메뉴 건너뛰기




Volumn 63, Issue 1, 2011, Pages 30-41

Effect of substrate binding loop mutations on the structure, kinetics, and inhibition of enoyl acyl carrier protein reductase from plasmodium falciparum

Author keywords

enoyl ACP reductase; mutant; P. falciparum; salt bridge; substrate binding loop; water bridge

Indexed keywords

ENOYL ACYL CARRIER PROTEIN REDUCTASE (NADH); ENZYME INHIBITOR; METHIONINE; PROTOZOAL PROTEIN; TRICLOSAN; VALINE; WATER;

EID: 79951979033     PISSN: 15216543     EISSN: 15216551     Source Type: Journal    
DOI: 10.1002/iub.412     Document Type: Article
Times cited : (6)

References (38)
  • 1
    • 0035126479 scopus 로고    scopus 로고
    • Triclosan offers protection against blood stages of malaria by inhibiting enoyl-ACP reductase of Plasmodium falciparum
    • DOI 10.1038/84612
    • 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. (Pubitemid 32148482)
    • (2001) Nature Medicine , vol.7 , Issue.2 , pp. 167-173
    • Surolia, N.1    Surolia, A.2
  • 2
    • 0030581109 scopus 로고    scopus 로고
    • Escherichia coli as a model for the regulation of dissociable (type II) fatty acid biosynthesis
    • DOI 10.1016/0005-2760(96)00056-2
    • Rock, C. O., and, Cronan, J. E., (1996) Escherichia coli as a model for the regulation of dissociable (type II) fatty acid biosynthesis. Biochim. Biophys. Acta 1302, 1-16. (Pubitemid 26267038)
    • (1996) Biochimica et Biophysica Acta - Lipids and Lipid Metabolism , vol.1302 , Issue.1 , pp. 1-16
    • Rock, C.O.1    Cronan, J.E.2
  • 5
    • 4644355051 scopus 로고    scopus 로고
    • Structural basis for the variation in triclosan affinity to enoyl reductases
    • DOI 10.1016/j.jmb.2004.08.033, PII S0022283604010113
    • Pidugu, L. S., Kapoor, M., Surolia, N., Surolia, A., and, Suguna, K., (2004) Structural basis for the variation in triclosan affinity to enoyl reductases. J. Mol. Biol. 343, 147-155. (Pubitemid 39277454)
    • (2004) Journal of Molecular Biology , vol.343 , Issue.1 , pp. 147-155
    • Pidugu, L.S.1    Kapoor, M.2    Surolia, N.3    Surolia, A.4    Suguna, K.5
  • 6
    • 77953581267 scopus 로고    scopus 로고
    • X-ray crystallographic analysis of the complexes ofenoyl acyl carrier protein reductase of Plasmodium falciparum with triclosan variants to elucidate the importance of different functional groups in enzyme inhibition
    • Maity, K., Bhargav, S. P., Sankaran, B., Surolia, N., Surolia, A., and, Suguna, K., (2010) X-ray crystallographic analysis of the complexes ofenoyl acyl carrier protein reductase of Plasmodium falciparum with triclosan variants to elucidate the importance of different functional groups in enzyme inhibition. IUBMB Life 62, 467-476.
    • (2010) IUBMB Life , vol.62 , pp. 467-476
    • Maity, K.1    Bhargav, S.P.2    Sankaran, B.3    Surolia, N.4    Surolia, A.5    Suguna, K.6
  • 8
    • 0035861962 scopus 로고    scopus 로고
    • Kinetic determinants of the interaction of enoyl-ACP reductase from Plasmodium Falciparum with its substrates and inhibitors
    • DOI 10.1006/bbrc.2001.6061
    • 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. (Pubitemid 34060079)
    • (2001) Biochemical and Biophysical Research Communications , vol.289 , Issue.4 , pp. 832-837
    • Kapoor, M.1    Jamal Dar, M.2    Surolia, A.3    Surolia, N.4
  • 9
    • 4344702214 scopus 로고    scopus 로고
    • Slow-tight-binding inhibition of enoyl-acyl carrier protein reductase from Plasmodium falciparum by triclosan
    • DOI 10.1042/BJ20031821
    • Kapoor, M., Reddy, C. C., Krishnasastry, M. V., Surolia, N., and, Surolia, A., (2004) Slow-tight-binding inhibition of enoyl-acyl carrier protein reductase from Plasmodium falciparum by triclosan. Biochem. J. 381, 719-724. (Pubitemid 39120481)
    • (2004) Biochemical Journal , vol.381 , Issue.3 , pp. 719-724
    • Kapoor, M.1    Chandramouli Reddy, C.2    Krishnasastry, M.V.3    Surolia, N.4    Surolia, A.5
  • 11
    • 4344584118 scopus 로고    scopus 로고
    • Mutational analysis of the triclosan-binding region of enoyl-ACP (acyl-carrier protein) reductase from Plasmodium falciparum
    • DOI 10.1042/BJ20040302
    • Kapoor, M., Gopalakrishnapai, J., Surolia, N., and, Surolia, A., (2004) Mutational analysis of the triclosan-binding region of enoyl-ACP (acyl-carrier protein) reductase from Plasmodium falciparum. Biochem. J. 381, 735-741. (Pubitemid 39120483)
    • (2004) Biochemical Journal , vol.381 , Issue.3 , pp. 735-741
    • Kapoor, M.1    Gopalakrishnapai, J.2    Surolia, N.3    Surolia, A.4
  • 12
    • 0030452311 scopus 로고    scopus 로고
    • A mechanism of drug action revealed by structural studies of Enoyl reductase
    • DOI 10.1126/science.274.5295.2107
    • Baldock, C., Rafferty, J. B., Sedelnikova, S. E., Baker, P. J., Stuitje, A. R., Slabas, A. R., Hawkes, T. R., and, Rice, D. W., (1996) A mechanism of drug action revealed by structural studies of enoyl reductase. Science 274, 2107-2110. (Pubitemid 27020709)
    • (1996) Science , vol.274 , Issue.5295 , pp. 2107-2110
    • Baldock, C.1    Rafferty, J.B.2    Sedelnikova, S.E.3    Baker, P.J.4    Stuitje, A.R.5    Slabas, A.R.6    Hawkes, T.R.7    Rice, D.W.8
  • 14
    • 0032775211 scopus 로고    scopus 로고
    • Structural basis and mechanism of enoyl reductase inhibition by triclosan
    • DOI 10.1006/jmbi.1999.2907
    • 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. (Pubitemid 29349393)
    • (1999) Journal of Molecular Biology , vol.290 , Issue.4 , pp. 859-865
    • Stewart, M.J.1    Parikh, S.2    Xiao, G.3    Tonge, P.J.4    Kisker, C.5
  • 15
    • 0032472224 scopus 로고    scopus 로고
    • Modification of the NADH of the isoniazid target (InhA) from Mycobacterium tuberculosis
    • DOI 10.1126/science.279.5347.98
    • Rozwarski, D. A., Grant, G. A., Barton, D. H., Jacobs, W. R., Jr., and, Sacchettini, J. C., (1998) Modification of the NADH of the isoniazid target (InhA) from Mycobacterium tuberculosis. Science 279, 98-102. (Pubitemid 28079164)
    • (1998) Science , vol.279 , Issue.5347 , 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
  • 17
    • 35448938486 scopus 로고    scopus 로고
    • Crystal structure of the Helicobacter pylori enoyl-acyl carrier protein reductase in complex with hydroxydiphenyl ether compounds, triclosan and diclosan
    • DOI 10.1002/prot.21586
    • Lee, H. H., Moon, J., and, Suh, S. W., (2007) Crystal structure of the Helicobacter pylori enoyl-acyl carrier protein reductase in complex with hydroxydiphenyl ether compounds, triclosan and diclosan. Proteins 69, 691-694. (Pubitemid 47623883)
    • (2007) Proteins: Structure, Function and Genetics , vol.69 , Issue.3 , pp. 691-694
    • Hyung, H.L.1    Moon, J.2    Se, W.S.3
  • 18
    • 33947318051 scopus 로고    scopus 로고
    • Studies of Toxoplasma gondii and Plasmodium falciparum enoyl acyl carrier protein reductase and implications for the development of antiparasitic agents
    • DOI 10.1107/S0907444906053625, PII S0907444906053625
    • Muench, S. P., Prigge, S. T., McLeod, R., Rafferty, J. B., Kirisits, M. J., Roberts, C. W., Mui, E. J., and, Rice, D. W., (2007) Studies of Toxoplasma gondii and Plasmodium falciparum enoyl acyl carrier protein reductase and implications for the development of antiparasitic agents. Acta Crystallogr. D Biol. Crystallogr. 63, 328-338. (Pubitemid 46438526)
    • (2007) Acta Crystallographica Section D: Biological Crystallography , vol.63 , Issue.3 , pp. 328-338
    • Muench, S.P.1    Prigge, S.T.2    McLeod, R.3    Rafferty, J.B.4    Kirisits, M.J.5    Roberts, C.W.6    Mui, E.J.7    Rice, D.W.8
  • 19
    • 0032490937 scopus 로고    scopus 로고
    • Triclosan targets lipid synthesis
    • McMurry, L. M., Oethinger, M., and, Levy, S. B., (1998) Triclosan targets lipid synthesis. Nature 394, 531-532.
    • (1998) Nature , vol.394 , pp. 531-532
    • McMurry, L.M.1    Oethinger, M.2    Levy, S.B.3
  • 20
    • 0032859660 scopus 로고    scopus 로고
    • Characterization of Pseudomonas aeruginosa enoyl-acyl carrier protein reductase (FabI): A target for the antimicrobial triclosan and its role in acylated homoserine lactone synthesis
    • Hoang, T. T., and, Schweizer, H. P., (1999) Characterization of Pseudomonas aeruginosa enoyl-acyl carrier protein reductase (FabI): a target for the antimicrobial triclosan and its role in acylated homoserine lactone synthesis. J. Bacteriol. 181, 5489-5497. (Pubitemid 29416374)
    • (1999) Journal of Bacteriology , vol.181 , Issue.17 , pp. 5489-5497
    • Hoang, T.T.1    Schweizer, H.P.2
  • 21
    • 0034704090 scopus 로고    scopus 로고
    • The enoyl-[acyl-carrier-protein] reductases FabI and FabL from Bacillus subtilis
    • DOI 10.1074/jbc.M005611200
    • 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. (Pubitemid 32064639)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.51 , pp. 40128-40133
    • Heath, R.J.1    Su, N.2    Murphy, C.K.3    Rock, C.O.4
  • 22
    • 34548335105 scopus 로고    scopus 로고
    • Crystallographic studies on the binding of isonicotinyl-NAD adduct to wild-type and isoniazid resistant 2-trans-enoyl-ACP (CoA) reductase from Mycobacterium tuberculosis
    • DOI 10.1016/j.jsb.2007.04.009, PII S1047847707000834
    • Dias, M. V., Vasconcelos, I. B., Prado, A. M., Fadel, V., Basso, L. A., de Azevedo, W. F., Jr., and, Santos, D. S., (2007) Crystallographic studies on the binding of isonicotinyl-NAD adduct to wild-type and isoniazid resistant 2-trans-enoyl-ACP (CoA) reductase from Mycobacterium tuberculosis. J. Struct. Biol. 159, 369-380. (Pubitemid 47348298)
    • (2007) Journal of Structural Biology , vol.159 , Issue.3 , pp. 369-380
    • Dias, M.V.B.1    Vasconcelos, I.B.2    Prado, A.M.X.3    Fadel, V.4    Basso, L.A.5    De Azevedo Jr., W.F.6    Santos, D.S.7
  • 23
    • 33646893263 scopus 로고    scopus 로고
    • Crystallographic and Pre-steady-state Kinetics Studies on Binding of NADH to Wild-type and Isoniazid-resistant Enoyl-ACP(CoA) Reductase Enzymes from Mycobacterium tuberculosis
    • DOI 10.1016/j.jmb.2006.03.055, PII S0022283606004189
    • Oliveira, J. S., Pereira, J. H., Canduri, F., Rodrigues, N. C., de Souza, O. N., de Azevedo, W. F., Jr., Basso, L. A., and, Santos, D. S., (2006) Crystallographic and pre-steady-state kinetics studies on binding of NADH to wild-type and isoniazid-resistant enoyl-ACP(CoA) reductase enzymes from Mycobacterium tuberculosis. J. Mol. Biol. 359, 646-666. (Pubitemid 43786403)
    • (2006) Journal of Molecular Biology , vol.359 , Issue.3 , pp. 646-666
    • Oliveira, J.S.1    Pereira, J.H.2    Canduri, F.3    Rodrigues, N.C.4    De Souza, O.N.5    De Azevedo Jr., W.F.6    Basso, L.A.7    Santos, D.S.8
  • 24
    • 33847694649 scopus 로고    scopus 로고
    • The inhibition of 5-enolpyruvylshikimate-3-phosphate synthase as a model for development of novel antimicrobials
    • DOI 10.2174/138945007780058951
    • Marques, M. R., Pereira, J. H., Oliveira, J. S., Basso, L. A., de Azevedo, W. F., Jr., Santos, D. S., and, Palma, M. S., (2007) The inhibition of 5-enolpyruvylshikimate-3-phosphate synthase as a model for development of novel antimicrobials. Curr. Drug Targets 8, 445-457. (Pubitemid 46381295)
    • (2007) Current Drug Targets , vol.8 , Issue.3 , pp. 445-457
    • Marques, M.R.1    Pereira, J.H.2    Oliveira, J.S.3    Basso, L.A.4    De Azevedo Jr., W.F.5    Santos, D.S.6    Palma, M.S.7
  • 26
  • 28
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project Number 4
    • Collaborative Computational Project Number 4. (1994) The CCP4 suite: programs for protein crystallography. Acta Crystallogr. D Biol. Crystallogr. 50, 760-763.
    • (1994) Acta Crystallogr. D Biol. Crystallogr. , vol.50 , pp. 760-763
  • 32
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • Laskowski, R. A., McArthur, M. W., Moss, D. S., and, Thornton, J. M., (1993) PROCHECK: a program to check the stereochemical quality of protein structures. J. Appl. Crystallogr. 26, 283-291.
    • (1993) J. Appl. Crystallogr. , vol.26 , pp. 283-291
    • Laskowski, R.A.1    McArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 33
    • 0001679473 scopus 로고    scopus 로고
    • ALIGN: A program to superimpose protein coordinates, accounting for insertions and deletions
    • Cohen, G. H., (1997) ALIGN: a program to superimpose protein coordinates accounting for insertions and deletions. J. Appl. Crystallogr. 30, 1160-1161. (Pubitemid 127791747)
    • (1997) Journal of Applied Crystallography , vol.30 , Issue.6 , pp. 1160-1161
    • Cohen, G.H.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.