메뉴 건너뛰기




Volumn 343, Issue 1, 2004, Pages 147-155

Structural basis for the variation in triclosan affinity to enoyl reductases

Author keywords

enoyl ACP reductase; FAS II; NADH; structural comparison; triclosan

Indexed keywords

ENOYL ACYL CARRIER PROTEIN REDUCTASE; NICOTINAMIDE ADENINE DINUCLEOTIDE; OXIDOREDUCTASE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE; TRICLOSAN; UNCLASSIFIED DRUG;

EID: 4644355051     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2004.08.033     Document Type: Article
Times cited : (61)

References (41)
  • 1
    • 0034804919 scopus 로고    scopus 로고
    • Lipid biosynthesis as a target for antibacterial agents
    • R.J. Heath, S.W. White, and C.O. Rock Lipid biosynthesis as a target for antibacterial agents Prog. Lipid Res. 40 2001 467 497
    • (2001) Prog. Lipid Res. , vol.40 , pp. 467-497
    • Heath, R.J.1    White, S.W.2    Rock, C.O.3
  • 2
    • 0035338328 scopus 로고    scopus 로고
    • Bacterial fatty-acid biosynthesis: A genomics-driven target for antibacterial drug discovery
    • D.J. Payne, P.V. Warren, D.J. Holmes, Y. Ji, and J.T. Lonsdale Bacterial fatty-acid biosynthesis: a genomics-driven target for antibacterial drug discovery Drug Discov. Today 6 2001 537 544
    • (2001) Drug Discov. Today , vol.6 , pp. 537-544
    • Payne, D.J.1    Warren, P.V.2    Holmes, D.J.3    Ji, Y.4    Lonsdale, J.T.5
  • 3
    • 33749176747 scopus 로고
    • Fatty acid synthase-an example of protein evolution by gene fusion
    • A.D. McCarthy, and D.G. Hardie Fatty acid synthase-an example of protein evolution by gene fusion Trends Biochem. Sci. 9 1984 60 63
    • (1984) Trends Biochem. Sci. , vol.9 , pp. 60-63
    • McCarthy, A.D.1    Hardie, D.G.2
  • 4
    • 0028557012 scopus 로고
    • The animal fatty acid synthase: One gene, one polypeptide, seven enzymes
    • S. Smith The animal fatty acid synthase: one gene, one polypeptide, seven enzymes FASEB J. 8 1994 1248 1259
    • (1994) FASEB J. , vol.8 , pp. 1248-1259
    • Smith, S.1
  • 5
    • 0030581109 scopus 로고    scopus 로고
    • Escherichia coli as a model for the regulation of dissociable (type II) fatty acid biosynthesis
    • C.O. Rock, and J.E. Cronan 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.2
  • 6
    • 0028988237 scopus 로고
    • Crystal structure and function of the isoniazid target of Mycobacterium tuberculosis
    • A. Dessen, A. Quemard, J.S. Blanchard, W.R. Jacobs Jr, and J.C. Sacchettini Crystal structure and function of the isoniazid target of Mycobacterium tuberculosis Science 267 1995 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
  • 7
    • 0032472224 scopus 로고    scopus 로고
    • Modification of the NADH of the isoniazid target (InhA) from Mycobacterium tuberculosis
    • D.A. Rozwarski, G.A. Grant, D.H.R. Barton, W.R. Jacobs Jr., and J.C. Sacchettini Modification of the NADH of the isoniazid target (InhA) from Mycobacterium tuberculosis Science 279 1998 98 102
    • (1998) Science , vol.279 , pp. 98-102
    • Rozwarski, D.A.1    Grant, G.A.2    Barton, D.H.R.3    Jacobs Jr., W.R.4    Sacchettini, J.C.5
  • 9
    • 0036008554 scopus 로고    scopus 로고
    • Paradigm shifts in malaria parasite biochemistry and anti-malarial chemotherapy
    • N. Surolia, S.P. Ramachandra Rao, and A. Surola Paradigm shifts in malaria parasite biochemistry and anti-malarial chemotherapy Bioessays 24 2002 192 196
    • (2002) Bioessays , vol.24 , pp. 192-196
    • Surolia, N.1    Ramachandra Rao, S.P.2    Surola, A.3
  • 10
    • 0142061141 scopus 로고    scopus 로고
    • Apicoplast fatty acid biosynthesis as a target for medical intervention in apicomplexan parasites
    • P. Gornicki Apicoplast fatty acid biosynthesis as a target for medical intervention in apicomplexan parasites Int. J. Parasitol. 33 2003 885 896
    • (2003) Int. J. Parasitol. , vol.33 , pp. 885-896
    • Gornicki, P.1
  • 12
    • 0028855972 scopus 로고
    • Enoyl-acyl carrier protein reductase (fabI) plays a determinant role in completing cycles of fatty acid elongation in Escherichia coli
    • R.J. Heath, and C.O. Rock Enoyl-acyl carrier protein reductase (fabI) plays a determinant role in completing cycles of fatty acid elongation in Escherichia coli J. Biol. Chem. 270 1995 26538 26542
    • (1995) J. Biol. Chem. , vol.270 , pp. 26538-26542
    • Heath, R.J.1    Rock, C.O.2
  • 13
    • 0026729159 scopus 로고
    • Handwashing in a neonatal intensive care nursery: Product acceptability and effectiveness of chlorhexidine gluconate 4% and triclosan 1%
    • J. Webster Handwashing in a neonatal intensive care nursery: product acceptability and effectiveness of chlorhexidine gluconate 4% and triclosan 1% J. Hosp. Infect. 21 1992 137 141
    • (1992) J. Hosp. Infect. , vol.21 , pp. 137-141
    • Webster, J.1
  • 14
    • 0032490937 scopus 로고    scopus 로고
    • Triclosan targets lipid synthesis
    • L.M. McMurry, M. Oethinger, and S.B. Levy Triclosan targets lipid synthesis Nature 394 1998 531 532
    • (1998) Nature , vol.394 , pp. 531-532
    • McMurry, L.M.1    Oethinger, M.2    Levy, S.B.3
  • 15
    • 0032515066 scopus 로고    scopus 로고
    • Broad-spectrum antimicrobial biocides target the FabI component of fatty acid synthesis
    • R.J. Heath, Y.T. Yu, M.A. Shapiro, E. Olson, and C.O. Rock Broad-spectrum antimicrobial biocides target the FabI component of fatty acid synthesis J. Biol. Chem. 273 1998 30316 30320
    • (1998) J. Biol. Chem. , vol.273 , pp. 30316-30320
    • Heath, R.J.1    Yu, Y.T.2    Shapiro, M.A.3    Olson, E.4    Rock, C.O.5
  • 16
    • 0033592365 scopus 로고    scopus 로고
    • Kinetic and structural characteristics of the inhibition of enoyl (acyl carrier protein) reductase by triclosan
    • W.H. Ward, G.A. Holdgate, S. Rowsell, E.G. McLean, R.A. Pauptit, and E. Clayton Kinetic and structural characteristics of the inhibition of enoyl (acyl carrier protein) reductase by triclosan Biochemistry 38 1999 12514 12525
    • (1999) Biochemistry , vol.38 , pp. 12514-12525
    • Ward, W.H.1    Holdgate, G.A.2    Rowsell, S.3    McLean, E.G.4    Pauptit, R.A.5    Clayton, E.6
  • 17
    • 0033055847 scopus 로고    scopus 로고
    • Genetic evidence that InhA of Mycobacterium smegmatis is a target for triclosan
    • L.M. McMurry, P.F. McDermott, and S.B. Levy Genetic evidence that InhA of Mycobacterium smegmatis is a target for triclosan Antimicrob. Agents Chemother. 43 1999 711 713
    • (1999) Antimicrob. Agents Chemother. , vol.43 , pp. 711-713
    • McMurry, L.M.1    McDermott, P.F.2    Levy, S.B.3
  • 18
    • 17644436310 scopus 로고    scopus 로고
    • Inhibition of InhA, the enoyl reductase from Mycobacterium tuberculosis, by triclosan and isoniazid
    • S.L. Parikh, G. Xiao, and P.J. Tonge Inhibition of InhA, the enoyl reductase from Mycobacterium tuberculosis, by triclosan and isoniazid Biochemistry 39 2000 7645 7650
    • (2000) Biochemistry , vol.39 , pp. 7645-7650
    • Parikh, S.L.1    Xiao, G.2    Tonge, P.J.3
  • 19
    • 0035126479 scopus 로고    scopus 로고
    • Triclosan offers protection against blood stages of malaria by inhibiting enoyl-ACP reductase of Plasmodium falciparum
    • N. Surolia, and A. Surolia Triclosan offers protection against blood stages of malaria by inhibiting enoyl-ACP reductase of Plasmodium falciparum Nature Med. 7 2001 167 173
    • (2001) Nature Med. , vol.7 , pp. 167-173
    • Surolia, N.1    Surolia, A.2
  • 20
    • 0037066782 scopus 로고    scopus 로고
    • Structural elucidation of the specificity of the antibacterial agent triclosan for malarial enoyl acyl carrier protein reductase
    • R. Perozzo, M. Kuo, A.S. Sidhu, J.T. Valiyaveettil, R. Bittman, and W.R. Jacobs Jr Structural elucidation of the specificity of the antibacterial agent triclosan for malarial enoyl acyl carrier protein reductase J. Biol. Chem. 277 2002 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
  • 21
    • 4344702214 scopus 로고    scopus 로고
    • Slow-tight-binding inhibition of enoyl-acyl carrier protein reductase from Plasmodium falciparum by triclosan
    • M. Kapoor, C.C. Reddy, M.V. Krishnasastry, N. Surolia, and A. Surolia Slow-tight-binding inhibition of enoyl-acyl carrier protein reductase from Plasmodium falciparum by triclosan Biochem. J. 381 2004 719 724
    • (2004) Biochem. J. , vol.381 , pp. 719-724
    • Kapoor, M.1    Reddy, C.C.2    Krishnasastry, M.V.3    Surolia, N.4    Surolia, A.5
  • 24
    • 0029645410 scopus 로고
    • Common themes in redox chemistry emerge from the X-ray structure of oilseed rape (Brassica napus) enoyl-acyl carrier protein reductase
    • J.B. Rafferty, J.W. Simon, C. Baldock, P.J. Artymiuk, P.J. Baker, and A.R. Stuitje Common themes in redox chemistry emerge from the X-ray structure of oilseed rape (Brassica napus) enoyl-acyl carrier protein reductase Structure 3 1995 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
  • 27
    • 0038757566 scopus 로고    scopus 로고
    • Targeting tuberculosis and malaria through inhibition of Enoyl reductase: Compound activity and structural data
    • M.R. Kuo, H.R. Morbidoni, D. Alland, S.F. Sneddon, B.B. Gourlie, and M.M. Staveski Targeting tuberculosis and malaria through inhibition of Enoyl reductase: compound activity and structural data J. Biol. Chem. 278 2003 20851 20859
    • (2003) J. Biol. Chem. , vol.278 , pp. 20851-20859
    • Kuo, M.R.1    Morbidoni, H.R.2    Alland, D.3    Sneddon, S.F.4    Gourlie, B.B.5    Staveski, M.M.6
  • 30
    • 0033550048 scopus 로고    scopus 로고
    • Roles of tyrosine 158 and lysine 165 in the catalytic mechanism of InhA, the enoyl-ACP reductase from Mycobacterium tuberculosis
    • S. Parikh, D.P. Moynihan, G. Xiao, and P.J. Tonge Roles of tyrosine 158 and lysine 165 in the catalytic mechanism of InhA, the enoyl-ACP reductase from Mycobacterium tuberculosis Biochemistry 38 1999 13623 13634
    • (1999) Biochemistry , vol.38 , pp. 13623-13634
    • Parikh, S.1    Moynihan, D.P.2    Xiao, G.3    Tonge, P.J.4
  • 31
    • 0035861962 scopus 로고    scopus 로고
    • Kinetic determinants of the interaction of enoyl-ACP reductase from Plasmodium falciparum with its substrates and inhibitors
    • M. Kapoor, M.J. Dar, A. Surolia, and N. Surolia Kinetic determinants of the interaction of enoyl-ACP reductase from Plasmodium falciparum with its substrates and inhibitors Biochem. Biophys. Res. Commun. 289 2001 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
  • 32
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Z. Otwinowski, and W. Minor Processing of X-ray diffraction data collected in oscillation mode Methods Enzymol. 276 1997 307 326
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 33
    • 84920325457 scopus 로고
    • AMoRe: An automated package for molecular replacement
    • J. Navaza AMoRe: an automated package for molecular replacement Acta Crystallog. A 50 1994 157 163
    • (1994) Acta Crystallog. a , vol.50 , pp. 157-163
    • Navaza, J.1
  • 35
  • 36
    • 0001679473 scopus 로고    scopus 로고
    • ALIGN: A program to superimpose protein coordinates, accounting for insertions and deletions
    • G.H. Cohen ALIGN: a program to superimpose protein coordinates, accounting for insertions and deletions J. Appl. Crystallog. 30 1997 1160 1161
    • (1997) J. Appl. Crystallog. , vol.30 , pp. 1160-1161
    • Cohen, G.H.1
  • 37
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project, Number 4
    • Collaborative Computational Project, Number 4 The CCP4 suite: programs for protein crystallography Acta Crystallog. D 50 1994 760 763
    • (1994) Acta Crystallog. D , vol.50 , pp. 760-763
  • 38
    • 0030841587 scopus 로고    scopus 로고
    • Electron density map interpretation
    • T.A. Jones, and M. Kjeldgaard Electron density map interpretation Methods Enzymol. 277 1997 173 230
    • (1997) Methods Enzymol. , vol.277 , pp. 173-230
    • Jones, T.A.1    Kjeldgaard, M.2
  • 39
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • P.J. Kraulis MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures J. Appl. Crystallog. 24 1991 946 950
    • (1991) J. Appl. Crystallog. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 40
    • 0030815133 scopus 로고    scopus 로고
    • Raster3D: Photorealistic molecular graphics
    • E.A. Merrit, and D.J. Bacon Raster3D: photorealistic molecular graphics Methods Enzymol. 277 1997 505 524
    • (1997) Methods Enzymol. , vol.277 , pp. 505-524
    • Merrit, E.A.1    Bacon, D.J.2
  • 41
    • 0030729838 scopus 로고    scopus 로고
    • An extensively modified version of MolScript that includes greatly enhanced coloring capabilities
    • R. Esnouf An extensively modified version of MolScript that includes greatly enhanced coloring capabilities J. Mol. Graph. 15 1997 132 134
    • (1997) J. Mol. Graph. , vol.15 , pp. 132-134
    • Esnouf, R.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.