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Volumn 182, Issue 2, 2000, Pages 365-370

β-ketoacyl-acyl carrier protein synthase III (FabH) is a determining factor in branched-chain fatty acid biosynthesis

Author keywords

[No Author keywords available]

Indexed keywords

3 OXOACYL ACYL CARRIER PROTEIN SYNTHASE; ACETYL COENZYME A; BACTERIAL PROTEIN; FATTY ACID;

EID: 0033986294     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.182.2.365-370.2000     Document Type: Article
Times cited : (222)

References (34)
  • 1
    • 0033609499 scopus 로고    scopus 로고
    • Purification and properties of the Streptomyces peucetius DpsC β-ketoacyl:Acyl carrier protein synthase III that specifies the propionate-starter unit for type II polyketide biosynthesis
    • Bao, W., P. J. Sheldon, and R. Hutchinson. 1999. Purification and properties of the Streptomyces peucetius DpsC β-ketoacyl:acyl carrier protein synthase III that specifies the propionate-starter unit for type II polyketide biosynthesis. Biochemistry 38:9752-9757.
    • (1999) Biochemistry , vol.38 , pp. 9752-9757
    • Bao, W.1    Sheldon, P.J.2    Hutchinson, R.3
  • 3
    • 33845261493 scopus 로고
    • A rapid method of total lipid extraction and purification
    • Bligh, E. G., and W. J. Dyer. 1959. A rapid method of total lipid extraction and purification. Can. J. Biochem. Physiol. 37:911-917.
    • (1959) Can. J. Biochem. Physiol. , vol.37 , pp. 911-917
    • Bligh, E.G.1    Dyer, W.J.2
  • 4
    • 0017184389 scopus 로고
    • A rapid and sensitive method for quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. 1976. A rapid and sensitive method for quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72:248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 5
    • 0014737367 scopus 로고
    • Comparative aspects of fatty acid synthesis in Bacillus and Escherichia coli
    • Butterworth, P. H., and K. Bloch. 1970. Comparative aspects of fatty acid synthesis in Bacillus and Escherichia coli. Eur. J. Biochem. 12:496-501.
    • (1970) Eur. J. Biochem. , vol.12 , pp. 496-501
    • Butterworth, P.H.1    Bloch, K.2
  • 6
    • 0032211844 scopus 로고    scopus 로고
    • Direct targets of phosphoinositide 3-kinase products in membrane traffic and signal transduction
    • Corvera, S., and M. P. Czech. 1998. Direct targets of phosphoinositide 3-kinase products in membrane traffic and signal transduction. Trends Cell Biol. 8:442-446.
    • (1998) Trends Cell Biol. , vol.8 , pp. 442-446
    • Corvera, S.1    Czech, M.P.2
  • 7
    • 0001517649 scopus 로고    scopus 로고
    • Biosynthesis of membrane lipids
    • F. C. Neidhardt, R. Curtis III, J. L. Ingraham, E. C. C. Lin, K. B. Low, B. Magasanik, W. S. Reznikoff, M. Riley, M. Schaechter, and H. E. Umbarger (ed.), American Society for Microbiology, Washington, D.C.
    • Cronan, J. E., Jr., and C. O. Rock. 1996. Biosynthesis of membrane lipids, p. 612-636. In F. C. Neidhardt, R. Curtis III, J. L. Ingraham, E. C. C. Lin, K. B. Low, B. Magasanik, W. S. Reznikoff, M. Riley, M. Schaechter, and H. E. Umbarger (ed.), Escherichia coli and Salmonella: cellular and molecular biology, 2nd ed. American Society for Microbiology, Washington, D.C.
    • (1996) Escherichia Coli and Salmonella: Cellular and Molecular Biology, 2nd Ed. , pp. 612-636
    • Cronan J.E., Jr.1    Rock, C.O.2
  • 10
    • 0031751326 scopus 로고    scopus 로고
    • Characterization of β-ketoacylacyl carrier protein synthase III from Streptomyces glaucescens and its role in initiation of fatty acid biosynthesis
    • Han, L., S. Lobo, and K. A. Reynolds. 1998. Characterization of β-ketoacylacyl 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
  • 11
    • 0028855972 scopus 로고
    • Enoyl-acyl carrier protein reductase (fabl) plays a determinant role in completing cycles of fatty acid elongation in Escherichia coli
    • Heath, R. J., and C. O. Rock. 1995. Enoyl-acyl carrier protein reductase (fabl) 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
  • 12
    • 17544367317 scopus 로고    scopus 로고
    • Inhibition of β-ketoacyl-acyl carrier protein synthase III (FabH) by acyl-acyl carrier protein in Escherichia coli
    • Heath, R. J., and C. O. Rock. 1996. Inhibition of β-ketoacyl-acyl carrier protein synthase III (FabH) by acyl-acyl carrier protein in Escherichia coli. J. Biol. Chem. 271:10996-11000.
    • (1996) J. Biol. Chem. , vol.271 , pp. 10996-11000
    • Heath, R.J.1    Rock, C.O.2
  • 13
    • 0029926496 scopus 로고    scopus 로고
    • Roles of the FabA and FabZ β-hydroxyacyl-acyl carrier protein dehydratases in Escherichia coli fatty acid biosynthesis
    • Heath, R. J., and C. O. Rock. 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
  • 14
    • 0024564710 scopus 로고
    • Acetoacetyl-acyl carrier protein synthase: A target for the antibiotic thiolactomycin
    • Jackowski, S., C. M. Murphy, J. E. Cronan, Jr., and C. O. Rock. 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., Jr.3    Rock, C.O.4
  • 15
    • 0023644886 scopus 로고
    • Acetoacetyl-acyl carrier protein synthase, a potential regulator of fatty acid biosynthesis in bacteria
    • Jackowski, S., and C. O. Rock. 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
  • 16
    • 0013587454 scopus 로고
    • Biosynthesis of branched chain fatty acids
    • Kaneda, T. 1963. Biosynthesis of branched chain fatty acids. J. Biol. Chem. 238:1229-1235.
    • (1963) J. Biol. Chem. , vol.238 , pp. 1229-1235
    • Kaneda, T.1
  • 17
    • 0013916553 scopus 로고
    • Biosynthesis of branched-chain fatty acids. IV. Factors affecting relative abundance of fatty acids produced by Bacillus subtilis
    • Kaneda, T. 1966. Biosynthesis of branched-chain fatty acids. IV. Factors affecting relative abundance of fatty acids produced by Bacillus subtilis. Can. J. Microbiol. 12:501-514.
    • (1966) Can. J. Microbiol. , vol.12 , pp. 501-514
    • Kaneda, T.1
  • 18
    • 0015231737 scopus 로고
    • 6-fatty acid isomers into the related long-chain fatty acids by growing cells of Bacillus subtilis
    • 6-fatty acid isomers into the related long-chain fatty acids by growing cells of Bacillus subtilis. Biochemistry 10:340-347.
    • (1971) Biochemistry , vol.10 , pp. 340-347
    • Kaneda, T.1
  • 19
    • 0024276071 scopus 로고
    • Steroselectivity in the 2-methylbutyrate incorporation into anteiso fatty acids in Bacillus subtilis mutants
    • Kaneda, T. 1988. Steroselectivity in the 2-methylbutyrate incorporation into anteiso fatty acids in Bacillus subtilis mutants. Biochim. Biophys. Acta 960: 10-18.
    • (1988) Biochim. Biophys. Acta , vol.960 , pp. 10-18
    • Kaneda, T.1
  • 20
    • 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
  • 21
    • 0030731108 scopus 로고    scopus 로고
    • The complete genome sequence of the gram-positive bacterium Bacillus subtilis
    • Kunst, F., et al. 1997. The complete genome sequence of the gram-positive bacterium Bacillus subtilis. Nature (London) 390:249-256.
    • (1997) Nature (London) , vol.390 , pp. 249-256
    • Kunst, F.1
  • 22
  • 23
    • 0024268196 scopus 로고
    • Biosynthesis of branched-chain fatty acids in Bacillis subtilis. A decarboxylase is essential for branched-chain fatty acid synthetase
    • Oku, H., and T. Kaneda. 1988. Biosynthesis of branched-chain fatty acids in Bacillis subtilis. A decarboxylase is essential for branched-chain fatty acid synthetase. J. Biol. Chem. 263:18386-18396.
    • (1988) J. Biol. Chem. , vol.263 , pp. 18386-18396
    • Oku, H.1    Kaneda, T.2
  • 24
    • 0030581109 scopus 로고    scopus 로고
    • Escherichia coli as a model for the regulation of dissociable (type II) fatty acid biosynthesis
    • Rock, C. O., and J. E. Cronan, Jr. 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., Jr.2
  • 25
    • 77956702324 scopus 로고    scopus 로고
    • Lipid metabolism in procaryotes
    • D. E. Vance and J. E. Vance (ed.), Elsevier Publishing Co., Amsterdam, The Netherlands
    • Rock, C. O., S. Jackowski, and J. E. Cronan, Jr. 1996. Lipid metabolism in procaryotes, p. 35-74. In D. E. Vance and J. E. Vance (ed.), Biochemistry of lipids, lipoproteins and membranes, vol. 31. Elsevier Publishing Co., Amsterdam, The Netherlands.
    • (1996) Biochemistry of Lipids, Lipoproteins and Membranes , vol.31 , pp. 35-74
    • Rock, C.O.1    Jackowski, S.2    Cronan J.E., Jr.3
  • 26
    • 0001308238 scopus 로고
    • Preparation and assay of acetyl phosphate
    • Stadtman, E. R. 1955. Preparation and assay of acetyl phosphate. Methods Enzymol. 1:228-232.
    • (1955) Methods Enzymol. , vol.1 , pp. 228-232
    • Stadtman, E.R.1
  • 27
    • 0001308240 scopus 로고
    • Preparation and assay of acyl-coenzyme A and other thioesters; use of hydroxylamine
    • Stadtman, E. R. 1957. Preparation and assay of acyl-coenzyme A and other thioesters; use of hydroxylamine. Methods Enzymol. 3:931-941.
    • (1957) Methods Enzymol. , vol.3 , pp. 931-941
    • Stadtman, E.R.1
  • 29
    • 0031783528 scopus 로고    scopus 로고
    • Overproduction of a functional fatty acid biosynthetic enzyme blocks fatty acid synthesis in Escherichia coli
    • Subrahmanyam, S., and J. E. Cronan, Jr. 1998. Overproduction of a functional fatty acid biosynthetic enzyme blocks fatty acid synthesis in Escherichia coli. J. Biol. Chem. 180:4595-4602.
    • (1998) J. Biol. Chem. , vol.180 , pp. 4595-4602
    • Subrahmanyam, S.1    Cronan J.E., Jr.2
  • 31
    • 0026775039 scopus 로고
    • Isolation and characterization of the β-ketoacyl-acyl carrier protein synthase III gene (fabH) from Escherichia coli K-12
    • Tsay, J.-T., W. Oh, T. J. Larson, S. Jackowski, and C. O. Rock. 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
  • 32
    • 0001348712 scopus 로고    scopus 로고
    • Biosynthesis of the branched-chain amino acids
    • F. C. Neidhardt, R. Curtiss III, J. L. Ingraham, E. C. C. Lin, K. B. Low, B. Magasanik, W. S. Reznikoff, M. Schlechter, and H. E. Umbarger (ed.), American Society for Microbiology. Washington, D.C.
    • Umbarger, H. 1996. Biosynthesis of the branched-chain amino acids, p. 442-457. In F. C. Neidhardt, R. Curtiss III, J. L. Ingraham, E. C. C. Lin, K. B. Low, B. Magasanik, W. S. Reznikoff, M. Schlechter, and H. E. Umbarger (ed.), Escherichia coli and Salmonella: cellular and molecular biology, 2nd ed. American Society for Microbiology. Washington, D.C.
    • (1996) Escherichia Coli and Salmonella: Cellular and Molecular Biology, 2nd Ed. , pp. 442-457
    • Umbarger, H.1
  • 33
    • 0027288094 scopus 로고
    • The primary structure of branched-chain α-oxo acid dehydrogenase from Bacillus subtilis and its similarity to other α-oxo acid dehydrogenases
    • Wang, G.-F., T. Kuriki, K. L. Roy, and T. Kaneda. 1993. The primary structure of branched-chain α-oxo acid dehydrogenase from Bacillus subtilis and its similarity to other α-oxo acid dehydrogenases. Eur. J. Biochem. 213: 1091-1099.
    • (1993) Eur. J. Biochem. , vol.213 , pp. 1091-1099
    • Wang, G.-F.1    Kuriki, T.2    Roy, K.L.3    Kaneda, T.4
  • 34
    • 0015218647 scopus 로고
    • Fatty acid-requirement mutant of Bacillus sublilis defective in branched chain α-keto acid dehydrogenase
    • Willecke, K., and A. B. Pardee. 1971. Fatty acid-requirement mutant of Bacillus sublilis defective in branched chain α-keto acid dehydrogenase. J. Biol. Chem. 246:5261-5272.
    • (1971) J. Biol. Chem. , vol.246 , pp. 5261-5272
    • Willecke, K.1    Pardee, A.B.2


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