메뉴 건너뛰기




Volumn 242, Issue 3, 1996, Pages 689-694

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

Author keywords

Enoyl acyl carrier protein reductase (FabI); Escherichia coli; Fatty acid biosynthesis; Palmitoyl CoA inhibition

Indexed keywords

ACYL CARRIER PROTEIN; OXIDOREDUCTASE; PALMITOYL COENZYME A;

EID: 0030431493     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1432-1033.1996.0689r.x     Document Type: Article
Times cited : (138)

References (28)
  • 2
    • 0014429312 scopus 로고
    • Studies on the mechanism of fatty acid synthesis
    • Weeks, G. & Wakil, S. J. (1968) Studies on the mechanism of fatty acid synthesis, J. Biol. Chem. 243, 1180-1189.
    • (1968) J. Biol. Chem. , vol.243 , pp. 1180-1189
    • Weeks, G.1    Wakil, S.J.2
  • 3
    • 0019410554 scopus 로고
    • Steric course of reaction catalyzed by the enoyl acyl-carrier-protein reductase of Escherichia coli
    • Saito, K., Kawaguchi, A., Seyama, Y., Yamakawa, T. & Okuda, S. (1981) Steric course of reaction catalyzed by the enoyl acyl-carrier-protein reductase of Escherichia coli, Eur. J. Biochem. 116, 581-586.
    • (1981) Eur. J. Biochem. , vol.116 , pp. 581-586
    • Saito, K.1    Kawaguchi, A.2    Seyama, Y.3    Yamakawa, T.4    Okuda, S.5
  • 4
    • 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, M. M., Konigstein, G. M., Nijkamp, H. J. J. & Stuitje, A. R. (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    Konigstein, G.M.2    Nijkamp, H.J.J.3    Stuitje, A.R.4
  • 5
    • 0030033704 scopus 로고    scopus 로고
    • Regulation of fatty acid elongation and initiation by acyl-acyl carrier protein in Escherichia coli
    • Heath, R. J. & Rock, C. O. (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
  • 7
    • 0024331888 scopus 로고
    • envM genes of Salmonella typhimurium and Escherichia coli
    • Turnowsky, F., Fuchs, K., Jeschek, C. & Högenauer, 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    Högenauer, G.4
  • 8
    • 0026713759 scopus 로고
    • Sequences of the envM gene and two mutated alleles in Escherichia coli
    • Bergler, H., Högenauer, G. & Turnowsky, F. (1992) Sequences of the envM gene and two mutated alleles in Escherichia coli, J. Gen. Microbiol. 138, 2093-2100.
    • (1992) J. Gen. Microbiol. , vol.138 , pp. 2093-2100
    • Bergler, H.1    Högenauer, G.2    Turnowsky, F.3
  • 9
    • 0028855972 scopus 로고
    • Enoyl-acyl carrier protein reductase (fabI) plays a determinant role in completing cycles of fatty acid elongation in Escherichia coli
    • Heath, R. J. & Rock, C. O. (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
  • 10
    • 0021138754 scopus 로고
    • Preparation and antibacterial activities of new 1,2,3-diazaborine derivatives and analogues
    • Grassberger, M. A., Turnowsky, F. & Hildebrand, J. (1984) Preparation and antibacterial activities of new 1,2,3-diazaborine derivatives and analogues, J. Med. Chem. 27, 947-953.
    • (1984) J. Med. Chem. , vol.27 , pp. 947-953
    • Grassberger, M.A.1    Turnowsky, F.2    Hildebrand, J.3
  • 11
    • 0025855940 scopus 로고
    • In vivo degradation of secreted fusion proteins by the Escherichia coli outer membrane protease OmpT
    • Baneyx, F. & Georgiou, G. (1991) In vivo degradation of secreted fusion proteins by the Escherichia coli outer membrane protease OmpT, J. Bacteriol. 173, 2696-2703.
    • (1991) J. Bacteriol. , vol.173 , pp. 2696-2703
    • Baneyx, F.1    Georgiou, G.2
  • 12
    • 0015903663 scopus 로고
    • Conditional mutations affecting the cell envelope of Escherichia coli K-12
    • Egan, A. F. & Russell, R. R. B. (1973) Conditional mutations affecting the cell envelope of Escherichia coli K-12, Genet. Res. 21, 139-152.
    • (1973) Genet. Res. , vol.21 , pp. 139-152
    • Egan, A.F.1    Russell, R.R.B.2
  • 16
    • 0025947274 scopus 로고
    • 3/methanol transesterification of lyophilized samples instead of Folch extraction gives higher yields
    • 3/methanol transesterification of lyophilized samples instead of Folch extraction gives higher yields, Anal. Biochem. 198, 184-190.
    • (1991) Anal. Biochem. , vol.198 , pp. 184-190
    • Sattler, W.1    Puhl, H.2    Hayn, M.3    Kostner, G.M.4    Esterbauer, H.5
  • 17
    • 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, J. E. 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 Jr., J.E.2
  • 18
    • 0029045836 scopus 로고
    • Regulation of malonyl-CoA metabolism by acyl-acyl carrier protein and β-ketoacyl-acyl carrier protein synthases in Escherichia coli
    • Heath, R. J. & Rock, C. O. (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
  • 19
    • 0029645410 scopus 로고
    • Common themes in redox chemistry emerge from the X-ray structure of oilseed rape (Brassica napus) enoyl acyl carrier protein reductase
    • Rafferty, J. B., Simon, J. W., Baldock, C., Artymiuk, P. J., Baker, P. J., Stuitje, A. R., Slabas, A. R. & Rice, D. W. (1995) Common themes in redox chemistry emerge from the X-ray structure of oilseed rape (Brassica napus) enoyl acyl carrier protein reductase, Structure 3, 927-938.
    • (1995) Structure , vol.3 , pp. 927-938
    • Rafferty, J.B.1    Simon, J.W.2    Baldock, C.3    Artymiuk, P.J.4    Baker, P.J.5    Stuitje, A.R.6    Slabas, A.R.7    Rice, D.W.8
  • 20
    • 0028073290 scopus 로고
    • Adding a positive charge at residue 46 of Drosophila alcohol dehydrogenase increases cofactor specificity for NADP
    • Chen, Z., Tsigelny, I., Lee, W. R., Baker, M. E. & Chang, S. H. (1994) Adding a positive charge at residue 46 of Drosophila alcohol dehydrogenase increases cofactor specificity for NADP, FEBS Lett. 356, 81-85.
    • (1994) FEBS Lett. , vol.356 , pp. 81-85
    • Chen, Z.1    Tsigelny, I.2    Lee, W.R.3    Baker, M.E.4    Chang, S.H.5
  • 21
    • 0025019734 scopus 로고
    • Redesign of the coenzyme specificity of a dehydrogenase by protein engineering
    • Scrutton, N. S., Berry, A. & Perham, R. N. (1990) Redesign of the coenzyme specificity of a dehydrogenase by protein engineering, Nature 343, 38-43.
    • (1990) Nature , vol.343 , pp. 38-43
    • Scrutton, N.S.1    Berry, A.2    Perham, R.N.3
  • 22
    • 0025867105 scopus 로고
    • An aspartate residue in yeast alcohol dehydrogenase 1 determines the specificity for coenzyme
    • Fan, F., Lorenzen, J. A. & Plapp, B. V. (1991) An aspartate residue in yeast alcohol dehydrogenase 1 determines the specificity for coenzyme, Biochemistry 30, 6397-6401.
    • (1991) Biochemistry , vol.30 , pp. 6397-6401
    • Fan, F.1    Lorenzen, J.A.2    Plapp, B.V.3
  • 23
    • 0028988237 scopus 로고
    • Crystal structure and function of the isoniazid target of Mycobacterium tuberculosis
    • Dessen, A., Quemard, A., Blanchard, J. S., Jacobs, W. R. Jr & Sacchettini, J. C. (1995) Crystal structure and function of the isoniazid target of Mycobacterium tuberculosis, Science 267, 1638-1641.
    • (1995) Science , vol.267 , pp. 1638-1641
    • Dessen, A.1    Quemard, A.2    Blanchard, J.S.3    Jacobs Jr., W.R.4    Sacchettini, J.C.5
  • 24
    • 0015057740 scopus 로고
    • Temperature control of phospholipid biosynthesis in Escherichia coli
    • Sinensky, M. (1971) Temperature control of phospholipid biosynthesis in Escherichia coli, J. Bacteriol. 106, 449-455.
    • (1971) J. Bacteriol. , vol.106 , pp. 449-455
    • Sinensky, M.1
  • 25
    • 0016817502 scopus 로고
    • Thermal regulation of the membrane lipid composition of Escherichia coli
    • Cronan, J. E. Jr (1975) Thermal regulation of the membrane lipid composition of Escherichia coli, J. Biol. Chem. 250, 7074-7077.
    • (1975) J. Biol. Chem. , vol.250 , pp. 7074-7077
    • Cronan Jr., J.E.1
  • 26
    • 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 As
    • DiRusso, C. C., Heimert, T. L. & Metzger, A. K. (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 As, 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
  • 27
    • 0001517649 scopus 로고    scopus 로고
    • Biosynthesis of membrane lipids
    • Neidhardt, F. C., ed. 2nd edn, ASM Press, Washington, DC
    • Cronan, J. E. Jr & Rock, C. O. (1996) Biosynthesis of membrane lipids, in Escherichia coli and Salmonella (Neidhardt, F. C., ed.) 2nd edn, pp. 612-636, ASM Press, Washington, DC.
    • (1996) Escherichia Coli and Salmonella , pp. 612-636
    • Cronan Jr., J.E.1    Rock, C.O.2
  • 28
    • 0030033704 scopus 로고    scopus 로고
    • Regulation of fatty acid elongation and initiation by acyl-acyl carrier protein in Escherichia coli
    • Heath, J. R. & Rock, C. O. (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, J.R.1    Rock, C.O.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.