    Tsai, S.C.5    Baldi, P.6
  • 132
    • 12844278679 scopus 로고    scopus 로고
    • Pathway to synthesis and processing of mycolic acids in Mycobacterium tuberculosis
    • Takayama K, Wang C & Besra GS (2005) Pathway to synthesis and processing of mycolic acids in Mycobacterium tuberculosis. Clin Microbiol Rev 18: 81-101.
    • (2005) Clin Microbiol Rev , vol.18 , pp. 81-101
    • Takayama, K.1    Wang, C.2    Besra, G.S.3
  • 133
    • 21144440616 scopus 로고    scopus 로고
    • Complete genome sequence and analysis of the multiresistant nosocomial pathogen Corynebacterium jeikeium K411, a lipid-requiring bacterium of the human skin flora
    • Tauch A, Kaiser O, Hain T et al. (2005) Complete genome sequence and analysis of the multiresistant nosocomial pathogen Corynebacterium jeikeium K411, a lipid-requiring bacterium of the human skin flora. J Bacteriol 187: 4671-4682.
    • (2005) J Bacteriol , vol.187 , pp. 4671-4682
    • Tauch, A.1    Kaiser, O.2    Hain, T.3
  • 134
    • 45249116205 scopus 로고    scopus 로고
    • The lifestyle of Corynebacterium urealyticum derived from its complete genome sequence established by pyrosequencing
    • Tauch A, Trost E, Tilker A et al. (2008) The lifestyle of Corynebacterium urealyticum derived from its complete genome sequence established by pyrosequencing. J Biotechnol 136: 11-21.
    • (2008) J Biotechnol , vol.136 , pp. 11-21
    • Tauch, A.1    Trost, E.2    Tilker, A.3
  • 135
    • 23944509003 scopus 로고    scopus 로고
    • Acetyl-coenzyme A carboxylase: crucial metabolic enzyme and attractive target for drug discovery
    • Tong L (2005) Acetyl-coenzyme A carboxylase: crucial metabolic enzyme and attractive target for drug discovery. Cell Mol Life Sci 62: 1784-1803.
    • (2005) Cell Mol Life Sci , vol.62 , pp. 1784-1803
    • Tong, L.1
  • 136
    • 33751579134 scopus 로고    scopus 로고
    • Acetyl-coenzyme A carboxylases: versatile targets for drug discovery
    • Tong L & Harwood HJ Jr (2006) Acetyl-coenzyme A carboxylases: versatile targets for drug discovery. J Cell Biochem 99: 1476-1488.
    • (2006) J Cell Biochem , vol.99 , pp. 1476-1488
    • Tong, L.1    Harwood Jr, H.J.2
  • 137
    • 0014010341 scopus 로고
    • Studies on the mechanism of fatty acid synthesis. XVI. Preparation and general properties of acyl-malonyl acyl carrier protein-condensing enzyme from Escherichia coli
    • Toomey RE & Wakil SJ (1966) Studies on the mechanism of fatty acid synthesis. XVI. Preparation and general properties of acyl-malonyl acyl carrier protein-condensing enzyme from Escherichia coli. J Biol Chem 241: 1159-1165.
    • (1966) J Biol Chem , vol.241 , pp. 1159-1165
    • Toomey, R.E.1    Wakil, S.J.2
  • 138
    • 1842577641 scopus 로고    scopus 로고
    • Enzymic activation and transfer of fatty acids as acyl-adenylates in mycobacteria
    • Trivedi OA, Arora P, Sridharan V, Tickoo R, Mohanty D & Gokhale RS (2004) Enzymic activation and transfer of fatty acids as acyl-adenylates in mycobacteria. Nature 428: 441-445.
    • (2004) Nature , vol.428 , pp. 441-445
    • Trivedi, O.A.1    Arora, P.2    Sridharan, V.3    Tickoo, R.4    Mohanty, D.5    Gokhale, R.S.6
  • 140
    • 0026775039 scopus 로고
    • Isolation and characterization of the beta-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 beta-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
  • 141
    • 65249174626 scopus 로고    scopus 로고
    • The Mycobacterium tuberculosis beta-ketoacyl-acyl carrier protein synthase III activity is inhibited by phosphorylation on a single threonine residue
    • Veyron-Churlet R, Molle V, Taylor RC, Brown AK, Besra GS, Zanella-Cleon I, Futterer K & Kremer L (2009) The Mycobacterium tuberculosis beta-ketoacyl-acyl carrier protein synthase III activity is inhibited by phosphorylation on a single threonine residue. J Biol Chem 284: 6414-6424.
    • (2009) J Biol Chem , vol.284 , pp. 6414-6424
    • Veyron-Churlet, R.1    Molle, V.2    Taylor, R.C.3    Brown, A.K.4    Besra, G.S.5    Zanella-Cleon, I.6    Futterer, K.7    Kremer, L.8
  • 142
    • 77951212397 scopus 로고    scopus 로고
    • Phosphorylation of the Mycobacterium tuberculosis beta-ketoacyl-acyl carrier protein reductase MabA regulates mycolic acid biosynthesis
    • Veyron-Churlet R, Zanella-Cleon I, Cohen-Gonsaud M, Molle V & Kremer L (2010) Phosphorylation of the Mycobacterium tuberculosis beta-ketoacyl-acyl carrier protein reductase MabA regulates mycolic acid biosynthesis. J Biol Chem 285: 12714-12725.
    • (2010) J Biol Chem , vol.285 , pp. 12714-12725
    • Veyron-Churlet, R.1    Zanella-Cleon, I.2    Cohen-Gonsaud, M.3    Molle, V.4    Kremer, L.5
  • 144
    • 0028085434 scopus 로고
    • Three-dimensional structure of the biotin carboxylase subunit of acetyl-CoA carboxylase
    • Waldrop GL, Rayment I & Holden HM (1994) Three-dimensional structure of the biotin carboxylase subunit of acetyl-CoA carboxylase. Biochemistry 33: 10249-10256.
    • (1994) Biochemistry , vol.33 , pp. 10249-10256
    • Waldrop, G.L.1    Rayment, I.2    Holden, H.M.3
  • 145
    • 0029160904 scopus 로고
    • In vivo analysis of straight-chain and branched-chain fatty acid biosynthesis in three actinomycetes
    • Wallace KK, Zhao B, McArthur HA & Reynolds KA (1995) In vivo analysis of straight-chain and branched-chain fatty acid biosynthesis in three actinomycetes. FEMS Microbiol Lett 131: 227-234.
    • (1995) FEMS Microbiol Lett , vol.131 , pp. 227-234
    • Wallace, K.K.1    Zhao, B.2    McArthur, H.A.3    Reynolds, K.A.4
  • 146
    • 0041813291 scopus 로고    scopus 로고
    • Crystal structure of the carboxyltransferase subunit of the bacterial sodium ion pump glutaconyl-coenzyme A decarboxylase
    • Wendt KS, Schall I, Huber R, Buckel W & Jacob U (2003) Crystal structure of the carboxyltransferase subunit of the bacterial sodium ion pump glutaconyl-coenzyme A decarboxylase. EMBO J 22: 3493-3502.
    • (2003) EMBO J , vol.22 , pp. 3493-3502
    • Wendt, K.S.1    Schall, I.2    Huber, R.3    Buckel, W.4    Jacob, U.5
  • 147
    • 22244466130 scopus 로고    scopus 로고
    • The structural biology of type II fatty acid biosynthesis
    • White SW, Zheng J, Zhang YM & Rock (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    Rock4
  • 148
    • 0017839021 scopus 로고
    • Subunit structure of Mycobacterium smegmatis fatty acid synthetase. Evidence for identical multifunctional polypeptide chains
    • Wood WI, Peterson DO & Bloch K (1978) Subunit structure of Mycobacterium smegmatis fatty acid synthetase. Evidence for identical multifunctional polypeptide chains. J Biol Chem 253: 2650-2656.
    • (1978) J Biol Chem , vol.253 , pp. 2650-2656
    • Wood, W.I.1    Peterson, D.O.2    Bloch, K.3
  • 149
    • 40949154700 scopus 로고    scopus 로고
    • Crystal structures of human and Staphylococcus aureus pyruvate carboxylase and molecular insights into the carboxyltransfer reaction
    • Xiang S & Tong L (2008) Crystal structures of human and Staphylococcus aureus pyruvate carboxylase and molecular insights into the carboxyltransfer reaction. Nat Struct Mol Biol 15: 295-302.
    • (2008) Nat Struct Mol Biol , vol.15 , pp. 295-302
    • Xiang, S.1    Tong, L.2
  • 150
    • 0030668421 scopus 로고    scopus 로고
    • Structure of the carboxy-terminal fragment of the apo-biotin carboxyl carrier subunit of Escherichia coli acetyl-CoA carboxylase
    • Yao X, Wei D, Soden C Jr, Summers MF & Beckett D (1997) Structure of the carboxy-terminal fragment of the apo-biotin carboxyl carrier subunit of Escherichia coli acetyl-CoA carboxylase. Biochemistry 36: 15089-15100.
    • (1997) Biochemistry , vol.36 , pp. 15089-15100
    • Yao, X.1    Wei, D.2    Soden Jr, C.3    Summers, M.F.4    Beckett, D.5
  • 151
    • 66349116676 scopus 로고    scopus 로고
    • A symmetrical tetramer for S. aureus pyruvate carboxylase in complex with coenzyme A
    • Yu LP, Xiang S, Lasso G, Gil D, Valle M & Tong L (2009) A symmetrical tetramer for S. aureus pyruvate carboxylase in complex with coenzyme A. Structure 17: 823-832.
    • (2009) Structure , vol.17 , pp. 823-832
    • Yu, L.P.1    Xiang, S.2    Lasso, G.3    Gil, D.4    Valle, M.5    Tong, L.6
  • 152
    • 0037470947 scopus 로고    scopus 로고
    • Crystal structure of the carboxyltransferase domain of acetyl-coenzyme A carboxylase
    • Zhang H, Yang Z, Shen Y & Tong L (2003) Crystal structure of the carboxyltransferase domain of acetyl-coenzyme A carboxylase. Science 299: 2064-2067.
    • (2003) Science , vol.299 , pp. 2064-2067
    • Zhang, H.1    Yang, Z.2    Shen, Y.3    Tong, L.4
  • 153
    • 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
  • 154
    • 66349100178 scopus 로고    scopus 로고
    • Transcriptional regulation in bacterial membrane lipid synthesis
    • Zhang YM & Rock CO (2009) Transcriptional regulation in bacterial membrane lipid synthesis. J Lipid Res 50 (suppl): S115-S119.
    • (2009) J Lipid Res , vol.50 , Issue.SUPPL.
    • Zhang, Y.M.1    Rock, C.O.2
  • 155
    • 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
  • 156
    • 3042606702 scopus 로고    scopus 로고
    • Characterization of Mycobacterium smegmatis expressing the Mycobacterium tuberculosis fatty acid synthase I (fas1) gene
    • Zimhony O, Vilcheze C & Jacobs WR Jr (2004) Characterization of Mycobacterium smegmatis expressing the Mycobacterium tuberculosis fatty acid synthase I (fas1) gene. J Bacteriol 186: 4051-4055.
    • (2004) J Bacteriol , vol.186 , pp. 4051-4055
    • Zimhony, O.1    Vilcheze, C.2    Jacobs Jr, W.R.3


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