메뉴 건너뛰기




Volumn 39, Issue 11, 2004, Pages 1055-1060

The reductase steps of the type II fatty acid synthase as antimicrobial targets

Author keywords

[No Author keywords available]

Indexed keywords

ANTIBIOTICS; BACTERIA; BIOCHEMISTRY; BIOSYNTHESIS; CRYSTAL STRUCTURE; GENES; PATHOLOGY;

EID: 12344300344     PISSN: 00244201     EISSN: None     Source Type: Journal    
DOI: 10.1007/s11745-004-1330-3     Document Type: Conference Paper
Times cited : (71)

References (47)
  • 1
    • 0001517649 scopus 로고    scopus 로고
    • Biosynthesis of Membrane Lipids
    • Neidhardt, F.C., Curtis, R., Gross, C.A., Ingraham, J.L., Lin, E.C.C., Low, K.B., Magasanik, B., Reznikoff, W., Riley, M., Schaechter, M., and Umbarger, H.E., eds., American Society for Microbiology, Washington, D.C.
    • Cronan, J.E., Jr., and Rock, C.O. (1996) Biosynthesis of Membrane Lipids, in Escherichia coli and Salmonella typhimurium: Cellular and Molecular Biology (Neidhardt, F.C., Curtis, R., Gross, C.A., Ingraham, J.L., Lin, E.C.C., Low, K.B., Magasanik, B., Reznikoff, W., Riley, M., Schaechter, M., and Umbarger, H.E., eds.), pp. 612-636, American Society for Microbiology, Washington, D.C.
    • (1996) Escherichia Coli and Salmonella Typhimurium: Cellular and Molecular Biology , pp. 612-636
    • Cronan Jr., J.E.1    Rock, C.O.2
  • 2
    • 0030581109 scopus 로고    scopus 로고
    • Escherichia coli as a Model for the Regulation of Dissociable (Type II) FA Biosynthesis
    • Rock, C.O., and Cronan, J.E., Jr. (1996) Escherichia coli as a Model for the Regulation of Dissociable (Type II) FA Biosynthesis, Biochim. Biophys. Acta 1302, 1-16.
    • (1996) Biochim. Biophys. Acta , vol.1302 , pp. 1-16
    • Rock, C.O.1    Cronan Jr., J.E.2
  • 4
    • 3042764816 scopus 로고    scopus 로고
    • FA Biosynthesis as a Target for Novel Antibacterials
    • Heath, R.J., and Rock, C.O. (2004) FA Biosynthesis as a Target for Novel Antibacterials, Curr. Opin. Investig. Drugs 5, 146-153.
    • (2004) Curr. Opin. Investig. Drugs , vol.5 , pp. 146-153
    • Heath, R.J.1    Rock, C.O.2
  • 5
    • 0034804919 scopus 로고    scopus 로고
    • Lipid Biosynthesis as a Target for Antibacterial Agents
    • Heath, R.J., White, S.W., and Rock, C.O. (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
  • 6
    • 0034780806 scopus 로고    scopus 로고
    • Bacterial FA Biosynthesis: Targets for Antibacterial Drug Discovery
    • Campbell, J.W., and Cronan, J.E., Jr. (2001) Bacterial FA Biosynthesis: Targets for Antibacterial Drug Discovery, Annu. Rev. Microbiol. 55, 305-332.
    • (2001) Annu. Rev. Microbiol. , vol.55 , pp. 305-332
    • Campbell, J.W.1    Cronan Jr., J.E.2
  • 8
    • 0032515066 scopus 로고    scopus 로고
    • Broad Spectrum Antimicrobial Biocides Target the FabI Component of FA Synthesis
    • Heath, R.J., Yu, Y.-T., Shapiro, M.A., Olson, E., and Rock, C.O. (1998) Broad Spectrum Antimicrobial Biocides Target the FabI Component of FA Synthesis, J. Biol. Chem. 273, 30316-30321.
    • (1998) J. Biol. Chem. , vol.273 , pp. 30316-30321
    • Heath, R.J.1    Yu, Y.-T.2    Shapiro, M.A.3    Olson, E.4    Rock, C.O.5
  • 10
    • 0021744394 scopus 로고
    • Inhibition of FA Synthesis by the Antibiotic Thiolactomycin
    • Hayashi, T., Yamamoto, O., Sasaki, H., and Okazaki, H. (1984) Inhibition of FA Synthesis by the Antibiotic Thiolactomycin, J. Antibiot. (Tokyo) 37, 1456-1461.
    • (1984) J. Antibiot. (Tokyo) , vol.37 , pp. 1456-1461
    • Hayashi, T.1    Yamamoto, O.2    Sasaki, H.3    Okazaki, H.4
  • 13
    • 0035126479 scopus 로고    scopus 로고
    • Triclosan Offers Protection Against Blood Stages of Malaria by Inhibiting Enoyl-ACP Reductase of Plasmodium falciparum
    • Surolia, N., and Surolia, A. (2001) Triclosan Offers Protection Against Blood Stages of Malaria by Inhibiting Enoyl-ACP Reductase of Plasmodium falciparum, Nat. Med. 7, 167-173.
    • (2001) Nat. Med. , vol.7 , pp. 167-173
    • Surolia, N.1    Surolia, A.2
  • 15
    • 0028855972 scopus 로고
    • Enoyl-acyl Carrier Protein Reductase (fabI) Plays a Determinant Role in Completing Cycles of FA Elongation in Escherichia coli
    • Heath, R.J., and Rock, C.O. (1995) Enoyl-acyl Carrier Protein Reductase (fabI) Plays a Determinant Role in Completing Cycles of FA 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
  • 16
    • 0024331888 scopus 로고
    • envM Genes of Salmonella typhimurium and Escherichia coli
    • Turnowsky, F., Fuchs, K., Jeschek, C., and 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
  • 17
    • 0034681329 scopus 로고    scopus 로고
    • Inhibition of the Staphylococcus aureus NADPH-Dependent Enoyl-acyl Carrier Protein Reductase by Triclosan and Hexachlorophene
    • Heath, R.J., Li, J., Roland, G.E., and Rock, C.O. (2000) Inhibition of the Staphylococcus aureus NADPH-Dependent Enoyl-acyl Carrier Protein Reductase by Triclosan and Hexachlorophene, J. Biol. Chem. 275, 4654-4659.
    • (2000) J. Biol. Chem. , vol.275 , pp. 4654-4659
    • Heath, R.J.1    Li, J.2    Roland, G.E.3    Rock, C.O.4
  • 18
    • 0034644010 scopus 로고    scopus 로고
    • A Triclosan-Resistant Bacterial Enzyme
    • Heath, R.J., and Rock, C.O. (2000) A Triclosan-Resistant Bacterial Enzyme, Nature (London) 406, 145-146.
    • (2000) Nature (London) , vol.406 , pp. 145-146
    • Heath, R.J.1    Rock, C.O.2
  • 20
    • 0034704090 scopus 로고    scopus 로고
    • The Enoyl-[Acyl-Carrier-Protein] Reductases FabI and FabL from Bacillus subtilis
    • Heath, R.J., Su, N., Murphy, C.K., and Rock, C.O. (2000) The Enoyl-[Acyl-Carrier-Protein] Reductases FabI and FabL from Bacillus subtilis, J. Biol. Chem. 275, 40128-40133.
    • (2000) J. Biol. Chem. , vol.275 , pp. 40128-40133
    • Heath, R.J.1    Su, N.2    Murphy, C.K.3    Rock, C.O.4
  • 21
    • 0028988237 scopus 로고
    • Crystal Structure and Function of the Isoniazid Target of Mycobacterium tuberculosis
    • Dessen, A., Quémard, A., Blanchard, J.S., Jacobs, W.R., Jr., and 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    Quémard, A.2    Blanchard, J.S.3    Jacobs Jr., W.R.4    Sacchettini, J.C.5
  • 23
    • 0032775211 scopus 로고    scopus 로고
    • Structural Basis and Mechanism of Enoyl Reductase Inhibition by Triclosan
    • Stewart, M.J., Parikh, S., Xiao, G., Tonge, P.J., and Kisker, C. (1999) Structural Basis and Mechanism of Enoyl Reductase Inhibition by Triclosan, J. Mol. Biol. 290, 859-865.
    • (1999) J. Mol. Biol. , vol.290 , pp. 859-865
    • Stewart, M.J.1    Parikh, S.2    Xiao, G.3    Tonge, P.J.4    Kisker, C.5
  • 25
    • 0037461276 scopus 로고    scopus 로고
    • Structure-Activity Studies of the Inhibition of FabI, the Enoyl Reductase from Escherichia coli, by Triclosan: Kinetic Analysis of Mutant FabIs
    • Sivaraman, S., Zwahlen, J., Bell, A.F., Hedstrom, L., and Tonge, P.J. (2003) Structure-Activity Studies of the Inhibition of FabI, the Enoyl Reductase from Escherichia coli, by Triclosan: Kinetic Analysis of Mutant FabIs, Biochemistry 42, 4406-4413.
    • (2003) Biochemistry , vol.42 , pp. 4406-4413
    • Sivaraman, S.1    Zwahlen, J.2    Bell, A.F.3    Hedstrom, L.4    Tonge, P.J.5
  • 26
    • 0345133299 scopus 로고    scopus 로고
    • The Isoniazid-NAD Adduct Is a Slow, Tight-Binding Inhibitor of InhA, the Mycobacterium tuberculosis Enoyl Reductase: Adduct Affinity and Drug Resistance
    • Rawat, R., Whitty, A., and Tonge, P.J. (2003) The Isoniazid-NAD Adduct Is a Slow, Tight-Binding Inhibitor of InhA, the Mycobacterium tuberculosis Enoyl Reductase: Adduct Affinity and Drug Resistance, Proc. Natl. Acad. Sci. USA 100, 13881-13886.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 13881-13886
    • Rawat, R.1    Whitty, A.2    Tonge, P.J.3
  • 27
    • 0033055847 scopus 로고    scopus 로고
    • Genetic Evidence that InhA of Mycobacterium smegmatis Is a Target for Triclosan
    • McMurry, L.M., McDermott, P.F., and Levy, S.B. (1999) Genetic Evidence that InhA of Mycobacterium smegmatis Is a Target for Triclosan, Antimicrob. Agents Chemother. 43, 711-713.
    • (1999) Antimicrob. Agents Chemother. , vol.43 , pp. 711-713
    • McMurry, L.M.1    McDermott, P.F.2    Levy, S.B.3
  • 28
    • 0037066782 scopus 로고    scopus 로고
    • Structural Elucidation of the Specificity of the Antibacterial Agent Triclosan for Malarial Enoyl Acyl Carrier Protein Reductase
    • Perozzo, R., Kuo, M., Sidhu, A.S., Valiyaveettil, J.T., Bittman, R., Jacobs, W.R., Jr., Fidock, D.A., and Sacchettini, J.C. (2002) Structural Elucidation of the Specificity of the Antibacterial Agent Triclosan for Malarial Enoyl Acyl Carrier Protein Reductase, J. Biol. Chem. 277, 13106-13114.
    • (2002) J. Biol. Chem. , vol.277 , pp. 13106-13114
    • Perozzo, R.1    Kuo, M.2    Sidhu, A.S.3    Valiyaveettil, J.T.4    Bittman, R.5    Jacobs Jr., W.R.6    Fidock, D.A.7    Sacchettini, J.C.8
  • 29
    • 0035861962 scopus 로고    scopus 로고
    • Kinetic Determinants of the Interaction of Enoyl-ACP Reductase from Plasmodium falciparum with Its Substrates and Inhibitors
    • Kapoor, M., Dar, M.J., Surolia, A., and Surolia, N. (2001) Kinetic Determinants of the Interaction of Enoyl-ACP Reductase from Plasmodium falciparum with Its Substrates and Inhibitors, Biochem. Biophys. Res. Commun. 289, 832-837.
    • (2001) Biochem. Biophys. Res. Commun. , vol.289 , pp. 832-837
    • Kapoor, M.1    Dar, M.J.2    Surolia, A.3    Surolia, N.4
  • 30
    • 1642540581 scopus 로고    scopus 로고
    • Inhibition of the Bacterial Enoyl Reductase FabI by Triclosan: A Structure-Reactivity Analysis of FabI Inhibition by Triclosan Analogues
    • Sivaraman, S., Sullivan, T.J., Johnson, F., Novichenok, P., Cui, G., Simmerling, C., and Tonge, P.J. (2004) Inhibition of the Bacterial Enoyl Reductase FabI by Triclosan: A Structure-Reactivity Analysis of FabI Inhibition by Triclosan Analogues, J. Med. Chem. 47, 509-518.
    • (2004) J. Med. Chem. , vol.47 , pp. 509-518
    • Sivaraman, S.1    Sullivan, T.J.2    Johnson, F.3    Novichenok, P.4    Cui, G.5    Simmerling, C.6    Tonge, P.J.7
  • 37
    • 0034602557 scopus 로고    scopus 로고
    • Kinetic Mechanism of NADH-Enoyl-ACP Reductase from Brassica napus
    • Fawcett, T., Copse, C.L., Simon, J.W., and Slabas, A.R. (2000) Kinetic Mechanism of NADH-Enoyl-ACP Reductase from Brassica napus, FEBS Lett. 484, 65-68.
    • (2000) FEBS Lett. , vol.484 , pp. 65-68
    • Fawcett, T.1    Copse, C.L.2    Simon, J.W.3    Slabas, A.R.4
  • 38
    • 0035980230 scopus 로고    scopus 로고
    • The Structure of β-Ketoacyl-[Acyl Carrier Protein] Reductase from Escherichia coli: Negative Cooperativity and Its Structural Basis
    • Price, A.C., Zhang, Y.-M., Rock, C.O., and White, S.W. (2001) The Structure of β-Ketoacyl-[Acyl Carrier Protein] Reductase from Escherichia coli: Negative Cooperativity and Its Structural Basis, Biochemistry 40, 12772-12781.
    • (2001) Biochemistry , vol.40 , pp. 12772-12781
    • Price, A.C.1    Zhang, Y.-M.2    Rock, C.O.3    White, S.W.4
  • 39
    • 1542602992 scopus 로고    scopus 로고
    • Cofactor-Induced Conformational Rearrangements Establish a Catalytically Competent Active Site and a Proton Relay Conduit in β-Ketoacyl-Acyl Carrier Protein Reductase (FabG)
    • Price, A.C., Zhang, Y.-M., Rock, C.O., and White, S.W. (2004) Cofactor-Induced Conformational Rearrangements Establish a Catalytically Competent Active Site and a Proton Relay Conduit in β-Ketoacyl-Acyl Carrier Protein Reductase (FabG), Structure 12, 417-428.
    • (2004) Structure , vol.12 , pp. 417-428
    • Price, A.C.1    Zhang, Y.-M.2    Rock, C.O.3    White, S.W.4
  • 40
    • 0036299101 scopus 로고    scopus 로고
    • Crystal Structure of MabA from Mycobacterium tuberculosis, a Reductase Involved in Long-Chain FA Biosynthesis
    • Cohen-Gonsaud, M., Ducasse, S., Hoh, F., Zerbib, D., Labesse, G., and Quemard, A. (2002) Crystal Structure of MabA from Mycobacterium tuberculosis, a Reductase Involved in Long-Chain FA 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
  • 41
    • 0029941170 scopus 로고    scopus 로고
    • Polar Allele Duplication for Transcriptional Analysis of Consecutive Essential Genes: Application to a Cluster of Escherichia coli FA Biosynthetic Genes
    • Zhang, Y., and Cronan, J.E., Jr. (1996) Polar Allele Duplication for Transcriptional Analysis of Consecutive Essential Genes: Application to a Cluster of Escherichia coli FA Biosynthetic Genes, J. Bacteriol. 178, 3614-3620.
    • (1996) J. Bacteriol. , vol.178 , pp. 3614-3620
    • Zhang, Y.1    Cronan Jr., J.E.2
  • 42
    • 1542286897 scopus 로고    scopus 로고
    • Isolation and Characterization of β-Ketoacyl-Acyl Carrier Protein Reductase (fabG) Mutants of Escherichia coli and Salmonella enterica Serovar Typhimurium
    • Lai, C.Y., and Cronan, J.E., Jr. (2004) Isolation and Characterization of β-Ketoacyl-Acyl Carrier Protein Reductase (fabG) Mutants of Escherichia coli and Salmonella enterica Serovar Typhimurium, J. Bacteriol. 186, 1869-1878.
    • (2004) J. Bacteriol. , vol.186 , pp. 1869-1878
    • Lai, C.Y.1    Cronan Jr., J.E.2
  • 43
    • 3843101649 scopus 로고    scopus 로고
    • Evaluation of Epigallocatechin Gallate and Related Plant Polyphenols as Inhibitors of the FabG and FabI Reductases of Bacterial Type II FA Synthase
    • Zhang, Y.-M., and Rock, C.O. (2004) Evaluation of Epigallocatechin Gallate and Related Plant Polyphenols as Inhibitors of the FabG and FabI Reductases of Bacterial Type II FA Synthase, J. Biol. Chem. 279, 30994-31001.
    • (2004) J. Biol. Chem. , vol.279 , pp. 30994-31001
    • Zhang, Y.-M.1    Rock, C.O.2
  • 45
    • 0034723345 scopus 로고    scopus 로고
    • Action Mechanism of Antitubercular Isoniazid. Activation by Mycobacterium tuberculosis KatG, Isolation, and Characterization of InhA Inhibitor
    • Lei, B., Wei, C.J., and Tu, S.C. (2000) Action Mechanism of Antitubercular Isoniazid. Activation by Mycobacterium tuberculosis KatG, Isolation, and Characterization of InhA Inhibitor, J. Biol. Chem. 275, 2520-2526.
    • (2000) J. Biol. Chem. , vol.275 , pp. 2520-2526
    • Lei, B.1    Wei, C.J.2    Tu, S.C.3
  • 46
    • 0032472224 scopus 로고    scopus 로고
    • Modification of NADH of the Isoniazid Target (InhA) from Mycobacterium tuberculosis
    • Rozwarski, D., Grant, G., Barton, D., Jacobs, W., and Sacchettini, J.C. (1998) Modification of NADH of the Isoniazid Target (InhA) from Mycobacterium tuberculosis, Science 279, 98-102.
    • (1998) Science , vol.279 , pp. 98-102
    • Rozwarski, D.1    Grant, G.2    Barton, D.3    Jacobs, W.4    Sacchettini, J.C.5
  • 47
    • 0031733687 scopus 로고    scopus 로고
    • The mabA Gene from the inhA Operon of Mycobacterium tuberculosis Encodes a 3-Ketoacyl Reductase That Fails to Confer Isoniazid Resistance
    • Banerjee, A., Sugantino, M., Sacchettini, J.C., and Jacobs, W.R., Jr. (1998) The mabA Gene from the inhA Operon of Mycobacterium tuberculosis Encodes a 3-Ketoacyl Reductase That Fails to Confer Isoniazid Resistance, Microbiology 144, 2697-2704.
    • (1998) Microbiology , vol.144 , pp. 2697-2704
    • Banerjee, A.1    Sugantino, M.2    Sacchettini, J.C.3    Jacobs Jr., W.R.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.