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Volumn 271, Issue 23-24, 2004, Pages 4769-4778

Escherichia coli cyclopropane fatty acid synthase: Mechanistic and site-directed mutagenetic studies

Author keywords

Chemical modification; Cyclopropane fatty acid synthase; Enzymatic reaction mechanism; Hydrogen isotope exchange; Site directed mutagenesis

Indexed keywords

5,5' DITHIOBIS(2 NITROBENZOIC ACID); CYCLOPROPANE; FATTY ACID SYNTHASE; RECOMBINANT ENZYME;

EID: 11244252157     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1432-1033.2004.04441.x     Document Type: Article
Times cited : (25)

References (40)
  • 1
    • 0031457094 scopus 로고    scopus 로고
    • Cyclopropane ring formation in membrane lipids of bacteria
    • Grogan, D.W. & Cronan, J.E. (1997) Cyclopropane ring formation in membrane lipids of bacteria. Microbiol. Mol. Biol. Rev. 61, 429-441.
    • (1997) Microbiol. Mol. Biol. Rev. , vol.61 , pp. 429-441
    • Grogan, D.W.1    Cronan, J.E.2
  • 2
    • 0037076436 scopus 로고    scopus 로고
    • Carbocyclic fatty-acids in plants: Biochemical and molecular genetic characterization of cyclopropane fatty acid synthesis of Sterculia foetida
    • Bao, X., Katz, S., Pollard, M. & Ohlrogges, J.B. (2002) Carbocyclic fatty-acids in plants: Biochemical and molecular genetic characterization of cyclopropane fatty acid synthesis of Sterculia foetida. Proc. Natl Acad. Sci. USA 99, 7172-7177.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 7172-7177
    • Bao, X.1    Katz, S.2    Pollard, M.3    Ohlrogges, J.B.4
  • 3
    • 0038305971 scopus 로고    scopus 로고
    • Characterization of cyclopropane fatty-acid synthase from Sterculia foetida
    • Bao, X., Thelen, J.J., Bonaventure, G. & Ohlrogges, J.B. (2003) Characterization of cyclopropane fatty-acid synthase from Sterculia foetida. J. Biol. Chem. 278, 12846-12853.
    • (2003) J. Biol. Chem. , vol.278 , pp. 12846-12853
    • Bao, X.1    Thelen, J.J.2    Bonaventure, G.3    Ohlrogges, J.B.4
  • 4
    • 0023729076 scopus 로고
    • Effects of sulfur-containing analogues of stearic acid on growth and fatty acid biosynthesis in the protozoan Crithidia fasciculata
    • Rahman, M.D., Ziering, D.L., Mannarelli, S.J., Swartz, K.L. & Huang, D. (1988) Effects of sulfur-containing analogues of stearic acid on growth and fatty acid biosynthesis in the protozoan Crithidia fasciculata. J. Med. Chem. 31, 1656-1659.
    • (1988) J. Med. Chem. , vol.31 , pp. 1656-1659
    • Rahman, M.D.1    Ziering, D.L.2    Mannarelli, S.J.3    Swartz, K.L.4    Huang, D.5
  • 5
    • 0016161619 scopus 로고
    • Studies on the biosynthesis of cyclopropane fatty acids in Escherichia coli
    • Cronan, J.E., Nunn, W.D. & Batchelor, J.G. (1974) Studies on the biosynthesis of cyclopropane fatty acids in Escherichia coli. Biochimica Biophysica Acta 348, 63-75.
    • (1974) Biochimica Biophysica Acta , vol.348 , pp. 63-75
    • Cronan, J.E.1    Nunn, W.D.2    Batchelor, J.G.3
  • 6
    • 0018416481 scopus 로고
    • Cyclopropane fatty acid synthase of Escherichia coli. Stabilization, purification, and interaction with phospholipid vesicles
    • Taylor, F.R. & Cronan. I.E. (1979) Cyclopropane fatty acid synthase of Escherichia coli. Stabilization, purification, and interaction with phospholipid vesicles. Biochemistry 18, 3292-3300.
    • (1979) Biochemistry , vol.18 , pp. 3292-3300
    • Taylor, F.R.1    Cronan, I.E.2
  • 7
    • 0019343650 scopus 로고
    • Cyclopropane fatty acid synthase from Escherichia coli
    • Taylor, F.R., Grogan, D.W. & Cronan. I.E. (1981) Cyclopropane fatty acid synthase from Escherichia coli. Methods Enzymol. 71, 133-139.
    • (1981) Methods Enzymol. , vol.71 , pp. 133-139
    • Taylor, F.R.1    Grogan, D.W.2    Cronan, I.E.3
  • 8
    • 0021271149 scopus 로고
    • Cloning and manipulation of the Escherichia coli cyclopropane fatty acid synthase gene: Physiological aspects of enzyme overproduction
    • Grogan, D.W. & Cronan. J.E. (1984) Cloning and manipulation of the Escherichia coli cyclopropane fatty acid synthase gene: physiological aspects of enzyme overproduction. J. Bacteriol. 158, 286-295.
    • (1984) J. Bacteriol. , vol.158 , pp. 286-295
    • Grogan, D.W.1    Cronan, J.E.2
  • 9
    • 0026447153 scopus 로고
    • Cyclopropane fatty acid synthase of Escherichia coli: Deduced amino acid sequence, purification, and studies of the enzyme active site
    • Wang, A., Grogan, D.W. & Cronan, J.E. (1992) Cyclopropane fatty acid synthase of Escherichia coli: deduced amino acid sequence, purification, and studies of the enzyme active site. Biochemistry 31, 11020-11028.
    • (1992) Biochemistry , vol.31 , pp. 11020-11028
    • Wang, A.1    Grogan, D.W.2    Cronan, J.E.3
  • 11
    • 0033634971 scopus 로고    scopus 로고
    • A novel mycolic acid cyclopropane synthetase is required for cording, persistance, and virulence of Mycobacterium tuberculosis
    • Glickman, M.S., Cox, J.S. & Jacobs, W.R. (2000) A novel mycolic acid cyclopropane synthetase is required for cording, persistance, and virulence of Mycobacterium tuberculosis. Mol. Cell. 5, 717-727.
    • (2000) Mol. Cell , vol.5 , pp. 717-727
    • Glickman, M.S.1    Cox, J.S.2    Jacobs, W.R.3
  • 12
    • 0038182191 scopus 로고    scopus 로고
    • The TB epidemic from 1992 to 2002
    • Raviglione, M.C. (2003) The TB epidemic from 1992 to 2002. Tuberculosis 83, 4-14.
    • (2003) Tuberculosis , vol.83 , pp. 4-14
    • Raviglione, M.C.1
  • 13
    • 17644448251 scopus 로고    scopus 로고
    • Synthesis and evaluation of analogues of 5-adenosyl-1-methionine, as inhibitors of the E. coli cyclopropane fatty acid synthase
    • Guérard, C., Bréard, M., Courtois, F., Drujon, T. & Ploux, O. (2004) Synthesis and evaluation of analogues of 5-adenosyl-1- methionine, as inhibitors of the E. coli cyclopropane fatty acid synthase. Bioorg Med. Chem. Lett. 14, 1661-1664.
    • (2004) Bioorg Med. Chem. Lett. , vol.14 , pp. 1661-1664
    • Guérard, C.1    Bréard, M.2    Courtois, F.3    Drujon, T.4    Ploux, O.5
  • 14
    • 50549195905 scopus 로고
    • The path of hydrogen in the formation of cyclopropane fatty acids
    • Pohl, S., Law, J.H. & Ryhage, R. (1963) The path of hydrogen in the formation of cyclopropane fatty acids. Biochem. Biophys. Acta 70, 583-585.
    • (1963) Biochem. Biophys. Acta , vol.70 , pp. 583-585
    • Pohl, S.1    Law, J.H.2    Ryhage, R.3
  • 15
    • 0014027829 scopus 로고
    • Biosynthesis of cyclopropane compounds
    • Polacheck, J.W., Tropp, B.E. & Law, J.H. (1966) Biosynthesis of cyclopropane compounds. J. Biol. Chem. 241, 3362-3364.
    • (1966) J. Biol. Chem. , vol.241 , pp. 3362-3364
    • Polacheck, J.W.1    Tropp, B.E.2    Law, J.H.3
  • 16
    • 33947292670 scopus 로고
    • Biosynthesis of cyclopropane rings
    • Law, J.H. (1971) Biosynthesis of cyclopropane rings. Acc. Chem. Res. 4, 199-203.
    • (1971) Acc. Chem. Res. , vol.4 , pp. 199-203
    • Law, J.H.1
  • 18
    • 0038277681 scopus 로고
    • The biosynthesis of cyclopropane faty acids. II. Mechanistic studies using methionine labelled with one, two, and three deuterium atoms in the methyl group
    • Buist, P.H. & MacLean, D.B. (1980) The biosynthesis of cyclopropane faty acids. II. Mechanistic studies using methionine labelled with one, two, and three deuterium atoms in the methyl group. Can. J. Chem. 60, 371-378.
    • (1980) Can. J. Chem. , vol.60 , pp. 371-378
    • Buist, P.H.1    MacLean, D.B.2
  • 19
    • 11244279781 scopus 로고
    • Stereochemische untersuchungen von biologischen alkylierungsreactionen
    • Arigoni, D. (1987) Stereochemische Untersuchungen von biologischen Alkylierungsreactionen. Chimia 41, 188-189.
    • (1987) Chimia , vol.41 , pp. 188-189
    • Arigoni, D.1
  • 20
    • 0001157254 scopus 로고
    • Some problems containing biological c-alkylation reactions and phytosterol biosynthesis
    • Lederer, E. (1969) Some problems containing biological c-alkylation reactions and phytosterol biosynthesis. Q. Rev. Chem. Soc. 23, 453-181.
    • (1969) Q. Rev. Chem. Soc. , vol.23 , pp. 453-181
    • Lederer, E.1
  • 21
    • 0001720546 scopus 로고
    • A laboratory model for the biosynthesis of cyclopropane rings. Copper-catalyzed cyclopropanation of olefins by sulfur ylides
    • Cohen, T., Herman, G., Chapman, T.M. & Kuhn, D. (1974) A laboratory model for the biosynthesis of cyclopropane rings. Copper-catalyzed cyclopropanation of olefins by sulfur ylides. J. Am. Chem. Soc. 96, 5627-5628.
    • (1974) J. Am. Chem. Soc. , vol.96 , pp. 5627-5628
    • Cohen, T.1    Herman, G.2    Chapman, T.M.3    Kuhn, D.4
  • 22
    • 0037192859 scopus 로고    scopus 로고
    • Crystal structures of mycolic acid cyclopropane synthases from Mycobacterium tuberculosis
    • Huang, C., Smith, V., Glickman, M.S., Jacobs, W.R. & Sacchettini, J.C. (2002) Crystal structures of mycolic acid cyclopropane synthases from Mycobacterium tuberculosis. J. Biol. Chem. 277, 11559-11569.
    • (2002) J. Biol. Chem. , vol.277 , pp. 11559-11569
    • Huang, C.1    Smith, V.2    Glickman, M.S.3    Jacobs, W.R.4    Sacchettini, J.C.5
  • 23
    • 0000821323 scopus 로고
    • An unexpected reversal of fluorine substituent effects in the biomethylenation of two positional isomers: A serendipitous discovery
    • Buist, P.H. & Pon, R.A. (1990) An unexpected reversal of fluorine substituent effects in the biomethylenation of two positional isomers: a serendipitous discovery. J. Org. Chem. 55, 6240-6241.
    • (1990) J. Org. Chem. , vol.55 , pp. 6240-6241
    • Buist, P.H.1    Pon, R.A.2
  • 24
    • 0347417961 scopus 로고    scopus 로고
    • Cyclopropane fatty acid synthase from Escherichia coli. Enzyme purification and inhibition by vinylfluorine and epoxide-containing substrate analogues
    • Molitor, E.J., Paschal, B.M. & Liu, H.-W. (2003) Cyclopropane fatty acid synthase from Escherichia coli. Enzyme purification and inhibition by vinylfluorine and epoxide-containing substrate analogues. Chembiochem. 4, 1352-1356.
    • (2003) Chembiochem , vol.4 , pp. 1352-1356
    • Molitor, E.J.1    Paschal, B.M.2    Liu, H.-W.3
  • 25
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M.M. (1976) A rapid and sensitive method for the 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
  • 26
    • 0014262615 scopus 로고
    • Lipids of Salmonella typhimurium and Escherichia coli: Structure and metabolism
    • Ames, G.F. (1968) Lipids of Salmonella typhimurium and Escherichia coli: structure and metabolism. J. Bacteriol. 95, 833-843.
    • (1968) J. Bacteriol. , vol.95 , pp. 833-843
    • Ames, G.F.1
  • 27
    • 77957002474 scopus 로고
    • Quantitative and qualiative analysis of lipids and lipid components
    • Dittmer, J.C. & Wells, M.A. (1969) Quantitative and qualiative analysis of lipids and lipid components. Methods Enzymol. 14, 482-530.
    • (1969) Methods Enzymol. , vol.14 , pp. 482-530
    • Dittmer, J.C.1    Wells, M.A.2
  • 28
    • 0035180468 scopus 로고    scopus 로고
    • Expression, purification, crystallization and preliminary X-ray analysis of Escherichia coli 5′-methylthioadenosine/S-adenosylhomocysteine nucleosidase
    • Lee, J.E., Cornell, K.A., Riscoe, M.K. & Howell, P.L. (2001) Expression, purification, crystallization and preliminary X-ray analysis of Escherichia coli 5′-methylthioadenosine/S-adenosylhomocysteine nucleosidase. Acta Crystallogr. D Biol. Crystallogr. 57, 150-152.
    • (2001) Acta Crystallogr. D Biol. Crystallogr. , vol.57 , pp. 150-152
    • Lee, J.E.1    Cornell, K.A.2    Riscoe, M.K.3    Howell, P.L.4
  • 30
    • 0001078895 scopus 로고
    • Relation between modification of functional groups of proteins and their biological activity
    • Tsou, C. (1962) Relation between modification of functional groups of proteins and their biological activity. Sci. Sin. 11, 1535-1558.
    • (1962) Sci. Sin. , vol.11 , pp. 1535-1558
    • Tsou, C.1
  • 31
    • 0025216076 scopus 로고
    • Overproduction and dissection of proteins by the expression-cassette polymerase chain reaction
    • MacFerrin, K.D., Terranova, M.P., Schreiber, S.L. & Verdine, G.L. (1990) Overproduction and dissection of proteins by the expression-cassette polymerase chain reaction. Proc. Natl Acad. Sci. USA 87, 1937-1941.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 1937-1941
    • MacFerrin, K.D.1    Terranova, M.P.2    Schreiber, S.L.3    Verdine, G.L.4
  • 32
    • 0028986132 scopus 로고
    • Mechanistic studies on CDP-6-deoxy-A-3,4-glucoseen reductase: The role of cysteine residues in catalysis as probed by chemical modification and site-directed mutagenesis
    • Ploux, O., Lei, Y., Vatanen, K. & Liu, H.-W. (1995) Mechanistic studies on CDP-6-deoxy-A-3,4-glucoseen reductase: The role of cysteine residues in catalysis as probed by chemical modification and site-directed mutagenesis. Biochemistry 34, 4159-4168.
    • (1995) Biochemistry , vol.34 , pp. 4159-4168
    • Ploux, O.1    Lei, Y.2    Vatanen, K.3    Liu, H.-W.4
  • 33
    • 0000470204 scopus 로고
    • Biochemistry of the cyclopropyl group
    • (Rappoport, Z., ed.). J. Wiley and Sons, NY
    • Liu, H.-W. & Walsh, C.T. (1987) Biochemistry of the cyclopropyl group. In The Chemistry of the Cyclopropyl Group (Rappoport, Z., ed.), pp. 959-1025. J. Wiley and Sons, NY.
    • (1987) The Chemistry of the Cyclopropyl Group , pp. 959-1025
    • Liu, H.-W.1    Walsh, C.T.2
  • 34
    • 0037547123 scopus 로고    scopus 로고
    • Introduction: Cyclopropanes and related rings
    • De Meijere, A. (2003) Introduction: cyclopropanes and related rings. Chem. Rev. 103, 931-932.
    • (2003) Chem. Rev. , vol.103 , pp. 931-932
    • De Meijere, A.1
  • 35
    • 0029803546 scopus 로고    scopus 로고
    • A common mechanism for the biosynthesis of methoxy and cyclopropyl mycolic acids in Mycobacterium tuberculosis
    • Yuan, Y. & Barry, C.E. (1996) A common mechanism for the biosynthesis of methoxy and cyclopropyl mycolic acids in Mycobacterium tuberculosis. Proc. Natl Acad. Sci. USA 93, 12828-12833.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 12828-12833
    • Yuan, Y.1    Barry, C.E.2
  • 37
    • 11244347706 scopus 로고
    • Enzyme-catalysed Claisen condensation
    • W.H. Freeman, New York
    • Walsh, C.T. (1979) Enzyme-catalysed Claisen condensation. In Enzymatic Reaction Mechanisms, pp. 759-763. W.H. Freeman, New York.
    • (1979) Enzymatic Reaction Mechanisms , pp. 759-763
    • Walsh, C.T.1
  • 38
    • 0029035664 scopus 로고
    • Cytosine methyltransferase from Escherichia coli in which active site cysteine is replaced with serine is partially active
    • Gabbara, S., Sheluho, D. & Bhagwat, A.S. (1995) Cytosine methyltransferase from Escherichia coli in which active site cysteine is replaced with serine is partially active. Biochemistry 34, 8914-8923.
    • (1995) Biochemistry , vol.34 , pp. 8914-8923
    • Gabbara, S.1    Sheluho, D.2    Bhagwat, A.S.3
  • 39
    • 0033616629 scopus 로고    scopus 로고
    • Catalytic acid/base residues of glutamate racemase
    • Glavas, S. & Tanner, M.E. (1999) Catalytic acid/base residues of glutamate racemase. Biochemistry 38, 4106-4113.
    • (1999) Biochemistry , vol.38 , pp. 4106-4113
    • Glavas, S.1    Tanner, M.E.2
  • 40
    • 0034725413 scopus 로고    scopus 로고
    • Identification of active site cysteine residues that function as general bases: Diaminopimelate epimerase
    • Koo, C.W., Sutherland, A., Vederas, J.C. & Blanchard, J.S. (2000) Identification of active site cysteine residues that function as general bases: diaminopimelate epimerase. J. Am. Chem. Soc. 122, 6122-6123.
    • (2000) J. Am. Chem. Soc. , vol.122 , pp. 6122-6123
    • Koo, C.W.1    Sutherland, A.2    Vederas, J.C.3    Blanchard, J.S.4


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