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Volumn 302, Issue 1, 2003, Pages 35-40

Glutamate-41 of Vibrio harveyi acyl carrier protein is essential for fatty acid synthase but not acyl-ACP synthetase activity

Author keywords

Acyl carrier protein; Acyl ACP synthetase; Circular dichroism; Fatty acid synthase; Gel electrophoresis; Site directed mutagenesis

Indexed keywords

ACYL CARRIER PROTEIN; ALANINE; BACTERIAL PROTEIN; CITRATE SYNTHASE; FATTY ACID SYNTHASE; GLUTAMATE 41; M PROTEIN; UNCLASSIFIED DRUG;

EID: 0037470457     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-291X(03)00108-6     Document Type: Article
Times cited : (15)

References (25)
  • 1
    • 0030581109 scopus 로고    scopus 로고
    • Escherichia coli as a model for the regulation of dissociable (type II) fatty acid biosynthesis
    • Rock C.O., Cronan J.E. Jr. Escherichia coli as a model for the regulation of dissociable (type II) fatty acid biosynthesis. Biochim. Biophys. Acta. 1302:1996;1-16.
    • (1996) Biochim. Biophys. Acta , vol.1302 , pp. 1-16
    • Rock, C.O.1    Cronan J.E., Jr.2
  • 2
    • 0023654454 scopus 로고
    • Biosynthesis of lipid A precursors in Escherichia coli. A cytoplasmic acyltransferase that converts UDP-N-acetylglucosamine to UDP-3-O-(R-3-hydroxymyristoyl)-N-acetylglucosamine
    • Anderson M.S., Raetz C.R. Biosynthesis of lipid A precursors in Escherichia coli. A cytoplasmic acyltransferase that converts UDP-N-acetylglucosamine to UDP-3-O-(R-3-hydroxymyristoyl)-N-acetylglucosamine. J. Biol. Chem. 262:1987;5159-5169.
    • (1987) J. Biol. Chem. , vol.262 , pp. 5159-5169
    • Anderson, M.S.1    Raetz, C.R.2
  • 3
    • 0030747906 scopus 로고    scopus 로고
    • A new metabolic link. The acyl carrier protein of lipid synthesis donates lipoic acid to the pyruvate dehydrogenase complex in Escherichia coli and mitochondria
    • Jordan S.W., Cronan J.E. Jr. A new metabolic link. The acyl carrier protein of lipid synthesis donates lipoic acid to the pyruvate dehydrogenase complex in Escherichia coli and mitochondria. J. Biol. Chem. 272:1997;17903-17906.
    • (1997) J. Biol. Chem. , vol.272 , pp. 17903-17906
    • Jordan, S.W.1    Cronan J.E., Jr.2
  • 4
    • 0026432638 scopus 로고
    • Activation of Escherichia coli prohaemolysin to the mature toxin by acyl carrier protein-dependent fatty acylation
    • Issartel J.P., Koronakis V., Hughes C. Activation of Escherichia coli prohaemolysin to the mature toxin by acyl carrier protein-dependent fatty acylation. Nature. 351:1991;759-761.
    • (1991) Nature , vol.351 , pp. 759-761
    • Issartel, J.P.1    Koronakis, V.2    Hughes, C.3
  • 5
    • 0029817781 scopus 로고    scopus 로고
    • Generation of cell-to-cell signals in quorum sensing: Acyl homoserine lactone synthase activity of a purified Vibrio fischeri LuxI protein
    • Schaefer A.L., Val D.L., Hanzelka B.L., Cronan J.E. Jr., Greenberg E.P. Generation of cell-to-cell signals in quorum sensing: acyl homoserine lactone synthase activity of a purified Vibrio fischeri LuxI protein. Proc. Natl. Acad. Sci. USA. 93:1996;9505-9509.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 9505-9509
    • Schaefer, A.L.1    Val, D.L.2    Hanzelka, B.L.3    Cronan J.E., Jr.4    Greenberg, E.P.5
  • 6
    • 0022410208 scopus 로고
    • Acyl-acyl carrier protein as a source of fatty acids for bacterial bioluminescence
    • Byers D.M., Meighen E.A. Acyl-acyl carrier protein as a source of fatty acids for bacterial bioluminescence. Proc. Natl. Acad. Sci. USA. 82:1985;6085-6089.
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 6085-6089
    • Byers, D.M.1    Meighen, E.A.2
  • 7
    • 0025613125 scopus 로고
    • Refinement of the NMR structures for acyl carrier protein with scalar coupling data
    • Kim Y., Prestegard J.H. Refinement of the NMR structures for acyl carrier protein with scalar coupling data. Proteins. 8:1990;377-385.
    • (1990) Proteins , vol.8 , pp. 377-385
    • Kim, Y.1    Prestegard, J.H.2
  • 8
    • 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 K.D., Lin L., Tam A., Mathew R., Hixon J., Stahl M., Fritz C.C., Seehra J., Somers W.S. 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 Fold. Des. 8:2000;883-895.
    • (2000) Structure Fold. Des. , 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
  • 9
    • 0030972114 scopus 로고    scopus 로고
    • Solution structure of the actinorhodin polyketide synthase acyl carrier protein from Streptomyces coelicolor A3(2)
    • Crump M.P., Crosby J., Dempsey C.E., Parkinson J.A., Murray M., Hopwood D.A., Simpson T.J. Solution structure of the actinorhodin polyketide synthase acyl carrier protein from Streptomyces coelicolor A3(2). Biochemistry. 36:1997;6000-6008.
    • (1997) Biochemistry , vol.36 , pp. 6000-6008
    • Crump, M.P.1    Crosby, J.2    Dempsey, C.E.3    Parkinson, J.A.4    Murray, M.5    Hopwood, D.A.6    Simpson, T.J.7
  • 10
    • 0037013187 scopus 로고    scopus 로고
    • The solution structure of acyl carrier protein from Mycobacterium tuberculosis
    • Wong H.C., Liu G., Zhang Y.M., Rock C.O., Zheng J. The solution structure of acyl carrier protein from Mycobacterium tuberculosis. J. Biol. Chem. 277:2002;15874-15880.
    • (2002) J. Biol. Chem. , vol.277 , pp. 15874-15880
    • Wong, H.C.1    Liu, G.2    Zhang, Y.M.3    Rock, C.O.4    Zheng, J.5
  • 11
    • 0036247948 scopus 로고    scopus 로고
    • Inhibitors of fatty acid synthesis as antimicrobial chemotherapeutics
    • Heath R.J., White S.W., Rock C.O. Inhibitors of fatty acid synthesis as antimicrobial chemotherapeutics. Appl. Microbiol. Biotechnol. 58:2002;695-703.
    • (2002) Appl. Microbiol. Biotechnol. , vol.58 , pp. 695-703
    • Heath, R.J.1    White, S.W.2    Rock, C.O.3
  • 12
    • 0035896547 scopus 로고    scopus 로고
    • Identification and analysis of the acyl carrier protein (ACP) docking site on β-ketoacyl-ACP synthase III
    • Zhang Y.M., Rao M.S., Heath R.J., Price A.C., Olson A.J., Rock C.O., White S.W. Identification and analysis of the acyl carrier protein (ACP) docking site on β-ketoacyl-ACP synthase III. J. Biol. Chem. 276:2001;8231-8238.
    • (2001) J. Biol. Chem. , vol.276 , pp. 8231-8238
    • Zhang, Y.M.1    Rao, M.S.2    Heath, R.J.3    Price, A.C.4    Olson, A.J.5    Rock, C.O.6    White, S.W.7
  • 13
    • 0030917810 scopus 로고    scopus 로고
    • Domains of Escherichia coli acyl carrier protein important for membrane-derived-oligosaccharide biosynthesis
    • Tang L., Weissborn A.C., Kennedy E.P. Domains of Escherichia coli acyl carrier protein important for membrane-derived-oligosaccharide biosynthesis. J. Bacteriol. 179:1997;3697-3705.
    • (1997) J. Bacteriol. , vol.179 , pp. 3697-3705
    • Tang, L.1    Weissborn, A.C.2    Kennedy, E.P.3
  • 14
    • 0035929665 scopus 로고    scopus 로고
    • Site-directed mutagenesis of acyl carrier protein (ACP) reveals amino acid residues involved in ACP structure and acyl-ACP synthetase activity
    • Flaman A.S., Chen J.M., Van Iderstine S.C., Byers D.M. Site-directed mutagenesis of acyl carrier protein (ACP) reveals amino acid residues involved in ACP structure and acyl-ACP synthetase activity. J. Biol. Chem. 276:2001;35934-35939.
    • (2001) J. Biol. Chem. , vol.276 , pp. 35934-35939
    • Flaman, A.S.1    Chen, J.M.2    Van Iderstine, S.C.3    Byers, D.M.4
  • 15
    • 0027403760 scopus 로고
    • Purification and characterization of fatty acyl-acyl carrier protein synthetase from Vibrio harveyi
    • Fice D., Shen Z., Byers D.M. Purification and characterization of fatty acyl-acyl carrier protein synthetase from Vibrio harveyi. J. Bacteriol. 175:1993;1865-1870.
    • (1993) J. Bacteriol. , vol.175 , pp. 1865-1870
    • Fice, D.1    Shen, Z.2    Byers, D.M.3
  • 16
    • 0026715776 scopus 로고
    • Preparation of fatty-acylated derivatives of acyl carrier protein using Vibrio harveyi acyl-ACP synthetase
    • Shen Z., Fice D., Byers D.M. Preparation of fatty-acylated derivatives of acyl carrier protein using Vibrio harveyi acyl-ACP synthetase. Anal. Biochem. 204:1992;34-39.
    • (1992) Anal. Biochem. , vol.204 , pp. 34-39
    • Shen, Z.1    Fice, D.2    Byers, D.M.3
  • 17
    • 0019887843 scopus 로고
    • Molecular properties of acyl carrier protein derivatives
    • Rock C.O., Cronan J.E. Jr., Armitage I.M. Molecular properties of acyl carrier protein derivatives. J. Biol. Chem. 256:1981;2669-2674.
    • (1981) J. Biol. Chem. , vol.256 , pp. 2669-2674
    • Rock, C.O.1    Cronan J.E., Jr.2    Armitage, I.M.3
  • 18
    • 0020198680 scopus 로고
    • Electrophoresis buffers for polyacrylamide gels at various pH
    • McLellan T. Electrophoresis buffers for polyacrylamide gels at various pH. Anal. Biochem. 126:1982;94-99.
    • (1982) Anal. Biochem. , vol.126 , pp. 94-99
    • McLellan, T.1
  • 19
    • 0030034657 scopus 로고    scopus 로고
    • Isolation of Vibrio harveyi acyl carrier protein and the fabG, acpP, and fabF genes involved in fatty acid biosynthesis
    • Shen Z., Byers D.M. Isolation of Vibrio harveyi acyl carrier protein and the fabG, acpP, and fabF genes involved in fatty acid biosynthesis. J. Bacteriol. 178:1996;571-573.
    • (1996) J. Bacteriol. , vol.178 , pp. 571-573
    • Shen, Z.1    Byers, D.M.2
  • 20
    • 0037121453 scopus 로고    scopus 로고
    • Identification of a key residue in the conformational stability of acyl carrier protein
    • Keating M.M., Gong H., Byers D.M. Identification of a key residue in the conformational stability of acyl carrier protein. Biochim. Biophys. Acta. 1601:2002;208-214.
    • (2002) Biochim. Biophys. Acta , vol.1601 , pp. 208-214
    • Keating, M.M.1    Gong, H.2    Byers, D.M.3
  • 21
    • 0016628149 scopus 로고
    • On the structure-function relationship of acyl carrier protein of Escherichia coli
    • Schulz H. On the structure-function relationship of acyl carrier protein of Escherichia coli. J. Biol. Chem. 250:1975;2299-2304.
    • (1975) J. Biol. Chem. , vol.250 , pp. 2299-2304
    • Schulz, H.1
  • 22
    • 0030037751 scopus 로고    scopus 로고
    • An isoleucine to valine substitution in Escherichia coli acyl carrier protein results in a functional protein of decreased molecular radius at elevated pH
    • Keating D.H., Cronan J.E. Jr. An isoleucine to valine substitution in Escherichia coli acyl carrier protein results in a functional protein of decreased molecular radius at elevated pH. J. Biol. Chem. 271:1996;15905-15910.
    • (1996) J. Biol. Chem. , vol.271 , pp. 15905-15910
    • Keating, D.H.1    Cronan J.E., Jr.2
  • 23
    • 0015219135 scopus 로고
    • Structure-function relationships of the acyl-carrier protein of Escherichia coli
    • Abita J.P., Lazdunski M., Ailhaud G. Structure-function relationships of the acyl-carrier protein of Escherichia coli. Eur. J. Biochem. 23:1971;412-420.
    • (1971) Eur. J. Biochem. , vol.23 , pp. 412-420
    • Abita, J.P.1    Lazdunski, M.2    Ailhaud, G.3
  • 24
    • 0024435205 scopus 로고
    • A dynamic model for the structure of acyl carrier protein in solution
    • Kim Y., Prestegard J.H. A dynamic model for the structure of acyl carrier protein in solution. Biochemistry. 28:1989;8792-8797.
    • (1989) Biochemistry , vol.28 , pp. 8792-8797
    • Kim, Y.1    Prestegard, J.H.2
  • 25
    • 0023731129 scopus 로고
    • Location of divalent ion sites in acyl carrier protein using relaxation perturbed 2D NMR
    • Frederick A.F., Kay L.E., Prestegard J.H. Location of divalent ion sites in acyl carrier protein using relaxation perturbed 2D NMR. FEBS Lett. 238:1988;43-48.
    • (1988) FEBS Lett. , vol.238 , pp. 43-48
    • Frederick, A.F.1    Kay, L.E.2    Prestegard, J.H.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.