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Volumn 6, Issue 1, 2008, Pages 95-103

Identification of an inhibitor of the MurC enzyme, which catalyzes an essential step in the peptidoglycan precursor synthesis pathway

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE; BACTERIAL ENZYME; C 1; ENZYME INHIBITOR; MURC ENZYME; MURC ENZYME INHIBITOR; PEPTIDOGLYCAN; PROTEIN PRECURSOR; UNCLASSIFIED DRUG;

EID: 40749131703     PISSN: 1540658X     EISSN: None     Source Type: Journal    
DOI: 10.1089/adt.2007.114     Document Type: Article
Times cited : (21)

References (35)
  • 1
    • 0035018011 scopus 로고    scopus 로고
    • Formation of the glycan chains in the synthesis of bacterial peptidoglycan
    • van Heijenoort J: Formation of the glycan chains in the synthesis of bacterial peptidoglycan. Glycobiology 2001;11:25R-36R.
    • (2001) Glycobiology , vol.11
    • van Heijenoort, J.1
  • 2
    • 0347538562 scopus 로고    scopus 로고
    • Antibiotics that act on cell wall biosynthesis
    • ASM Press, Washington, DC
    • Walsh C: Antibiotics that act on cell wall biosynthesis. In: Antibiotics - Actions, Origins, Resistance, pp. 23-49. ASM Press, Washington, DC, 2003.
    • (2003) Antibiotics - Actions, Origins, Resistance , pp. 23-49
    • Walsh, C.1
  • 3
    • 33748324503 scopus 로고    scopus 로고
    • Structure, function and dynamics in the Mur family of bacterial cell wall ligases
    • Smith CA: Structure, function and dynamics in the Mur family of bacterial cell wall ligases. J Mol Biol 2006;362:640-655.
    • (2006) J Mol Biol , vol.362 , pp. 640-655
    • Smith, C.A.1
  • 4
    • 2342623377 scopus 로고    scopus 로고
    • Biochemical characterization of an inhibitor of Escherichia coli UDP-N-acetylmuramyl-L-alanine ligase
    • Ehmann DE, Demerit JE, Hull KG, Fisher SL: Biochemical characterization of an inhibitor of Escherichia coli UDP-N-acetylmuramyl-L-alanine ligase. Biochim Biophys Acta 2004;1698:167-174.
    • (2004) Biochim Biophys Acta , vol.1698 , pp. 167-174
    • Ehmann, D.E.1    Demerit, J.E.2    Hull, K.G.3    Fisher, S.L.4
  • 5
    • 0035833985 scopus 로고    scopus 로고
    • Biochemical characterization of a phosphinate inhibitor of Escherichia coli MurC
    • Marmor S, Peterson CP, Reck F, Yang W, Gao N, Fisher SL: Biochemical characterization of a phosphinate inhibitor of Escherichia coli MurC. Biochemistry 2001;40:12207-12214.
    • (2001) Biochemistry , vol.40 , pp. 12207-12214
    • Marmor, S.1    Peterson, C.P.2    Reck, F.3    Yang, W.4    Gao, N.5    Fisher, S.L.6
  • 6
    • 0035806048 scopus 로고    scopus 로고
    • Inhibitors of the bacterial cell wall biosynthesis enzyme MurC
    • Reck F, Marmor S, Fisher S, Wuonola MA: Inhibitors of the bacterial cell wall biosynthesis enzyme MurC. Bioorg Med Chem Lett 2001;11:1451-1454.
    • (2001) Bioorg Med Chem Lett , vol.11 , pp. 1451-1454
    • Reck, F.1    Marmor, S.2    Fisher, S.3    Wuonola, M.A.4
  • 9
    • 0019766646 scopus 로고
    • Inhibition of cell wall biosynthesis by analogues and alanine
    • Neuhaus FC, Hammes WP: Inhibition of cell wall biosynthesis by analogues and alanine. Pharmacol Ther 1981;14:265-319.
    • (1981) Pharmacol Ther , vol.14 , pp. 265-319
    • Neuhaus, F.C.1    Hammes, W.P.2
  • 10
    • 0037223505 scopus 로고    scopus 로고
    • Structure and function of the Mur enzymes: Development of novel inhibitors
    • El Zoeiby A, Sanschagrin F, Levesque RC: Structure and function of the Mur enzymes: development of novel inhibitors. Mol Microbiol 2003;47:1-12.
    • (2003) Mol Microbiol , vol.47 , pp. 1-12
    • El Zoeiby, A.1    Sanschagrin, F.2    Levesque, R.C.3
  • 11
    • 33845894155 scopus 로고    scopus 로고
    • Multi-targeting by monotherapeutic antibacterials
    • Silver LL: Multi-targeting by monotherapeutic antibacterials. Nat Rev Drug Discov 2007;6:41-55.
    • (2007) Nat Rev Drug Discov , vol.6 , pp. 41-55
    • Silver, L.L.1
  • 12
    • 0030880888 scopus 로고    scopus 로고
    • Invariant amino acids in the Mur peptide synthetases of bacterial peptidoglycan synthesis and their modification by site-directed mutagenesis in the UDP-MurNAc: L-alanine ligase from Escherichia coli
    • Bouhss A, Mengin-Lecreulx D, Blanot D, van Heijenoort J, Parquet C: Invariant amino acids in the Mur peptide synthetases of bacterial peptidoglycan synthesis and their modification by site-directed mutagenesis in the UDP-MurNAc: L-alanine ligase from Escherichia coli. Biochemistry 1997;36:11556-11563.
    • (1997) Biochemistry , vol.36 , pp. 11556-11563
    • Bouhss, A.1    Mengin-Lecreulx, D.2    Blanot, D.3    van Heijenoort, J.4    Parquet, C.5
  • 14
    • 33845509079 scopus 로고    scopus 로고
    • Structure of Escherichia coli UDP-N-acetylmuramoyl:L-alanine ligase (MurC)
    • Deva T, Baker EN, Squire CJ, Smith CA: Structure of Escherichia coli UDP-N-acetylmuramoyl:L-alanine ligase (MurC). Acta Cryst D 2006;62:1466-1474.
    • (2006) Acta Cryst D , vol.62 , pp. 1466-1474
    • Deva, T.1    Baker, E.N.2    Squire, C.J.3    Smith, C.A.4
  • 15
    • 0035815667 scopus 로고    scopus 로고
    • Crystal structure of UDP-N-acetylmurmoyl-L-alanyl- D-glutamate:meso-diaminopimelate ligase from Escherichia coli
    • Gordon E, Flouret B, Chantalat L, van Heijenoort J, Mengin-Lecreulx D, Dideberg O: Crystal structure of UDP-N-acetylmurmoyl-L-alanyl- D-glutamate:meso-diaminopimelate ligase from Escherichia coli. J Biol Chem 2001;276:10999-11006.
    • (2001) J Biol Chem , vol.276 , pp. 10999-11006
    • Gordon, E.1    Flouret, B.2    Chantalat, L.3    van Heijenoort, J.4    Mengin-Lecreulx, D.5    Dideberg, O.6
  • 17
    • 0038492584 scopus 로고    scopus 로고
    • Crystal structures of active fully assembled substrate- and product-bound complexes of UDP-N-acetylmuramic acid:L-alanine ligase (MurC) from Haemophilus influenzae
    • Mol CD, Brooun A, Dougan DR, Hilgers MT, Tari LW, Wijnands RA, et al.: Crystal structures of active fully assembled substrate- and product-bound complexes of UDP-N-acetylmuramic acid:L-alanine ligase (MurC) from Haemophilus influenzae. J Bacteriol 2003;185:4152-4162.
    • (2003) J Bacteriol , vol.185 , pp. 4152-4162
    • Mol, C.D.1    Brooun, A.2    Dougan, D.R.3    Hilgers, M.T.4    Tari, L.W.5    Wijnands, R.A.6
  • 18
    • 0034423412 scopus 로고    scopus 로고
    • Crystal structure of Escherichia coli UDP-MurNAc-tripeptide D-alanyl- D-alanine-adding enzyme (MurF) at 2.3 Å resolution
    • Yan Y, Munshi S, Leiting B, Anderson MS, Chrzas J, Chen Z: Crystal structure of Escherichia coli UDP-MurNAc-tripeptide D-alanyl- D-alanine-adding enzyme (MurF) at 2.3 Å resolution. J Mol Biol 2000;304:435-445.
    • (2000) J Mol Biol , vol.304 , pp. 435-445
    • Yan, Y.1    Munshi, S.2    Leiting, B.3    Anderson, M.S.4    Chrzas, J.5    Chen, Z.6
  • 19
    • 0031007336 scopus 로고    scopus 로고
    • Conditionally lethal Escherichia coli murein mutants contain point defects that map to regions conserved among murein and folyl poly-γ-glutamate ligases: Identification of a ligase superfamily
    • Eveland SS, Pompliano DL, Anderson MS: Conditionally lethal Escherichia coli murein mutants contain point defects that map to regions conserved among murein and folyl poly-γ-glutamate ligases: identification of a ligase superfamily. Biochemistry 1997;36:6223-6229.
    • (1997) Biochemistry , vol.36 , pp. 6223-6229
    • Eveland, S.S.1    Pompliano, D.L.2    Anderson, M.S.3
  • 20
    • 0032768860 scopus 로고    scopus 로고
    • Formation of adenosine 5′-tetraphosphate from the acyl phosphate intermediate: A difference between the MurC and MurD synthetases of Escherichia coli
    • Bouhss A, Dementin S, van Heijenoort J, Parquet C, Blanot D: Formation of adenosine 5′-tetraphosphate from the acyl phosphate intermediate: a difference between the MurC and MurD synthetases of Escherichia coli. FEBS Lett 1999;453:15-19.
    • (1999) FEBS Lett , vol.453 , pp. 15-19
    • Bouhss, A.1    Dementin, S.2    van Heijenoort, J.3    Parquet, C.4    Blanot, D.5
  • 21
    • 0030960337 scopus 로고    scopus 로고
    • Evaluation of the kinetic mechanism of Escherichia coli uridine diphosphate-N-acetylmuramate:L-alanine ligase
    • Emanuele JJ, Jin H, Yanchunas J, Villafranca JJ: Evaluation of the kinetic mechanism of Escherichia coli uridine diphosphate-N-acetylmuramate:L-alanine ligase. Biochemistry 1997;36:7264-7271.
    • (1997) Biochemistry , vol.36 , pp. 7264-7271
    • Emanuele, J.J.1    Jin, H.2    Yanchunas, J.3    Villafranca, J.J.4
  • 22
    • 0030020538 scopus 로고    scopus 로고
    • Biochemical evidence for the formation of a covalent acyl-phosphate linkage between UDP-N-acetylmuramate and ATP in the Escherichia coli UDP-N-acetylmuramate:L-alanine ligase-catalyzed reaction
    • Falk PJ, Ervin KM, Volk KS, Ho H-T: Biochemical evidence for the formation of a covalent acyl-phosphate linkage between UDP-N-acetylmuramate and ATP in the Escherichia coli UDP-N-acetylmuramate:L-alanine ligase-catalyzed reaction. Biochemistry 1996;35:1417-1422.
    • (1996) Biochemistry , vol.35 , pp. 1417-1422
    • Falk, P.J.1    Ervin, K.M.2    Volk, K.S.3    Ho, H.-T.4
  • 23
    • 0029077340 scopus 로고
    • Over-production, purification and properties of the uridine-diphosphate- N-acetylmuramate:L-alanine ligase from Escherichia coli
    • Liger D, Masson A, Blanot D, van Heijenoort J, Parquet C: Over-production, purification and properties of the uridine-diphosphate- N-acetylmuramate:L-alanine ligase from Escherichia coli. Eur J Biochem 1995;230:80-87.
    • (1995) Eur J Biochem , vol.230 , pp. 80-87
    • Liger, D.1    Masson, A.2    Blanot, D.3    van Heijenoort, J.4    Parquet, C.5
  • 24
    • 3943067061 scopus 로고    scopus 로고
    • Drug discovery
    • Mullin R: Drug discovery. Chem Eng News 2004;82:23-32.
    • (2004) Chem Eng News , vol.82 , pp. 23-32
    • Mullin, R.1
  • 26
    • 0037061628 scopus 로고    scopus 로고
    • A common mechanism underlying promiscuous inhibitors from virtual and high-throughput screening
    • McGovern SL, Caselli E, Grigorieff N, Shoichet BK: A common mechanism underlying promiscuous inhibitors from virtual and high-throughput screening. J Med Chem 2002;45:1712-1722.
    • (2002) J Med Chem , vol.45 , pp. 1712-1722
    • McGovern, S.L.1    Caselli, E.2    Grigorieff, N.3    Shoichet, B.K.4
  • 29
    • 34547534673 scopus 로고    scopus 로고
    • Probing the barrier function of the outer membrane with chemical conditionality
    • Ruiz N, Wu T, Kahne D, Silhavy TJ: Probing the barrier function of the outer membrane with chemical conditionality. ACS Chem Biol 2006;1:385-395.
    • (2006) ACS Chem Biol , vol.1 , pp. 385-395
    • Ruiz, N.1    Wu, T.2    Kahne, D.3    Silhavy, T.J.4
  • 30
    • 0024506353 scopus 로고
    • A collection of strains containing genetically linked alternating antibiotic resistance elements for genetic mapping of Escherichia coli
    • Singer M, Baker TA, Schnitzler G, Deischel SM, Goel M, Dove W, et al.: A collection of strains containing genetically linked alternating antibiotic resistance elements for genetic mapping of Escherichia coli. Microbiol Rev 1989;53:1-24.
    • (1989) Microbiol Rev , vol.53 , pp. 1-24
    • Singer, M.1    Baker, T.A.2    Schnitzler, G.3    Deischel, S.M.4    Goel, M.5    Dove, W.6
  • 31
    • 0033003760 scopus 로고    scopus 로고
    • A simple statistical parameter for use in evaluation and validation of high throughput screening assays
    • Zhang J-H, Chung TDY, Oldenburg KR: A simple statistical parameter for use in evaluation and validation of high throughput screening assays. J Biomol Screen 1999;4:67-75.
    • (1999) J Biomol Screen , vol.4 , pp. 67-75
    • Zhang, J.-H.1    Chung, T.D.Y.2    Oldenburg, K.R.3
  • 32
    • 0034181706 scopus 로고    scopus 로고
    • Confirmation of primary active substances from high throughput screening of chemical and biological populations: A statistical approach and practical considerations
    • Zhang J-H, Chung TDY, Oldenburg KR: Confirmation of primary active substances from high throughput screening of chemical and biological populations: a statistical approach and practical considerations. J Comb Chem 2000;2:258-265.
    • (2000) J Comb Chem , vol.2 , pp. 258-265
    • Zhang, J.-H.1    Chung, T.D.Y.2    Oldenburg, K.R.3
  • 33
    • 0034665744 scopus 로고    scopus 로고
    • Structural and functional similarities in the ADP-forming amidebond ligase superfamily: Implications for a substrate-induced conformational change in folylpolyglutamate synthetase
    • Sheng Y, Sun X, Shen Y, Bognar AL, Smith CA: Structural and functional similarities in the ADP-forming amidebond ligase superfamily: implications for a substrate-induced conformational change in folylpolyglutamate synthetase. J Mol Biol 2000;302:427-440.
    • (2000) J Mol Biol , vol.302 , pp. 427-440
    • Sheng, Y.1    Sun, X.2    Shen, Y.3    Bognar, A.L.4    Smith, C.A.5
  • 34
    • 0020443521 scopus 로고
    • Complete analysis of cellular nucleotides by two-dimensional thin layer chromatography
    • Bochner BR, Ames BN: Complete analysis of cellular nucleotides by two-dimensional thin layer chromatography. J Biol Chem 1982;257:9759-9769.
    • (1982) J Biol Chem , vol.257 , pp. 9759-9769
    • Bochner, B.R.1    Ames, B.N.2
  • 35
    • 0030571267 scopus 로고    scopus 로고
    • On-line monitoring of intracellular ATP concentrations in Escherichia coli fermentations
    • Lasko DR, Wang DIC: On-line monitoring of intracellular ATP concentrations in Escherichia coli fermentations. Biotechnol Bioeng 1996;52:364-372.
    • (1996) Biotechnol Bioeng , vol.52 , pp. 364-372
    • Lasko, D.R.1    Wang, D.I.C.2


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