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Volumn 377, Issue 4, 2008, Pages 1238-1242

Epigallocatechin gallate is a slow-tight binding inhibitor of enoyl-ACP reductase from Plasmodium falciparum

Author keywords

EGCG; Enoyl ACP reductase; Malaria; PfENR; Plasmodium falciparum; Slow; Tight binding inhibitor; Triclosan

Indexed keywords

ENOYL ACYL CARRIER PROTEIN REDUCTASE (NADH); EPIGALLOCATECHIN GALLATE; TRICLOSAN;

EID: 56349158676     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2008.10.135     Document Type: Article
Times cited : (17)

References (26)
  • 1
    • 56349090639 scopus 로고    scopus 로고
    • WHO. Communicable Disease Repot - Roll Back Malaria [online] , (2002) 1-19.
    • WHO. Communicable Disease Repot - Roll Back Malaria [online] , (2002) 1-19.
  • 2
    • 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. Triclosan offers protection against blood stages of malaria by inhibiting enoyl-ACP reductase of Plasmodium falciparum. Nat. Med. 7 (2001) 167-173
    • (2001) Nat. Med. , vol.7 , pp. 167-173
    • Surolia, N.1    Surolia, A.2
  • 3
    • 0030581109 scopus 로고    scopus 로고
    • Escherichia coli as a model for the regulation of dissociable (type II) fatty acid biosynthesis
    • Rock C.O., and Cronan J.E. 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
  • 4
    • 0037411269 scopus 로고    scopus 로고
    • Structural and functional organization of the animal fatty acid synthase
    • Smith S., Witkowski A., and Joshi A.K. Structural and functional organization of the animal fatty acid synthase. Prog. Lipid Res. 42 (2003) 289-317
    • (2003) Prog. Lipid Res. , vol.42 , pp. 289-317
    • Smith, S.1    Witkowski, A.2    Joshi, A.K.3
  • 7
    • 0035861962 scopus 로고    scopus 로고
    • Kinetic determination 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. Kinetic determination 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
  • 8
    • 4344702214 scopus 로고    scopus 로고
    • Slow-tight-binding inhibition of enoyl-acyl carrier protein reductase from Plasmodium falciparum by triclosan
    • Kapoor M., Reddy C.C., Krishnasastry M.V., Surolia N., and Surolia A. 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
  • 10
    • 4344584118 scopus 로고    scopus 로고
    • Mutational analysis of the triclosan-binding region of enoyl-ACP (acyl carrier protein) reductase from Plasmodium falciparum
    • Kapoor M., Gopalakrishnapai J., Surolia N., and Surolia A. Mutational analysis of the triclosan-binding region of enoyl-ACP (acyl carrier protein) reductase from Plasmodium falciparum. Biochem. J. 381 (2004) 735-741
    • (2004) Biochem. J. , vol.381 , pp. 735-741
    • Kapoor, M.1    Gopalakrishnapai, J.2    Surolia, N.3    Surolia, A.4
  • 11
    • 4644355051 scopus 로고    scopus 로고
    • Structural basis for the variation in triclosan affinity to Enoyl Reductases
    • Pidugu L.S., Kapoor M., Surolia N., Surolia A., and Suguna K. Structural basis for the variation in triclosan affinity to Enoyl Reductases. J. Mol. Biol. 343 (2004) 147-155
    • (2004) J. Mol. Biol. , vol.343 , pp. 147-155
    • Pidugu, L.S.1    Kapoor, M.2    Surolia, N.3    Surolia, A.4    Suguna, K.5
  • 12
    • 33750036420 scopus 로고    scopus 로고
    • Novel diphenyl ethers: design, docking studies, synthesis and inhibition of enoyl ACP reductase of Plasmodium falciparum and Escherichia coli
    • Chhibber M., Kumar G., Parasuraman P., Ramya T.N., Surolia N., and Surolia A. Novel diphenyl ethers: design, docking studies, synthesis and inhibition of enoyl ACP reductase of Plasmodium falciparum and Escherichia coli. Bioorg. Med. Chem. 14 (2006) 8086-8098
    • (2006) Bioorg. Med. Chem. , vol.14 , pp. 8086-8098
    • Chhibber, M.1    Kumar, G.2    Parasuraman, P.3    Ramya, T.N.4    Surolia, N.5    Surolia, A.6
  • 13
    • 43749084141 scopus 로고    scopus 로고
    • Design, synthesis, and application of novel triclosan prodrugs as potential antimalarial and antibacterial agents
    • Mishra S., Karmodiya K., Parasuraman P., Surolia A., and Surolia N. Design, synthesis, and application of novel triclosan prodrugs as potential antimalarial and antibacterial agents. Bioorg. Med. Chem. 16 (2008) 5536-5546
    • (2008) Bioorg. Med. Chem. , vol.16 , pp. 5536-5546
    • Mishra, S.1    Karmodiya, K.2    Parasuraman, P.3    Surolia, A.4    Surolia, N.5
  • 14
    • 34250189143 scopus 로고    scopus 로고
    • Discovery of a rhodanine class of compounds as inhibitors of Plasmodium falciparum enoyl-acyl carrier protein reductase
    • Kumar G., Parasuraman P., Sharma S.K., Banerjee T., Karmodiya K., Surolia N., and Surolia A. Discovery of a rhodanine class of compounds as inhibitors of Plasmodium falciparum enoyl-acyl carrier protein reductase. J. Med. Chem. 50 (2007) 2665-2667
    • (2007) J. Med. Chem. , vol.50 , pp. 2665-2667
    • Kumar, G.1    Parasuraman, P.2    Sharma, S.K.3    Banerjee, T.4    Karmodiya, K.5    Surolia, N.6    Surolia, A.7
  • 15
    • 33847401359 scopus 로고    scopus 로고
    • Green tea catechins potentiates triclosan binding to Enoyl ACP Reductase from Plasmodium falciparum PfENR
    • Sharma S.K., Parasuraman P., Kumar G., Surolia N., and Surolia A. Green tea catechins potentiates triclosan binding to Enoyl ACP Reductase from Plasmodium falciparum PfENR. J. Med. Chem. 50 (2007) 765-775
    • (2007) J. Med. Chem. , vol.50 , pp. 765-775
    • Sharma, S.K.1    Parasuraman, P.2    Kumar, G.3    Surolia, N.4    Surolia, A.5
  • 17
    • 22344452397 scopus 로고    scopus 로고
    • Medicinal benefits of green tea: part II. Review of anticancer properties
    • Cooper R., Morré D.J., and Morré D.M. Medicinal benefits of green tea: part II. Review of anticancer properties. J. Alternat. Complement. Med. 11 (2005) 639-652
    • (2005) J. Alternat. Complement. Med. , vol.11 , pp. 639-652
    • Cooper, R.1    Morré, D.J.2    Morré, D.M.3
  • 19
    • 33644949188 scopus 로고    scopus 로고
    • Neuroprotective effects of green and black teas and their catechin gallate esters against beta-amyloid-induced toxicity
    • Bastianetto S., Yao Z.X., Papadopoulos V., and Quirion R. Neuroprotective effects of green and black teas and their catechin gallate esters against beta-amyloid-induced toxicity. Eur. J. Neurosci. 23 (2006) 55-64
    • (2006) Eur. J. Neurosci. , vol.23 , pp. 55-64
    • Bastianetto, S.1    Yao, Z.X.2    Papadopoulos, V.3    Quirion, R.4
  • 20
    • 33644854044 scopus 로고    scopus 로고
    • Green tea extract and its major polyphenol (-)-epigallocatechin gallate improve muscle function in a mouse model for Duchenne muscular dystrophy
    • Dorchies O.M., Wagner S., Vuadens O., Waldhauser K., Buetler T.M., Kucera P., and Ruegg U.T. Green tea extract and its major polyphenol (-)-epigallocatechin gallate improve muscle function in a mouse model for Duchenne muscular dystrophy. Am. J. Physiol. Cell. Physiol. 290 (2006) 616-625
    • (2006) Am. J. Physiol. Cell. Physiol. , vol.290 , pp. 616-625
    • Dorchies, O.M.1    Wagner, S.2    Vuadens, O.3    Waldhauser, K.4    Buetler, T.M.5    Kucera, P.6    Ruegg, U.T.7
  • 21
    • 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 fatty-acid synthase
    • Zhang Y.M., and Rock C.O. Evaluation of epigallocatechin gallate and related plant polyphenols as inhibitors of the FabG and FabI reductases of bacterial type II fatty-acid synthase. J. Biol. Chem. 279 (2004) 30994-31001
    • (2004) J. Biol. Chem. , vol.279 , pp. 30994-31001
    • Zhang, Y.M.1    Rock, C.O.2
  • 22
    • 33744819176 scopus 로고    scopus 로고
    • Inhibition of Plasmodium falciparum fatty acid biosynthesis: evaluation of FabG, FabZ, and FabI as drug targets for flavonoids
    • Tasdemir D., Lack G., Burn R., Ruedi P., Scapozza L., and Perozzo R. Inhibition of Plasmodium falciparum fatty acid biosynthesis: evaluation of FabG, FabZ, and FabI as drug targets for flavonoids. J. Med. Chem. 49 (2006) 3345-3353
    • (2006) J. Med. Chem. , vol.49 , pp. 3345-3353
    • Tasdemir, D.1    Lack, G.2    Burn, R.3    Ruedi, P.4    Scapozza, L.5    Perozzo, R.6
  • 23
    • 39149099113 scopus 로고    scopus 로고
    • Combined effect of epigallocatechin gallate and triclosan on enoyl-ACP reductase of Mycobacterium tuberculosis
    • Sharma S.K., Kumar G., Kapoor M., and Surolia A. Combined effect of epigallocatechin gallate and triclosan on enoyl-ACP reductase of Mycobacterium tuberculosis. Biochem. Biophys. Res. Commun. 368 (2008) 12-17
    • (2008) Biochem. Biophys. Res. Commun. , vol.368 , pp. 12-17
    • Sharma, S.K.1    Kumar, G.2    Kapoor, M.3    Surolia, A.4
  • 24
    • 12344300344 scopus 로고    scopus 로고
    • The reductase steps of the type II fatty acid synthase as antimicrobial targets
    • Zhang Y.M., Lu Y.J., and Rock C.O. The reductase steps of the type II fatty acid synthase as antimicrobial targets. Lipids 39 (2004) 1055-1060
    • (2004) Lipids , vol.39 , pp. 1055-1060
    • Zhang, Y.M.1    Lu, Y.J.2    Rock, C.O.3
  • 25
    • 0023728105 scopus 로고
    • The behaviour and significance of slow tight binding enzyme inhibitors
    • Morrison J.F., and Walsh C. The behaviour and significance of slow tight binding enzyme inhibitors. Adv.Enzymol. Relat. Areas Mol. Biol. 61 (1988) 201-301
    • (1988) Adv.Enzymol. Relat. Areas Mol. Biol. , vol.61 , pp. 201-301
    • Morrison, J.F.1    Walsh, C.2
  • 26
    • 0001396685 scopus 로고
    • The slow binding and slow, tight-binding inhibition of enzyme catalysed reactions
    • Morrison J.F. The slow binding and slow, tight-binding inhibition of enzyme catalysed reactions. Trends Biochem. Sci. 7 (1982) 102-105
    • (1982) Trends Biochem. Sci. , vol.7 , pp. 102-105
    • Morrison, J.F.1


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