메뉴 건너뛰기




Volumn 19, Issue 12, 2009, Pages 1582-1589

Inhibitory mechanism of novel inhibitors of UDP-N-acetylglucosamine enolpyruvyl transferase from Haemophilus influenzae

Author keywords

Cell wall synthesis; Cys117 loop; Haemophilus influenzae; Inhibitors; MurA

Indexed keywords

BACTERIAL ENZYME; CYSTEINE; EBSELEN; FOSFOMYCIN; THIOL DERIVATIVE; THIOMERSAL; THIRAM; UNCLASSIFIED DRUG; URIDINE DIPHOSPHATE N ACETYLGLUCOSAMINE ENOLPYRUVYLTRANSFERASE;

EID: 74749100120     PISSN: 10177825     EISSN: 17388872     Source Type: Journal    
DOI: 10.4014/jmb.0905.05036     Document Type: Article
Times cited : (16)

References (28)
  • 1
    • 0030854329 scopus 로고    scopus 로고
    • Plasmid-encoded fosfomycin resistance in bacteria isolated from the urinary tract in a multicenter survey
    • Arca, P., G. Reguera, and C. Hardisson. 1997. Plasmid-encoded fosfomycin resistance in bacteria isolated from the urinary tract in a multicenter survey. J. Antimicrob. Chemother. 40: 393-399.
    • (1997) J. Antimicrob. Chemother , vol.40 , pp. 393-399
    • Arca, P.1    Reguera, G.2    Hardisson, C.3
  • 3
    • 0041589365 scopus 로고    scopus 로고
    • Thimerosal induces DNA breaks, caspase-3 activation, membrane damage, and cell death in cultured human neurons and fibroblasts
    • Baskin, D. S., H. Ngo, and V. V. Didenko. 2003. Thimerosal induces DNA breaks, caspase-3 activation, membrane damage, and cell death in cultured human neurons and fibroblasts. Toxicol. Sci. 74: 361-368.
    • (2003) Toxicol. Sci , vol.74 , pp. 361-368
    • Baskin, D.S.1    Ngo, H.2    Didenko, V.V.3
  • 5
    • 0342618500 scopus 로고    scopus 로고
    • Fosfomycin resistance protein (FosA) is a manganese metalloglutathione transferase related to glyoxalase I and the extradiol dioxygenases
    • Bernat, B. A., L. T. Laughlin, and R. N. Armstrong. 1997. Fosfomycin resistance protein (FosA) is a manganese metalloglutathione transferase related to glyoxalase I and the extradiol dioxygenases. Biochemistry 36: 3050-3055.
    • (1997) Biochemistry , vol.36 , pp. 3050-3055
    • Bernat, B.A.1    Laughlin, L.T.2    Armstrong, R.N.3
  • 6
    • 0029064598 scopus 로고
    • MurA (MurZ), the enzyme that catalyzes the first committed step in peptidoglycan biosynthesis, is essential in Escherichia coli
    • Brown, E. D., E. I. Vivas, C. T. Walsh, and R. Kolter. 1995. MurA (MurZ), the enzyme that catalyzes the first committed step in peptidoglycan biosynthesis, is essential in Escherichia coli. J. Bacteriol. 177: 4194-4197.
    • (1995) J. Bacteriol , vol.177 , pp. 4194-4197
    • Brown, E.D.1    Vivas, E.I.2    Walsh, C.T.3    Kolter, R.4
  • 7
    • 0026880575 scopus 로고
    • Intracellular steps of bacterial cell wall peptidoglycan biosynthesis: Enzymology, antibiotics, and antibiotic resistance
    • Bugg. T. D. and C. T. Walsh. 1992. Intracellular steps of bacterial cell wall peptidoglycan biosynthesis: Enzymology, antibiotics, and antibiotic resistance. Nat. Prod. Rep. 9: 199-215.
    • (1992) Nat. Prod. Rep , vol.9 , pp. 199-215
    • Bugg, T.D.1    Walsh, C.T.2
  • 8
    • 0014622610 scopus 로고
    • Advances in techniques of testing mycobacterial drug sensitivity, and the use of sensitivity tests in tuberculosis control programs
    • Canetti, G., W. Fox, A. Khomenko, H. T. Mahler, N. K. Menon, D. A. Mitchison, N. Rist, and N. A. Smelev. 1969. Advances in techniques of testing mycobacterial drug sensitivity, and the use of sensitivity tests in tuberculosis control programs. Bull. World Health Organ. 41: 21-43.
    • (1969) Bull. World Health Organ , vol.41 , pp. 21-43
    • Canetti, G.1    Fox, W.2    Khomenko, A.3    Mahler, H.T.4    Menon, N.K.5    Mitchison, D.A.6    Rist, N.7    Smelev, N.A.8
  • 10
    • 85030519821 scopus 로고    scopus 로고
    • Performance Standards for Antimicrobial Susceptibility Testing
    • Clinical and Laboratory Standards Institute, Wayne, Pa
    • Clinical and Laboratory Standards Institute. 2006. Performance Standards for Antimicrobial Susceptibility Testing. Sixteenth Informational Supplement M100-S16, Wayne, Pa.
    • (2006) Sixteenth Informational , Issue.SUPPL.EMENT M100-S16
  • 12
    • 13544252827 scopus 로고    scopus 로고
    • Evidence that the fosfomycin target Cys115 in UDP-N-acetylglucosamine enolpyruvyl transferase (MurA) is essential for product release
    • Eschenburg, S., M. Priestman, and E. Schonbrunn. 2005. Evidence that the fosfomycin target Cys115 in UDP-N-acetylglucosamine enolpyruvyl transferase (MurA) is essential for product release. J. Biol. Chem. 280: 3757-3763.
    • (2005) J. Biol. Chem , vol.280 , pp. 3757-3763
    • Eschenburg, S.1    Priestman, M.2    Schonbrunn, E.3
  • 13
    • 0032891974 scopus 로고    scopus 로고
    • Emergence of fosfomycin-resistant isolates of Shiga-like toxin-producing Escherichia coli O26
    • Horii, T., T. Kimura, K. Sato, K. Shibayama, and M. Ohta. 1999. Emergence of fosfomycin-resistant isolates of Shiga-like toxin-producing Escherichia coli O26. Antimicrob. Agents Chemother. 43: 789-793
    • (1999) Antimicrob. Agents Chemother , vol.43 , pp. 789-793
    • Horii, T.1    Kimura, T.2    Sato, K.3    Shibayama, K.4    Ohta, M.5
  • 15
    • 0029967416 scopus 로고    scopus 로고
    • Characterization of a Cys115 to Asp substitution in the Escherichia coli cell wall biosynthetic enzyme UDP-GlcNAc enolpyruvyl transferase (MurA) that confers resistance to inactivation by the antibiotic fosfomycin
    • Kim, D. H., W. J. Lees, K. E. Kempsell, W. S. Lane, K. Duncan, and C. T. Walsh. 1996. Characterization of a Cys115 to Asp substitution in the Escherichia coli cell wall biosynthetic enzyme UDP-GlcNAc enolpyruvyl transferase (MurA) that confers resistance to inactivation by the antibiotic fosfomycin. Biochemistry 35: 4923-4928.
    • (1996) Biochemistry , vol.35 , pp. 4923-4928
    • Kim, D.H.1    Lees, W.J.2    Kempsell, K.E.3    Lane, W.S.4    Duncan, K.5    Walsh, C.T.6
  • 16
    • 0028070055 scopus 로고
    • Kinetics, stoichiometry, and identification of the reactive thiolate in the inactivation of UDP-GlcNac enolpyruvyl transferase by the antibiotic fosfomycin
    • Marquardt, J. L., E. D. Brown, W. S. Lane, T. M. Haley, Y. Ichikawa, C.-H. Wong, and C. T. Walsh. 1994. Kinetics, stoichiometry, and identification of the reactive thiolate in the inactivation of UDP-GlcNac enolpyruvyl transferase by the antibiotic fosfomycin. Biochemistry 33: 10646-10651.
    • (1994) Biochemistry , vol.33 , pp. 10646-10651
    • Marquardt, J.L.1    Brown, E.D.2    Lane, W.S.3    Haley, T.M.4    Ichikawa, Y.5    Wong, C.-H.6    Walsh, C.T.7
  • 17
    • 0026803196 scopus 로고
    • Cloning and sequencing of Escherichia coli mreZ and purification of its product, a UDP-N-acetylglucosamine enolpyruvyl transferase
    • Marquardt, J. L., D. A. Siegele, R. Kolter, and C. T. Walsh. 1992. Cloning and sequencing of Escherichia coli mreZ and purification of its product, a UDP-N-acetylglucosamine enolpyruvyl transferase. J. Bacteriol. 174: 5748-5752.
    • (1992) J. Bacteriol , vol.174 , pp. 5748-5752
    • Marquardt, J.L.1    Siegele, D.A.2    Kolter, R.3    Walsh, C.T.4
  • 18
    • 0030566871 scopus 로고    scopus 로고
    • Kinetic study of the reaction of ebselen with peroxynitrite
    • Masumoto, H., R. Kissner, W. H. Koppenol, and H. Sies. 1996. Kinetic study of the reaction of ebselen with peroxynitrite. FEBS Lett. 398: 179-182.
    • (1996) FEBS Lett , vol.398 , pp. 179-182
    • Masumoto, H.1    Kissner, R.2    Koppenol, W.H.3    Sies, H.4
  • 19
    • 33751094053 scopus 로고    scopus 로고
    • A peptide inhibitor of MurA UDP-N-acetylglucosamine enolpyruvyl transferase: The first committed step in peptidoglycan biosynthesis
    • Molina-Lopez, J., F. Sanschagrin, and R. C. Levesque. 2006. A peptide inhibitor of MurA UDP-N-acetylglucosamine enolpyruvyl transferase: The first committed step in peptidoglycan biosynthesis. Peptides 27: 3115-3121.
    • (2006) Peptides , vol.27 , pp. 3115-3121
    • Molina-Lopez, J.1    Sanschagrin, F.2    Levesque, R.C.3
  • 20
    • 0024316299 scopus 로고
    • Susceptibility of methicillin-resistant Staphylococcus aureus to the selenium-containing compound 2-phenyl-1,2-benzoisoselenazol-3(2H)-one (PZ51)
    • Nozawa, R., T. Yokoda, and T. Fujimoto. 1989. Susceptibility of methicillin-resistant Staphylococcus aureus to the selenium-containing compound 2-phenyl-1,2-benzoisoselenazol-3(2H)-one (PZ51). Antimicrob. Agents Chemother. 33: 1388-1390.
    • (1989) Antimicrob. Agents Chemother , vol.33 , pp. 1388-1390
    • Nozawa, R.1    Yokoda, T.2    Fujimoto, T.3
  • 21
    • 0018416496 scopus 로고
    • Elleman's reagent: 5,5′ Dithiobis (2-nitrobenzoic acid) - a reexamination
    • Riddles, P. W., R. L. Blakeley, and B. Zerner. 1979. Elleman's reagent: 5,5′ Dithiobis (2-nitrobenzoic acid) - a reexamination. Anal. Biochem. 94: 75-81.
    • (1979) Anal. Biochem , vol.94 , pp. 75-81
    • Riddles, P.W.1    Blakeley, R.L.2    Zerner, B.3
  • 22
    • 0029114721 scopus 로고
    • Molecular actions of ebselen-an antiinflammatory antioxidant
    • 1589 Jin et al
    • Schewe, T. 1995. Molecular actions of ebselen-an antiinflammatory antioxidant. Gen. Pharmacol. 26: 1153-1169. 1589 Jin et al.
    • (1995) Gen. Pharmacol , vol.26 , pp. 1153-1169
    • Schewe, T.1
  • 23
    • 0034612339 scopus 로고    scopus 로고
    • Structural basis for the interaction of the fluorescence probe 8-anilino-1-naphthalene sulfonate (ANS) with the antibiotic target MurA
    • Schonbrunn, E., S. Schenburg, K. Luger, W. Kabsch, and N. Amrhein. 2000. Structural basis for the interaction of the fluorescence probe 8-anilino-1-naphthalene sulfonate (ANS) with the antibiotic target MurA. Proc. Natl. Acad. Sci. U.S.A. 97: 6345-6349.
    • (2000) Proc. Natl. Acad. Sci. U.S.A , vol.97 , pp. 6345-6349
    • Schonbrunn, E.1    Schenburg, S.2    Luger, K.3    Kabsch, W.4    Amrhein, N.5
  • 24
    • 0032522591 scopus 로고    scopus 로고
    • Studies on the conformational changes in the bacterial cell wall biosynthetic enzyme UDP-N-acetylglucosamine enolpyruvyltransferase (MurA)
    • Schonbrunn, E., D. I. Svergun, N. Amrhein, and M. H. J. Koch. 1998. Studies on the conformational changes in the bacterial cell wall biosynthetic enzyme UDP-N-acetylglucosamine enolpyruvyltransferase (MurA). Eur. J. Biochem. 253: 406-412.
    • (1998) Eur. J. Biochem , vol.253 , pp. 406-412
    • Schonbrunn, E.1    Svergun, D.I.2    Amrhein, N.3    Koch, M.H.J.4
  • 25
    • 0142030488 scopus 로고    scopus 로고
    • Thiram: Degradation, applications and analytical methods
    • Sharma, V. K., J. S. Aulakh, and A. K. Malik. 2003. Thiram: Degradation, applications and analytical methods. J. Environ. Monit. 5: 717-723.
    • (2003) J. Environ. Monit , vol.5 , pp. 717-723
    • Sharma, V.K.1    Aulakh, J.S.2    Malik, A.K.3
  • 26
    • 0030589610 scopus 로고    scopus 로고
    • Structure of UDP-N-acetylglucosamine enolpyruvyl transferase, an enzyme essential for the synthesis of bacterial peptidoglycan, complexed with substrate UDP-N-acetylglucosamine and the drug fosfomycin
    • Skarzynski, T., A. Mistry, A. Wonacott, S. E. Hutchinson, V. A. Kelly, and K. Duncan. 1996. Structure of UDP-N-acetylglucosamine enolpyruvyl transferase, an enzyme essential for the synthesis of bacterial peptidoglycan, complexed with substrate UDP-N-acetylglucosamine and the drug fosfomycin. Structure 4: 1465-1474.
    • (1996) Structure , vol.4 , pp. 1465-1474
    • Skarzynski, T.1    Mistry, A.2    Wonacott, A.3    Hutchinson, S.E.4    Kelly, V.A.5    Duncan, K.6
  • 27
    • 27244449189 scopus 로고    scopus 로고
    • Crystallization and preliminary X-ray crystallographic analysis of UDP-N-acetylglucosamine enolpyruvyl transferase from Haemophilus influenzae in complex with UDP-N-acetylglucosamine and fosfomycin
    • Yoon, H. J., M. J. Ku, H. J. Ahn, B. I. Lee, B. Mikami, and S. W. Suh. 2005. Crystallization and preliminary X-ray crystallographic analysis of UDP-N-acetylglucosamine enolpyruvyl transferase from Haemophilus influenzae in complex with UDP-N-acetylglucosamine and fosfomycin. Mol. Cells 19: 398-401.
    • (2005) Mol. Cells , vol.19 , pp. 398-401
    • Yoon, H.J.1    Ku, M.J.2    Ahn, H.J.3    Lee, B.I.4    Mikami, B.5    Suh, S.W.6
  • 28
    • 41149117918 scopus 로고    scopus 로고
    • Crystal structure of UDP-N-acetylglucosamine enolpyruvyl transferase from Haemophilus influenza in complex with DSP-N-acetylglucosamine and fosfomycin
    • Yoon, H. J., S. J. Lee, B. Mikami, H. J. Park, J. Yoo, and S. W. Suh. 2008. Crystal structure of UDP-N-acetylglucosamine enolpyruvyl transferase from Haemophilus influenza in complex with DSP-N-acetylglucosamine and fosfomycin. Proteins 71: 1032-1037.
    • (2008) Proteins , vol.71 , pp. 1032-1037
    • Yoon, H.J.1    Lee, S.J.2    Mikami, B.3    Park, H.J.4    Yoo, J.5    Suh, S.W.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.