메뉴 건너뛰기




Volumn 368, Issue 1, 2008, Pages 12-17

Combined effect of epigallocatechin gallate and triclosan on enoyl-ACP reductase of Mycobacterium tuberculosis

Author keywords

EGCG; Enoyl reductase; Epigallocatechin gallate; FAS I; FAS II; Fluorescence titration; InhA; Mycobacterium tuberculosis; Scatchard plot; Tea catechins; Triclosan; Tuberculosis

Indexed keywords

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

EID: 39149099113     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2007.10.191     Document Type: Article
Times cited : (27)

References (27)
  • 1
    • 39149090421 scopus 로고    scopus 로고
    • World Health Organization, Fact sheet on tuberculosis, 2005, .
    • World Health Organization, Fact sheet on tuberculosis, 2005, .
  • 3
    • 34250198660 scopus 로고    scopus 로고
    • The Mycobacterium tuberculosis FAS-II condensing enzymes: their role in mycolic acid biosynthesis, acid-fastness, pathogenesis and in future drug development
    • Bhatt A., Molle V., Besra G.S., Jacobs Jr. W.R., and Kremer L. The Mycobacterium tuberculosis FAS-II condensing enzymes: their role in mycolic acid biosynthesis, acid-fastness, pathogenesis and in future drug development. Mol. Microbiol. 64 6 (2007) 1442-1454
    • (2007) Mol. Microbiol. , vol.64 , Issue.6 , pp. 1442-1454
    • Bhatt, A.1    Molle, V.2    Besra, G.S.3    Jacobs Jr., W.R.4    Kremer, L.5
  • 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
  • 5
    • 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
  • 6
    • 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 2 (2001) 167-173
    • (2001) Nat. Med. , vol.7 , Issue.2 , pp. 167-173
    • Surolia, N.1    Surolia, A.2
  • 7
    • 2942746756 scopus 로고    scopus 로고
    • The potential of bacterial fatty acid biosynthetic enzymes as a source of novel antibacterial agents
    • Payne D.J. The potential of bacterial fatty acid biosynthetic enzymes as a source of novel antibacterial agents. Drug News Perspect. 17 3 (2004) 187-194
    • (2004) Drug News Perspect. , vol.17 , Issue.3 , pp. 187-194
    • Payne, D.J.1
  • 8
    • 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
  • 9
    • 33847779109 scopus 로고    scopus 로고
    • Enoyl reductases as targets for the development of anti-tubercular and anti-malarial agents
    • Oliveira J.S., Vasconcelos I.B., Moreira I.S., Santos D.S., and Basso L.A. Enoyl reductases as targets for the development of anti-tubercular and anti-malarial agents. Curr. Drug Targets 8 3 (2007) 399-411
    • (2007) Curr. Drug Targets , vol.8 , Issue.3 , pp. 399-411
    • Oliveira, J.S.1    Vasconcelos, I.B.2    Moreira, I.S.3    Santos, D.S.4    Basso, L.A.5
  • 11
    • 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
  • 12
    • 33847401359 scopus 로고    scopus 로고
    • Green tea catechins potentiate 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 potentiate triclosan binding to enoyl-ACP reductase from Plasmodium falciparum (PfENR). J. Med. Chem. 50 4 (2007) 765-775
    • (2007) J. Med. Chem. , vol.50 , Issue.4 , pp. 765-775
    • Sharma, S.K.1    Parasuraman, P.2    Kumar, G.3    Surolia, N.4    Surolia, A.5
  • 13
    • 0033709606 scopus 로고    scopus 로고
    • Isoniazid affects multiple components of the type II fatty acid synthase system of Mycobacterium tuberculosis
    • Slayden R.A., Lee R.E., and Barry III C.E. Isoniazid affects multiple components of the type II fatty acid synthase system of Mycobacterium tuberculosis. Mol. Microbiol. 38 3 (2000) 514-525
    • (2000) Mol. Microbiol. , vol.38 , Issue.3 , pp. 514-525
    • Slayden, R.A.1    Lee, R.E.2    Barry III, C.E.3
  • 14
    • 17644436310 scopus 로고    scopus 로고
    • Inhibition of InhA, the enoyl reductase from Mycobacterium tuberculosis, by triclosan and isoniazid
    • Parikh S.L., Xiao G., and Tonge P.J. Inhibition of InhA, the enoyl reductase from Mycobacterium tuberculosis, by triclosan and isoniazid. Biochemistry 39 26 (2000) 7645-7650
    • (2000) Biochemistry , vol.39 , Issue.26 , pp. 7645-7650
    • Parikh, S.L.1    Xiao, G.2    Tonge, P.J.3
  • 15
    • 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
  • 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
  • 18
    • 30944455694 scopus 로고    scopus 로고
    • Green tea polyphenol inhibits Mycobacterium tuberculosis survival within human macrophages
    • Anand P.K., Kaul D., and Sharma M. Green tea polyphenol inhibits Mycobacterium tuberculosis survival within human macrophages. Int. J. Biochem. Cell. Biol. 38 4 (2006) 600-609
    • (2006) Int. J. Biochem. Cell. Biol. , vol.38 , Issue.4 , pp. 600-609
    • Anand, P.K.1    Kaul, D.2    Sharma, M.3
  • 19
    • 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
    • Parikh S., Moynihan D.P., Xiao G., and Tonge P.J. 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
  • 20
    • 84969001783 scopus 로고
    • The attraction of proteins for small molecules and ions
    • Scatchard G. The attraction of proteins for small molecules and ions. Ann. N.Y. Acad. Sci. 51 (1949) 660
    • (1949) Ann. N.Y. Acad. Sci. , vol.51 , pp. 660
    • Scatchard, G.1
  • 24
    • 39149084759 scopus 로고    scopus 로고
    • Molecular Operating Environment [MOE 2001.07], Chemical Computing Group Inc., 1255 University St., Suite 1600, Montreal, Que., Canada H3B 3X3.
    • Molecular Operating Environment [MOE 2001.07], Chemical Computing Group Inc., 1255 University St., Suite 1600, Montreal, Que., Canada H3B 3X3.
  • 25
    • 33750111588 scopus 로고    scopus 로고
    • Pyrrolidine carboxamides as a novel class of inhibitors of enoyl acyl carrier protein reductase from Mycobacterium tuberculosis
    • He X., Alian A., Stroud R., and Ortiz de Montellano P.R. Pyrrolidine carboxamides as a novel class of inhibitors of enoyl acyl carrier protein reductase from Mycobacterium tuberculosis. J. Med. Chem. 49 21 (2006) 6308-6323
    • (2006) J. Med. Chem. , vol.49 , Issue.21 , pp. 6308-6323
    • He, X.1    Alian, A.2    Stroud, R.3    Ortiz de Montellano, P.R.4
  • 26
    • 33947651030 scopus 로고    scopus 로고
    • Development of modern InhA inhibitors to combat drug resistant strains of Mycobacterium tuberculosis
    • Tonge P.J., Kisker C., and Slayden R.A. Development of modern InhA inhibitors to combat drug resistant strains of Mycobacterium tuberculosis. Curr. Top. Med. Chem. 7 5 (2007) 489-498
    • (2007) Curr. Top. Med. Chem. , vol.7 , Issue.5 , pp. 489-498
    • Tonge, P.J.1    Kisker, C.2    Slayden, R.A.3
  • 27
    • 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 1 (2004) 147-155
    • (2004) J. Mol. Biol. , vol.343 , Issue.1 , pp. 147-155
    • Pidugu, L.S.1    Kapoor, M.2    Surolia, N.3    Surolia, A.4    Suguna, K.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.