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Volumn 6, Issue 1, 2002, Pages 1-20

The bacterial cell wall as a source of antibacterial targets

Author keywords

Antibiotic; Cell wall; Glycopeptide; Murein; Penicillin; Peptidoglycan; Target based drug discovery; Transglycosylation; Transpeptidation; Vancomycin; lactam

Indexed keywords

4 THIAZOLIDINONE DERIVATIVE; ANTIINFECTIVE AGENT; BETA LACTAM; BETA LACTAMASE; BETA LACTAMASE INHIBITOR; CARBAPENEM; CARBAPENEM DERIVATIVE; CEFALEXIN; CEPHALOSPORIN DERIVATIVE; CLAVULANIC ACID; DESLEUCYL CHLOROBIPHENYL VANCOMYCIN; DISULFIDE; ENZYME INHIBITOR; FOSFOMYCIN; GLYCOPEPTIDE; LIPOSIDOMYCIN DERIVATIVE; MERSACIDIN; METICILLIN; MOENOMYCIN A; MONOBACTAM DERIVATIVE; MUREIDOMYCIN A; ORITAVANCIN; OXACILLIN; PENICILLIN G; PEPTIDASE; PURINE DERIVATIVE; PYRAZOLOPYRIMIDINE DERIVATIVE; TEICOPLANIN; TRANSPEPTIDASE INHIBITOR; UNCLASSIFIED DRUG; VANCOMYCIN; PEPTIDOGLYCAN;

EID: 0036480755     PISSN: 14728222     EISSN: None     Source Type: Journal    
DOI: 10.1517/14728222.6.1.1     Document Type: Review
Times cited : (126)

References (152)
  • 1
    • 34249332889 scopus 로고    scopus 로고
    • The complete guide to anti-infectives
    • Richmond, Surrey UK Ed, PJB Publications
    • HALLS G: The complete guide to anti-infectives. In: Scripp Reports. Richmond, Surrey UK (Ed.), PJB Publications (1999).
    • (1999) Scripp Reports
    • HALLS, G.1
  • 2
    • 0024354604 scopus 로고
    • Genetic analysis of temperature-sensitive lethal mutants of Salmonella typhimurium
    • SCHMID MB, KAPUR N, ISAACSON DR, LINDROOS P, SHARPE C: Genetic analysis of temperature-sensitive lethal mutants of Salmonella typhimurium. Genetics (1989) 123:625-633.
    • (1989) Genetics , vol.123 , pp. 625-633
    • SCHMID, M.B.1    KAPUR, N.2    ISAACSON, D.R.3    LINDROOS, P.4    SHARPE, C.5
  • 3
    • 0001025490 scopus 로고    scopus 로고
    • Transposable element tools for microbial genetics
    • Neidhardt FC Ed, ASM Press
    • BERG CM, BERG DA: Transposable element tools for microbial genetics. In: Escherichia coli and Salmonella. Neidhardt FC (Ed.): ASM Press (1996): 588-2612.
    • (1996) Escherichia coli and Salmonella , pp. 588-2612
    • BERG, C.M.1    BERG, D.A.2
  • 4
    • 0035929121 scopus 로고    scopus 로고
    • Identification of critical staphylococcal genes using conditional phenotypes generated by antisense RNA
    • JI Y, ZHANG B, VAN SF et al.: Identification of critical staphylococcal genes using conditional phenotypes generated by antisense RNA. Science (2001) 293:2266-2269.
    • (2001) Science , vol.293 , pp. 2266-2269
    • JI, Y.1    ZHANG, B.2    VAN, S.F.3
  • 5
    • 0034739007 scopus 로고    scopus 로고
    • Complete genome sequence of Pseudomonas aeruginosa PA01, an opportunistic pathogen
    • STOVER CK, PHAM XQ, ERWIN AL et al.: Complete genome sequence of Pseudomonas aeruginosa PA01, an opportunistic pathogen. Nature (2000) 406:959-964.
    • (2000) Nature , vol.406 , pp. 959-964
    • STOVER, C.K.1    PHAM, X.Q.2    ERWIN, A.L.3
  • 6
    • 0035945586 scopus 로고    scopus 로고
    • Genome sequence of enterohaemorrhagic Escherichia coli O157:H7
    • PERNA NT, PLUNKETT G 3RD, BURLAND V et al.: Genome sequence of enterohaemorrhagic Escherichia coli O157:H7. Nature (2001) 409:529-533.
    • (2001) Nature , vol.409 , pp. 529-533
    • PERNA, N.T.1    PLUNKETT 3RD, G.2    BURLAND, V.3
  • 7
    • 0035925904 scopus 로고    scopus 로고
    • Whole genome sequencing of meticillin-resistant Staphylococcus aureus
    • KURODA M, OHTA T, UCHIYAMA I et al.: Whole genome sequencing of meticillin-resistant Staphylococcus aureus. Lancet (2001) 357:1225-1240.
    • (2001) Lancet , vol.357 , pp. 1225-1240
    • KURODA, M.1    OHTA, T.2    UCHIYAMA, I.3
  • 8
    • 0034806849 scopus 로고    scopus 로고
    • Genome of the Bacterium Streptococcus pneumoniae Strain R6
    • HOSKINS J, ALBORN WE JR., ARNOLD J et al.: Genome of the Bacterium Streptococcus pneumoniae Strain R6. J. Bacterial (2001) 183:5709-5717.
    • (2001) J. Bacterial , vol.183 , pp. 5709-5717
    • HOSKINS, J.1    ALBORN, W.J.2    ARNOLD, J.3
  • 9
    • 0033998632 scopus 로고    scopus 로고
    • PAYNE DJ, WALLIS NG, GENTRY DR, ROSENBERG M: The impact of genomics on novel antibacterial targets. Curr. Opin. Drug Discov. (2000) 3:177-190. • Review of antibacterial targets including peptidoglycan biosynthesis enzymes.
    • PAYNE DJ, WALLIS NG, GENTRY DR, ROSENBERG M: The impact of genomics on novel antibacterial targets. Curr. Opin. Drug Discov. (2000) 3:177-190. • Review of antibacterial targets including peptidoglycan biosynthesis enzymes.
  • 10
    • 0034176710 scopus 로고    scopus 로고
    • Using bioinformatics in gene and drug discovery
    • SEARLS D: Using bioinformatics in gene and drug discovery. Drug Discov. Today (2000) 5:135-143.
    • (2000) Drug Discov. Today , vol.5 , pp. 135-143
    • SEARLS, D.1
  • 11
    • 0032979077 scopus 로고    scopus 로고
    • MOIR DT, SHAW KJ, HARE RS, VOVIS GF: Genomics and antimicrobial drug discovery. Antimicrob. Agents Chemother. (1999) 43:439-446. • Review of antibacterial target selection using genomics. Includes internet links.
    • MOIR DT, SHAW KJ, HARE RS, VOVIS GF: Genomics and antimicrobial drug discovery. Antimicrob. Agents Chemother. (1999) 43:439-446. • Review of antibacterial target selection using genomics. Includes internet links.
  • 12
    • 0033668153 scopus 로고    scopus 로고
    • Mining bacterial genomes for antimicrobial targets
    • LOFERER H: Mining bacterial genomes for antimicrobial targets. Mol. Med. Today (2000) 6:470-474.
    • (2000) Mol. Med. Today , vol.6 , pp. 470-474
    • LOFERER, H.1
  • 14
    • 0001011919 scopus 로고    scopus 로고
    • GOODWILL KE, TENNANT MG, STEVENS RC: High throughput x-ray crystallography for structure-based drug design. Drug Discov. Today (2001) 6:S113-S118. • Good summary of automating structural biology for drug discovery.
    • GOODWILL KE, TENNANT MG, STEVENS RC: High throughput x-ray crystallography for structure-based drug design. Drug Discov. Today (2001) 6:S113-S118. • Good summary of automating structural biology for drug discovery.
  • 15
    • 34249317864 scopus 로고    scopus 로고
    • SCHAECHTER M: Biology of infectious agents. In: Mechanisms of Microbial Disease (3rd Edition). SchaechterM, Engleberg NC, Eisenstein BI, Medoff G (Eds.), Lippincott Williams & Wilkins (1989):18-38. •• Good chapter in an excellent textbook covering microbial disease.
    • SCHAECHTER M: Biology of infectious agents. In: Mechanisms of Microbial Disease (3rd Edition). SchaechterM, Engleberg NC, Eisenstein BI, Medoff G (Eds.), Lippincott Williams & Wilkins (1989):18-38. •• Good chapter in an excellent textbook covering microbial disease.
  • 16
    • 0034884365 scopus 로고    scopus 로고
    • Identification of the UDP-MurNAc-pentapeptide:L-alanine ligase for synthesis of branched peptidoglycan precursors in Enterococcus faecalis
    • BOUHSS A, JOSSEAUME N, ALLANIC D et al.: Identification of the UDP-MurNAc-pentapeptide:L-alanine ligase for synthesis of branched peptidoglycan precursors in Enterococcus faecalis. J. Bacteriol. (2001) 183:5122-5127.
    • (2001) J. Bacteriol , vol.183 , pp. 5122-5127
    • BOUHSS, A.1    JOSSEAUME, N.2    ALLANIC, D.3
  • 17
    • 0026049801 scopus 로고
    • Serine beta-lactamases and penicillin-binding proteins
    • GHUYSEN JM: Serine beta-lactamases and penicillin-binding proteins. Ann. Rev. Microbiol. (1991) 45:37-67.
    • (1991) Ann. Rev. Microbiol , vol.45 , pp. 37-67
    • GHUYSEN, J.M.1
  • 18
    • 0031973490 scopus 로고    scopus 로고
    • Kinship and diversification of bacterial penicillin-binding proteins and beta-lactamases
    • MASSOVA I, MOBASHERY S: Kinship and diversification of bacterial penicillin-binding proteins and beta-lactamases. Antimicrob. Agents Chemother. (1998) 42:1-17.
    • (1998) Antimicrob. Agents Chemother , vol.42 , pp. 1-17
    • MASSOVA, I.1    MOBASHERY, S.2
  • 19
    • 0034006505 scopus 로고    scopus 로고
    • Penicillin binding protein 5 affects cell diameter, contour, and morphology of Escherichia coli
    • NELSON DE, YOUNG KD: Penicillin binding protein 5 affects cell diameter, contour, and morphology of Escherichia coli. J. Bacteriol. (2000) 182:1714-1721.
    • (2000) J. Bacteriol , vol.182 , pp. 1714-1721
    • NELSON, D.E.1    YOUNG, K.D.2
  • 20
    • 0032985224 scopus 로고    scopus 로고
    • Escherichia coli mutants lacking all possible combinations of eight penicillin binding proteins: Viability, characteristics, and implications for peptidoglycan synthesis
    • DENOME SA, ELF PK, HENDERSON TA, NELSON DE, YOUNG KD: Escherichia coli mutants lacking all possible combinations of eight penicillin binding proteins: viability, characteristics, and implications for peptidoglycan synthesis. J. Bacteriol. (1999) 181:3981-3993.
    • (1999) J. Bacteriol , vol.181 , pp. 3981-3993
    • DENOME, S.A.1    ELF, P.K.2    HENDERSON, T.A.3    NELSON, D.E.4    YOUNG, K.D.5
  • 21
    • 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
  • 22
    • 0034903171 scopus 로고    scopus 로고
    • Identification and characterization of a monofunctional glycosyltransferase from Staphylococcus aureus
    • WANG QM, PEERY RB, JOHNSON RB, ALBORN WE, YEH W-K, SKATRUD PL: Identification and characterization of a monofunctional glycosyltransferase from Staphylococcus aureus. J. Bacteriol. (2001) 183:4779-4785.
    • (2001) J. Bacteriol , vol.183 , pp. 4779-4785
    • WANG, Q.M.1    PEERY, R.B.2    JOHNSON, R.B.3    ALBORN, W.E.4    YEH, W.-K.5    SKATRUD, P.L.6
  • 23
    • 0031736387 scopus 로고    scopus 로고
    • Multimodular penicillin-binding proteins: An enigmatic family of orthologs and paralogs
    • GOFFIN C, GHUYSEN J-M: Multimodular penicillin-binding proteins: an enigmatic family of orthologs and paralogs. Microbiol. Mol. Biol. Rev. (1998) 62:1079-1093.
    • (1998) Microbiol. Mol. Biol. Rev , vol.62 , pp. 1079-1093
    • GOFFIN, C.1    GHUYSEN, J.-M.2
  • 24
    • 0015462556 scopus 로고
    • Peptidoglycan types of bacterial cell walls and their taxonomic implications
    • SCHLEIFER KH, KANDLER O: Peptidoglycan types of bacterial cell walls and their taxonomic implications. Bacteriol. Rev. (1972) 36:407-477.
    • (1972) Bacteriol. Rev , vol.36 , pp. 407-477
    • SCHLEIFER, K.H.1    KANDLER, O.2
  • 25
    • 0035977042 scopus 로고    scopus 로고
    • DESSEN A, MOUZ N, HOPKINS J, DIDEBERG O: Crystal structure of PBP2x from a highly penicillin-resistant Streptococcus pneumoniae clinical isolate: A mosaic framework containing 83 mutations. J. Biol Chem. (2001) 276:45106-12. • Accepted manuscript providing structural interpretation of penicillin resistance through mutations in PBP2x.
    • DESSEN A, MOUZ N, HOPKINS J, DIDEBERG O: Crystal structure of PBP2x from a highly penicillin-resistant Streptococcus pneumoniae clinical isolate: A mosaic framework containing 83 mutations. J. Biol Chem. (2001) 276:45106-12. • Accepted manuscript providing structural interpretation of penicillin resistance through mutations in PBP2x.
  • 26
    • 0024358135 scopus 로고
    • Horizontal transfer of penicillin-binding protein genes in penicillin-resistant clinical isolates of Streptococcus pneumoniae
    • DOWSON CG, HUTCHISON A, BRANNIGAN JA et al.: Horizontal transfer of penicillin-binding protein genes in penicillin-resistant clinical isolates of Streptococcus pneumoniae. Proc. Natl. Acad Sci. USA (1989) 86:8842-8846.
    • (1989) Proc. Natl. Acad Sci. USA , vol.86 , pp. 8842-8846
    • DOWSON, C.G.1    HUTCHISON, A.2    BRANNIGAN, J.A.3
  • 27
    • 0028420272 scopus 로고
    • Resistance to antibiotics mediated by target alterations
    • SPRATT BG: Resistance to antibiotics mediated by target alterations. Science (1994) 264:388-393.
    • (1994) Science , vol.264 , pp. 388-393
    • SPRATT, B.G.1
  • 28
    • 0029933563 scopus 로고    scopus 로고
    • Separation of abnormal cell wall composition from penicillin resistance through genetic transformation of Streptococcus pneumoniae
    • SEVERIN A, FIGUEIREDO A, TOMASZ A: Separation of abnormal cell wall composition from penicillin resistance through genetic transformation of Streptococcus pneumoniae. J. Bacteriol. (1996) 178:1788-1792.
    • (1996) J. Bacteriol , vol.178 , pp. 1788-1792
    • SEVERIN, A.1    FIGUEIREDO, A.2    TOMASZ, A.3
  • 29
    • 0034623055 scopus 로고    scopus 로고
    • Characterization of the murMN operon involved in the synthesis of branched peptidoglycan peptides in Streptococcus pneumoniae
    • FILIPE SR, PINHO MG, TOMASZ A: Characterization of the murMN operon involved in the synthesis of branched peptidoglycan peptides in Streptococcus pneumoniae. J. Biol. Chem. (2000) 275:27768-27774.
    • (2000) J. Biol. Chem , vol.275 , pp. 27768-27774
    • FILIPE, S.R.1    PINHO, M.G.2    TOMASZ, A.3
  • 30
    • 0034712839 scopus 로고    scopus 로고
    • Inhibition of the expression of penicillin resistance in Streptococcus pneumoniae by inactivation of cell wall muropeptide branching genes
    • FILIPE SR, TOMASZ A: Inhibition of the expression of penicillin resistance in Streptococcus pneumoniae by inactivation of cell wall muropeptide branching genes. Proc. Natl. Acad. Sci. USA (2000) 97:4891-4896.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 4891-4896
    • FILIPE, S.R.1    TOMASZ, A.2
  • 31
    • 0029071785 scopus 로고    scopus 로고
    • BUSH K, JACOBY G, MEDEIROS A: A functional classification scheme for beta-lactamases and its correlation with molecular structure. Antimicrob. Agents Chemother. (1995) 39:1211-1233. •• Good review of β-lactamases.
    • BUSH K, JACOBY G, MEDEIROS A: A functional classification scheme for beta-lactamases and its correlation with molecular structure. Antimicrob. Agents Chemother. (1995) 39:1211-1233. •• Good review of β-lactamases.
  • 32
    • 0035491150 scopus 로고    scopus 로고
    • MILLER LA, RATNAM K, PAYNE DJ: β-lactamase-inhibitor combinations in the 21st century: current agents and new developments. Curr. Opin. Pharmacol. (2001) 1:451-458. •• Good review of a drug combination approach to overcoming β-lactam resistance.
    • MILLER LA, RATNAM K, PAYNE DJ: β-lactamase-inhibitor combinations in the 21st century: current agents and new developments. Curr. Opin. Pharmacol. (2001) 1:451-458. •• Good review of a drug combination approach to overcoming β-lactam resistance.
  • 33
    • 0019278405 scopus 로고
    • A multifaceted approach to the study of the side-chain conformation in beta-lactamase-resistant penicillins
    • BLANPAIN PC, NAGY JB, LAURENT GH, DURANT FV: A multifaceted approach to the study of the side-chain conformation in beta-lactamase-resistant penicillins. J. Med. Chem. (1980) 23:1283-1292.
    • (1980) J. Med. Chem , vol.23 , pp. 1283-1292
    • BLANPAIN, P.C.1    NAGY, J.B.2    LAURENT, G.H.3    DURANT, F.V.4
  • 34
    • 0021931688 scopus 로고
    • Amino acid substitutions that reduce the affinity of penicillin-binding protein 3 of Escherichia coli for cephalexin
    • HEDGE PJ, SPRATT BG: Amino acid substitutions that reduce the affinity of penicillin-binding protein 3 of Escherichia coli for cephalexin. Eur. J. Biochem. (1985) 151:111-121.
    • (1985) Eur. J. Biochem , vol.151 , pp. 111-121
    • HEDGE, P.J.1    SPRATT, B.G.2
  • 35
    • 0035845487 scopus 로고    scopus 로고
    • An acquired and a native penicillin-binding protein cooperate in building the cell wall of drug-resistant Staphylococci
    • PINHO MG, DE LENCASTRE H, TOMASZ A: An acquired and a native penicillin-binding protein cooperate in building the cell wall of drug-resistant Staphylococci. Proc. Natl Acad Sci. USA (2001) 183:6525-31.
    • (2001) Proc. Natl Acad Sci. USA , vol.183 , pp. 6525-6531
    • PINHO, M.G.1    DE LENCASTRE, H.2    TOMASZ, A.3
  • 36
    • 0035295449 scopus 로고    scopus 로고
    • Effect of beta-lactam antibiotics on the in vitro development of resistance in Pseudomonas aeruginosa
    • CARSENTI ETESSE H, CAVALLO JD, ROGER PM: Effect of beta-lactam antibiotics on the in vitro development of resistance in Pseudomonas aeruginosa. Clin. Microbiol Inject. (2001) 7:144-151.
    • (2001) Clin. Microbiol Inject , vol.7 , pp. 144-151
    • CARSENTI, E.H.1    CAVALLO, J.D.2    ROGER, P.M.3
  • 37
    • 0024593426 scopus 로고
    • Oxacillin-hydrolysing beta-lactamases. A comparative analysis at nucleotide and amino acid sequence levels
    • MOSSAKOWSKA D, ALI NA, DALE JW: Oxacillin-hydrolysing beta-lactamases. A comparative analysis at nucleotide and amino acid sequence levels. Eur. J. Biochem. (1989) 180:309-318.
    • (1989) Eur. J. Biochem , vol.180 , pp. 309-318
    • MOSSAKOWSKA, D.1    ALI, N.A.2    DALE, J.W.3
  • 38
    • 0033609444 scopus 로고    scopus 로고
    • X-ray structure of the Asn276Asp variant of the Escherichia coli TEM-1 beta-lactamase: Direct observation of electrostatic modulation in resistance to inactivation by clavulanic acid
    • SWAREN P, GOLEMI D, CABANTOUS S: X-ray structure of the Asn276Asp variant of the Escherichia coli TEM-1 beta-lactamase: direct observation of electrostatic modulation in resistance to inactivation by clavulanic acid. Biochemistry (1999) 38:9570-9576.
    • (1999) Biochemistry , vol.38 , pp. 9570-9576
    • SWAREN, P.1    GOLEMI, D.2    CABANTOUS, S.3
  • 39
    • 0032487847 scopus 로고    scopus 로고
    • Structure-based enhancement of boronic acid-based inhibitors of AmpC beta-lactamase
    • WESTON GS, BLAZQUEZ J, BAQUERO F, SHOICHET BK: Structure-based enhancement of boronic acid-based inhibitors of AmpC beta-lactamase. J. Med. Chem. (1998) 41:4577-4586.
    • (1998) J. Med. Chem , vol.41 , pp. 4577-4586
    • WESTON, G.S.1    BLAZQUEZ, J.2    BAQUERO, F.3    SHOICHET, B.K.4
  • 40
    • 0034327676 scopus 로고    scopus 로고
    • Crystal structures of substrate and inhibitor complexes with ampC β-lactamase: Possible implications for substrate-assisted catalysis
    • PATERA A, BLASZCZAK LC, SHOICHET B: Crystal structures of substrate and inhibitor complexes with ampC β-lactamase: possible implications for substrate-assisted catalysis. J. Am. Chem. Soc. (2000) 122:10504-10512.
    • (2000) J. Am. Chem. Soc , vol.122 , pp. 10504-10512
    • PATERA, A.1    BLASZCZAK, L.C.2    SHOICHET, B.3
  • 41
    • 0034974174 scopus 로고    scopus 로고
    • Structure-based design and in-parallel synthesis of inhibitors of AmpC beta-lactamase
    • TONDI D, POWERS RA, CASELLI E et al.: Structure-based design and in-parallel synthesis of inhibitors of AmpC beta-lactamase. Chem. Biol. (2001) 8:593-611.
    • (2001) Chem. Biol , vol.8 , pp. 593-611
    • TONDI, D.1    POWERS, R.A.2    CASELLI, E.3
  • 42
    • 0034625157 scopus 로고    scopus 로고
    • Structure-based design guides the improved efficacy of deacylation transition state analogue inhibitors of TEM-1 beta-Lactamase
    • NESS S, MARTIN R, KINDLER AM et al.: Structure-based design guides the improved efficacy of deacylation transition state analogue inhibitors of TEM-1 beta-Lactamase. Biochemistry (2000) 39:5312-5321.
    • (2000) Biochemistry , vol.39 , pp. 5312-5321
    • NESS, S.1    MARTIN, R.2    KINDLER, A.M.3
  • 43
    • 0032562183 scopus 로고    scopus 로고
    • Crystal structure of an acylation transition-state analog of the TEM-1 beta-lactamase. Mechanistic implications for class A beta-lactamases
    • MAVEYRAUD L, PRATT RF, SAMAMA JP: Crystal structure of an acylation transition-state analog of the TEM-1 beta-lactamase. Mechanistic implications for class A beta-lactamases. Biochemistry (1998) 37:2622-2628.
    • (1998) Biochemistry , vol.37 , pp. 2622-2628
    • MAVEYRAUD, L.1    PRATT, R.F.2    SAMAMA, J.P.3
  • 44
    • 0034681922 scopus 로고    scopus 로고
    • Crystal structure of the IMP-1 metallo beta-lactamase from Pseudomonas aeruginosa and its complex with a mercaptocarboxylate inhibitor binding determinants of a potent, broad-spectrum inhibitor
    • CONCHA NO, JANSON CA, ROWLING P et al.: Crystal structure of the IMP-1 metallo beta-lactamase from Pseudomonas aeruginosa and its complex with a mercaptocarboxylate inhibitor binding determinants of a potent, broad-spectrum inhibitor. Biochemistry (2000) 39:4288-4298.
    • (2000) Biochemistry , vol.39 , pp. 4288-4298
    • CONCHA, N.O.1    JANSON, C.A.2    ROWLING, P.3
  • 45
    • 0035852621 scopus 로고    scopus 로고
    • LEE W, MCDONOUGH MA, KOTRA L et al.: A 1.2Å snapshot of the final step of bacterial cell wall biosynthesis. Proc. Natl. Acad. Sci. USA (2001) 98:1427-1431. • Structure of a unique cephalosporin bound to a PBP that provides insight into transpeptidation mechanism and transpeptidase/lactamase selectivity.
    • LEE W, MCDONOUGH MA, KOTRA L et al.: A 1.2Å snapshot of the final step of bacterial cell wall biosynthesis. Proc. Natl. Acad. Sci. USA (2001) 98:1427-1431. • Structure of a unique cephalosporin bound to a PBP that provides insight into transpeptidation mechanism and transpeptidase/lactamase selectivity.
  • 46
    • 0028774039 scopus 로고
    • The structure of an asymmetric dimer relevant to the mode of action of the glycopeptide antibiotics
    • GROVES P, SEARLE MS, MACKAY JP, WILLIAMS DH: The structure of an asymmetric dimer relevant to the mode of action of the glycopeptide antibiotics. Structure (1994) 2:747-754.
    • (1994) Structure , vol.2 , pp. 747-754
    • GROVES, P.1    SEARLE, M.S.2    MACKAY, J.P.3    WILLIAMS, D.H.4
  • 47
    • 0026355435 scopus 로고
    • Molecular basis for vancomycin resistance in Enterococcus faecium BM4147: Biosynthesis of a depsipeptide peptidoglycan precursor by vancomycin resistance proteins vanH and vanA
    • BUGG TD, WRIGHT GD, DUTKA-MALEN S et al.: Molecular basis for vancomycin resistance in Enterococcus faecium BM4147: biosynthesis of a depsipeptide peptidoglycan precursor by vancomycin resistance proteins vanH and vanA. Biochemistry (1991) 30:10408-10415.
    • (1991) Biochemistry , vol.30 , pp. 10408-10415
    • BUGG, T.D.1    WRIGHT, G.D.2    DUTKA-MALEN, S.3
  • 48
    • 0027328589 scopus 로고    scopus 로고
    • WALSH CT: Vancomycin resistance: decoding the molecular logic. Science (1993) 261:308-309. • Review of vancomycin mechanism of action and resistance.
    • WALSH CT: Vancomycin resistance: decoding the molecular logic. Science (1993) 261:308-309. • Review of vancomycin mechanism of action and resistance.
  • 49
    • 0033613122 scopus 로고    scopus 로고
    • VanX: A bacterial D-alanyl-D-alanine dipeptidase: resistance, immunity, or survival function?
    • LESSARD IA, WALSH CT: VanX: a bacterial D-alanyl-D-alanine dipeptidase: resistance, immunity, or survival function? Proc. Natl Acad. Sci. USA (1999) 96:11028-11032.
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 11028-11032
    • LESSARD, I.A.1    WALSH, C.T.2
  • 50
    • 0035943435 scopus 로고    scopus 로고
    • CHIOSIS G, BONECA IG: Selective cleavage of D-Ala-D-Lac by small molecules: re-sensitizing resistant bacteria to vancomycin. Science (2001) 293:1484-1487. • Novel approach to overcoming vancomycin resistance.
    • CHIOSIS G, BONECA IG: Selective cleavage of D-Ala-D-Lac by small molecules: re-sensitizing resistant bacteria to vancomycin. Science (2001) 293:1484-1487. • Novel approach to overcoming vancomycin resistance.
  • 51
    • 0033606246 scopus 로고    scopus 로고
    • Combinatorial library approach for the identification of synthetic receptors targeting vancomycin-resistant bacteria
    • XU R, GREIVELDINGER G, MARENUS LE, COOPER A, ELLMAN JA: Combinatorial library approach for the identification of synthetic receptors targeting vancomycin-resistant bacteria. J. Am. Chem. Soc. (1999) 121:4898-4899.
    • (1999) J. Am. Chem. Soc , vol.121 , pp. 4898-4899
    • XU, R.1    GREIVELDINGER, G.2    MARENUS, L.E.3    COOPER, A.4    ELLMAN, J.A.5
  • 52
    • 0029802138 scopus 로고    scopus 로고
    • Antimicrobial-drug resistance
    • GOLD HS, MOELLERING RC: Antimicrobial-drug resistance. N. Engl J. Med. (1996) 335:1445-1453.
    • (1996) N. Engl J. Med , vol.335 , pp. 1445-1453
    • GOLD, H.S.1    MOELLERING, R.C.2
  • 53
  • 54
    • 0028855994 scopus 로고
    • Two conformers of the glycopcptide antibiotic teicoplanin with distinct ligand binding sites
    • WESTWELL MS, GERHARD U, WILLIAMS DH: Two conformers of the glycopcptide antibiotic teicoplanin with distinct ligand binding sites. J. Antibiot. (Tokyo) (1995) 48:1292-1298.
    • (1995) J. Antibiot. (Tokyo) , vol.48 , pp. 1292-1298
    • WESTWELL, M.S.1    GERHARD, U.2    WILLIAMS, D.H.3
  • 55
    • 0029820318 scopus 로고    scopus 로고
    • SCHWALBERS, MCINTOSH AC, QAIYUMI S et al.: In vitro activity of LY333328, an investigational glycopeptide antibiotic, against enterococci and staphylococci. Antimicrob. Agents Chemother. (1996) 40:2416-2419.
    • SCHWALBERS, MCINTOSH AC, QAIYUMI S et al.: In vitro activity of LY333328, an investigational glycopeptide antibiotic, against enterococci and staphylococci. Antimicrob. Agents Chemother. (1996) 40:2416-2419.
  • 56
    • 0031051359 scopus 로고    scopus 로고
    • In vitro activity and spectrum of LY333328, a novel glycopeptide derivative
    • JONES RN, BARRETT MS, ERWIN ME: In vitro activity and spectrum of LY333328, a novel glycopeptide derivative. Antimicrob. Agents Chemother. (1997) 41:488-493.
    • (1997) Antimicrob. Agents Chemother , vol.41 , pp. 488-493
    • JONES, R.N.1    BARRETT, M.S.2    ERWIN, M.E.3
  • 57
    • 0030479181 scopus 로고    scopus 로고
    • Novel vancomycin dimers with activity against vancomycin-resistant enterococci
    • SUNDRAM UM, GRIFFIN JH, NICAS TI: Novel vancomycin dimers with activity against vancomycin-resistant enterococci. J. Am. Chem. Soc. (1996) 118:13107-13108.
    • (1996) J. Am. Chem. Soc , vol.118 , pp. 13107-13108
    • SUNDRAM, U.M.1    GRIFFIN, J.H.2    NICAS, T.I.3
  • 58
    • 0030920563 scopus 로고    scopus 로고
    • Time-kill curves for a semisynthetic glycopeptide, LY333328, against vancomycin- susceptible and vancomycin-resistant Enterococcus faecium strains
    • ZELENITSKY SA, KARLOWSKY JA, ZHANEL GG, HOBAN DJ, NICAS T: Time-kill curves for a semisynthetic glycopeptide, LY333328, against vancomycin- susceptible and vancomycin-resistant Enterococcus faecium strains. Antimicrob. Agents Chemother. (1997) 41:1407-1408.
    • (1997) Antimicrob. Agents Chemother , vol.41 , pp. 1407-1408
    • ZELENITSKY, S.A.1    KARLOWSKY, J.A.2    ZHANEL, G.G.3    HOBAN, D.J.4    NICAS, T.5
  • 59
    • 0031662779 scopus 로고    scopus 로고
    • Comparison of inhibitory and bactericidal activities and postantibiotic effects of LY333328 and ampicillin used singly and in combination against vancomycin-resistant Enterococcus faecium
    • BALTCH AL, SMITH RP, RITZ WJ, BOPP LH: Comparison of inhibitory and bactericidal activities and postantibiotic effects of LY333328 and ampicillin used singly and in combination against vancomycin-resistant Enterococcus faecium. Antimicrob. Agents Chemother. (1998) 42:2564-2568.
    • (1998) Antimicrob. Agents Chemother , vol.42 , pp. 2564-2568
    • BALTCH, A.L.1    SMITH, R.P.2    RITZ, W.J.3    BOPP, L.H.4
  • 60
    • 0034694714 scopus 로고    scopus 로고
    • The role of hydrocarbon substituents in the biological activity of glycopeptide antibiotics
    • KERNS R, DONG SD, FUKUZAWA S et al.: The role of hydrocarbon substituents in the biological activity of glycopeptide antibiotics. J. Am. Chem. Soc. (2000) 122:12608-12609.
    • (2000) J. Am. Chem. Soc , vol.122 , pp. 12608-12609
    • KERNS, R.1    DONG, S.D.2    FUKUZAWA, S.3
  • 61
    • 0033574743 scopus 로고    scopus 로고
    • GE M, CHEN Z, ONISHI HR et al.: Vancomycin derivatives that inhibit peptidoglycan biosynthesis without binding D-Ala-D-Ala. Science (1999) 284:507-511. •• Excellent description of developing glycopeptides from vancomycin that inhibit transglycosylation rather than transpeptidation.
    • GE M, CHEN Z, ONISHI HR et al.: Vancomycin derivatives that inhibit peptidoglycan biosynthesis without binding D-Ala-D-Ala. Science (1999) 284:507-511. •• Excellent description of developing glycopeptides from vancomycin that inhibit transglycosylation rather than transpeptidation.
  • 62
    • 0035850868 scopus 로고    scopus 로고
    • Genetic basis for activity differences between vancomycin and glycolipid derivatives of vancomycin
    • EGGERT US, RUIZ N, FALCONE BV et al.: Genetic basis for activity differences between vancomycin and glycolipid derivatives of vancomycin. Science (2001):294:361-4.
    • (2001) Science , vol.294 , pp. 361-364
    • EGGERT, U.S.1    RUIZ, N.2    FALCONE, B.V.3
  • 63
    • 0035910508 scopus 로고    scopus 로고
    • Specific binding of nisin to the peptidoglycan precursor lipid II combines pore formation and inhibition of cell wall biosynthesis for potent antibiotic activity
    • WIEDEMANN I, BREUKINK E, VAN KRAAIJ C et al.: Specific binding of nisin to the peptidoglycan precursor lipid II combines pore formation and inhibition of cell wall biosynthesis for potent antibiotic activity. J. Biol. Chem. (2001) 276:1772-1779.
    • (2001) J. Biol. Chem , vol.276 , pp. 1772-1779
    • WIEDEMANN, I.1    BREUKINK, E.2    VAN KRAAIJ, C.3
  • 65
    • 13044269653 scopus 로고    scopus 로고
    • Discovery of novel disaccharide antibacterial agents using a combinatorial library approach
    • SOFIA MJ, ALLANSON N, HATZENBUHLER NT et al.: Discovery of novel disaccharide antibacterial agents using a combinatorial library approach. J. Med. Chem. (1999) 42:3193-3198.
    • (1999) J. Med. Chem , vol.42 , pp. 3193-3198
    • SOFIA, M.J.1    ALLANSON, N.2    HATZENBUHLER, N.T.3
  • 66
    • 0034529940 scopus 로고    scopus 로고
    • Antibacterial activity of synthetic analogues based on the disaccharide structure of moenomycin, an inhibitor of bacterial transglycosylase
    • BAIZMAN ER, BRANSTROM AA, LONGLEY CB et al.: Antibacterial activity of synthetic analogues based on the disaccharide structure of moenomycin, an inhibitor of bacterial transglycosylase. Microbiology (2000) 146:3129-3140.
    • (2000) Microbiology , vol.146 , pp. 3129-3140
    • BAIZMAN, E.R.1    BRANSTROM, A.A.2    LONGLEY, C.B.3
  • 68
    • 0034090551 scopus 로고    scopus 로고
    • A simple screen for murein transglycosylase inhibitors
    • VOLLMER W, HOLTJE J-V: A simple screen for murein transglycosylase inhibitors. Antimicrob. Agents Chemother. (2000) 44:1181-1185.
    • (2000) Antimicrob. Agents Chemother , vol.44 , pp. 1181-1185
    • VOLLMER, W.1    HOLTJE, J.-V.2
  • 69
    • 0035933529 scopus 로고    scopus 로고
    • A protein antibiotic in the phage Qbeta virion: Diversity in lysis targets
    • BERNHARDT TG, WANG IN, STRUCK DK, YOUNG R: A protein antibiotic in the phage Qbeta virion: diversity in lysis targets. Science (2001) 292:2326-2329.
    • (2001) Science , vol.292 , pp. 2326-2329
    • BERNHARDT, T.G.1    WANG, I.N.2    STRUCK, D.K.3    YOUNG, R.4
  • 70
    • 0027130834 scopus 로고
    • Evidence that the reaction of the UDP-N-acetylglucoamine 1-carboxyvinyltransferase proceeds through the O-phosphothioketal of pyruvic acid bound to Cys115 of the enzyme
    • WANKE C, AMRHEIN N: Evidence that the reaction of the UDP-N-acetylglucoamine 1-carboxyvinyltransferase proceeds through the O-phosphothioketal of pyruvic acid bound to Cys115 of the enzyme. Eur. J. Biochem. (1993) 218:861-870.
    • (1993) Eur. J. Biochem , vol.218 , pp. 861-870
    • WANKE, C.1    AMRHEIN, N.2
  • 71
    • 0028070055 scopus 로고
    • Kinetics, stoichiometry, and identification of the reactive thiolate in the inactivation of UDP-GlcNAc enolpyruvoyl transferase by the antibiotic fosfomycin
    • MARQUARDT JL, BROWN ED, LANE WS et al.: Kinetics, stoichiometry, and identification of the reactive thiolate in the inactivation of UDP-GlcNAc enolpyruvoyl transferase by the antibiotic fosfomycin. Biochemistry (1994) 33:10646-10651.
    • (1994) Biochemistry , vol.33 , pp. 10646-10651
    • MARQUARDT, J.L.1    BROWN, E.D.2    LANE, W.S.3
  • 73
    • 0027233035 scopus 로고
    • Selective inhibition of the bacterial translocase reaction in peptidoglycan synthesis by mureidomycins
    • INUKAI M, ISONO F, TAKATSUKI A: Selective inhibition of the bacterial translocase reaction in peptidoglycan synthesis by mureidomycins. Antimicrob. Agents Chemother. (1993) 37:980-983.
    • (1993) Antimicrob. Agents Chemother , vol.37 , pp. 980-983
    • INUKAI, M.1    ISONO, F.2    TAKATSUKI, A.3
  • 74
    • 0026081814 scopus 로고
    • Mureidomycin A, a new inhibitor of bacterial peptidoglycan synthesis
    • ISONO F, INUKAI M: Mureidomycin A, a new inhibitor of bacterial peptidoglycan synthesis. Antimicrob. Agents Chemother. (1991) 35:234-236.
    • (1991) Antimicrob. Agents Chemother , vol.35 , pp. 234-236
    • ISONO, F.1    INUKAI, M.2
  • 75
    • 0032428375 scopus 로고    scopus 로고
    • Selective inhibition of the bacterial peptidoglycan biosynthesis by the new types of liposidomycins
    • KIMURA K, IKEDA Y, KAGAMIS et al.: Selective inhibition of the bacterial peptidoglycan biosynthesis by the new types of liposidomycins. J. Antibiot. (Tokyo) (1998) 51:1099-1104.
    • (1998) J. Antibiot. (Tokyo) , vol.51 , pp. 1099-1104
    • KIMURA, K.1    IKEDA, Y.2    KAGAMIS3
  • 76
    • 0029902635 scopus 로고    scopus 로고
    • Modes of action of tunicamycin, liposidomycin B, and mureidomycin A: Inhibition of phospho-N-acetylmuramyl-pentapeptide translocase from Escherichia coli
    • BRANDISH PE, KIMURA KI, INUKAI M, SOUTHGATE R, LONSDALE JT, BUGG TD: Modes of action of tunicamycin, liposidomycin B, and mureidomycin A: inhibition of phospho-N-acetylmuramyl-pentapeptide translocase from Escherichia coli. Antimicrob. Agents Chemother. (1996) 40:1640-1644.
    • (1996) Antimicrob. Agents Chemother , vol.40 , pp. 1640-1644
    • BRANDISH, P.E.1    KIMURA, K.I.2    INUKAI, M.3    SOUTHGATE, R.4    LONSDALE, J.T.5    BUGG, T.D.6
  • 77
    • 0031725647 scopus 로고    scopus 로고
    • BOYLE DS, DONACHIE WD: mraY is an essential gene for cell growth in Escherichia coli. J. Bacteriol. (1998) 180:6429-6432.
    • BOYLE DS, DONACHIE WD: mraY is an essential gene for cell growth in Escherichia coli. J. Bacteriol. (1998) 180:6429-6432.
  • 78
    • 0028279550 scopus 로고
    • Sequence divergence of the murB and rrfB genes from Escherichia coli and Salmonella typhimurium
    • DOMBROSKY PM, SCHMID MB, YOUNG KD: Sequence divergence of the murB and rrfB genes from Escherichia coli and Salmonella typhimurium. Arch. Microbiol. (1994) 161:501-507.
    • (1994) Arch. Microbiol , vol.161 , pp. 501-507
    • DOMBROSKY, P.M.1    SCHMID, M.B.2    YOUNG, K.D.3
  • 79
    • 0033927088 scopus 로고    scopus 로고
    • A method for demonstrating gene essentiality in Staphylococcus aureus
    • JANA M, LUONG TT, KOMATSUZAWA H, SHIGETA M, LEE CY: A method for demonstrating gene essentiality in Staphylococcus aureus. Plasmid (2000) 44:100-104.
    • (2000) Plasmid , vol.44 , pp. 100-104
    • JANA, M.1    LUONG, T.T.2    KOMATSUZAWA, H.3    SHIGETA, M.4    LEE, C.Y.5
  • 80
    • 0027434077 scopus 로고
    • Identification of the glmU gene encoding N-acetylglucosamine-1-phosphate uridyltransferase in Escherichia coli
    • MENGIN-LECREULX D, VAN HEIJENOORT J: Identification of the glmU gene encoding N-acetylglucosamine-1-phosphate uridyltransferase in Escherichia coli. J. Bacteriol. (1993) 175:6150-6157.
    • (1993) J. Bacteriol , vol.175 , pp. 6150-6157
    • MENGIN-LECREULX, D.1    VAN HEIJENOORT, J.2
  • 81
    • 0032995017 scopus 로고    scopus 로고
    • Cloning and sequencing of Staphylococcus aureus murC, a gene essential for cell wall biosynthesis
    • LOWE AM, DERESIEWICZ RL: Cloning and sequencing of Staphylococcus aureus murC, a gene essential for cell wall biosynthesis. DNA Sea. (1999) 10:19-23.
    • (1999) DNA Sea , vol.10 , pp. 19-23
    • LOWE, A.M.1    DERESIEWICZ, R.L.2
  • 82
    • 0032850461 scopus 로고    scopus 로고
    • Comparison of the D-glutamate-adding enzymes from selected gram-positive and gram-negative bacteria
    • WALSH AW, FALK PJ, THANASSI J, DISCOTTO L, PUCCI MJ, HO HT: Comparison of the D-glutamate-adding enzymes from selected gram-positive and gram-negative bacteria. J. Bacteriol. (1999) 181:5395-5401.
    • (1999) J. Bacteriol , vol.181 , pp. 5395-5401
    • WALSH, A.W.1    FALK, P.J.2    THANASSI, J.3    DISCOTTO, L.4    PUCCI, M.J.5    HO, H.T.6
  • 83
    • 0029064598 scopus 로고
    • MurA (MurZ), the enzyme that catalyzes the first committed step in peptidoglycan biosynthesis, is essential in Escherichia coli
    • BROWN E, VIVAS E, WALSH C, KOLTER R: MurA (MurZ), the enzyme that catalyzes the first committed step in peptidoglycan biosynthesis, is essential in Escherichia coli. J. Bacteriol. (1995) 177:4194-4627.
    • (1995) J. Bacteriol , vol.177 , pp. 4194-4627
    • BROWN, E.1    VIVAS, E.2    WALSH, C.3    KOLTER, R.4
  • 84
    • 0033981615 scopus 로고    scopus 로고
    • Cloning, over-expression and purification of Pseudomonas aeruginosa murC encoding uridine diphosphate N-acetylmuramate: L-alanine ligase
    • EL ZOEIBY A, SANSCHAGRIN F, LAMOUREUX J, DARVEAU A, LEVESQUE RC: Cloning, over-expression and purification of Pseudomonas aeruginosa murC encoding uridine diphosphate N-acetylmuramate: L-alanine ligase. FEMS Microbiol. Lett. (2000) 183:281-288.
    • (2000) FEMS Microbiol. Lett , vol.183 , pp. 281-288
    • EL ZOEIBY, A.1    SANSCHAGRIN, F.2    LAMOUREUX, J.3    DARVEAU, A.4    LEVESQUE, R.C.5
  • 85
    • 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
  • 86
    • 0027938707 scopus 로고
    • Copurification of glucosamine-1-phosphate acetyltransferase and N-acetylglucosamine-1-phosphate uridyltransferase activities of Escherichia coli: Characterization of the glmU gene product as a bifunctional enzyme catalyzing two subsequent steps in the pathway for UDP-N-acetylglucosamine synthesis
    • MENGIN-LECREULX D, VAN HEIJENOORT J: Copurification of glucosamine-1-phosphate acetyltransferase and N-acetylglucosamine-1-phosphate uridyltransferase activities of Escherichia coli: characterization of the glmU gene product as a bifunctional enzyme catalyzing two subsequent steps in the pathway for UDP-N-acetylglucosamine synthesis. J. Bacteriol. (1994) 176:5788-5795.
    • (1994) J. Bacteriol , vol.176 , pp. 5788-5795
    • MENGIN-LECREULX, D.1    VAN HEIJENOORT, J.2
  • 87
    • 0030051742 scopus 로고    scopus 로고
    • Acetyltransfer precedes uridylyltransfer in the formation of UDP-N-acetylglucosamine in separable active sites of the bifunctional GlmU protein of Escherichia coli
    • GEHRING AM, LEES WJ, MINDIOLA DJ, WALSH CT, BROWN ED: Acetyltransfer precedes uridylyltransfer in the formation of UDP-N-acetylglucosamine in separable active sites of the bifunctional GlmU protein of Escherichia coli. Biochemistry (1996) 35:579-585.
    • (1996) Biochemistry , vol.35 , pp. 579-585
    • GEHRING, A.M.1    LEES, W.J.2    MINDIOLA, D.J.3    WALSH, C.T.4    BROWN, E.D.5
  • 88
    • 0035830887 scopus 로고    scopus 로고
    • Dissection of the bifunctional Escherichia coli N-acetylglucosamine-1- phosphate uridyltransferase enzyme into autonomously functional domains and evidence that trimerization is absolutely required for glucosamine-1-phosphate acetyltransferase activity and cell growth
    • POMPEO F, BOURNE Y, VAN HEIJENOORT J, FASSY F, MENGIN-LECREULX D: Dissection of the bifunctional Escherichia coli N-acetylglucosamine-1- phosphate uridyltransferase enzyme into autonomously functional domains and evidence that trimerization is absolutely required for glucosamine-1-phosphate acetyltransferase activity and cell growth. J. Biol Chem. (2001) 276:3833-3839.
    • (2001) J. Biol Chem , vol.276 , pp. 3833-3839
    • POMPEO, F.1    BOURNE, Y.2    VAN HEIJENOORT, J.3    FASSY, F.4    MENGIN-LECREULX, D.5
  • 89
    • 0035916240 scopus 로고    scopus 로고
    • Structure of the Escherichia coli GlmU pyrophosphorylase and acetyltransferase active sites
    • OLSEN LR, RODERICK SL: Structure of the Escherichia coli GlmU pyrophosphorylase and acetyltransferase active sites. Biochemistry (2001) 40:1913-1921.
    • (2001) Biochemistry , vol.40 , pp. 1913-1921
    • OLSEN, L.R.1    RODERICK, S.L.2
  • 90
    • 0035853790 scopus 로고    scopus 로고
    • Crystal structure of Streptococcus pneumoniae N-acetylgl ucosamine-1-phosphate uridyltransferase bound to acetyl-coenzyme A reveals a novel active site architecture
    • SULZENBACHER G, GAL L, PENEFF C, FASSY F, BOURNE Y: Crystal structure of Streptococcus pneumoniae N-acetylgl ucosamine-1-phosphate uridyltransferase bound to acetyl-coenzyme A reveals a novel active site architecture. J. Biol Chem. (2001) 276:11844-11851.
    • (2001) J. Biol Chem , vol.276 , pp. 11844-11851
    • SULZENBACHER, G.1    GAL, L.2    PENEFF, C.3    FASSY, F.4    BOURNE, Y.5
  • 91
    • 0030073022 scopus 로고    scopus 로고
    • WALSH CT, BENSON TE, KIM DH, LEES WJ: The versatility of phosphoenolpyruvate and its vinyl ether products in biosynthesis. Chem. Biol. (1996) 3:83-91. •• Great review of the enzyme mechanisms using phosphoenolpyruvate in biosynthesis.
    • WALSH CT, BENSON TE, KIM DH, LEES WJ: The versatility of phosphoenolpyruvate and its vinyl ether products in biosynthesis. Chem. Biol. (1996) 3:83-91. •• Great review of the enzyme mechanisms using phosphoenolpyruvate in biosynthesis.
  • 92
    • 0033939999 scopus 로고    scopus 로고
    • Two active forms of UDP-N-acetylglucosamine enolpyruvyl transferase in Gram-positive bacteria
    • DU W, BROWN JR, SYLVESTER DR et al.: Two active forms of UDP-N-acetylglucosamine enolpyruvyl transferase in Gram-positive bacteria. J. Bacteriol (2000) 182:4146-4627.
    • (2000) J. Bacteriol , vol.182 , pp. 4146-4627
    • DU, W.1    BROWN, J.R.2    SYLVESTER, D.R.3
  • 93
    • 0029967416 scopus 로고    scopus 로고
    • 115 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 (1996) 35:4923-4928. • Good example of how structure-function studies can be used to explain mechanisms of resistance at a molecular level.
    • 115 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 (1996) 35:4923-4928. • Good example of how structure-function studies can be used to explain mechanisms of resistance at a molecular level.
  • 94
    • 0032891974 scopus 로고    scopus 로고
    • Emergence of fosfomycin-resistant isolates of Shiga-like toxin-producing Escherichia coli O26
    • HORII T, KIMURA T, SATO K, SHIBAYAMA K, OHTA M: Emergence of fosfomycin-resistant isolates of Shiga-like toxin-producing Escherichia coli O26. Antimicrob. Agents Chemother. (1999) 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
  • 95
    • 0030854329 scopus 로고    scopus 로고
    • Plasmid-encoded fosfomycin resistance in bacteria isolated from the urinary tract in a multicentre survey
    • ARCA P, REGUERA G, HARDISSON C: Plasmid-encoded fosfomycin resistance in bacteria isolated from the urinary tract in a multicentre survey. J. Antimicrob. Chemother. (1997) 40:393-399.
    • (1997) J. Antimicrob. Chemother , vol.40 , pp. 393-399
    • ARCA, P.1    REGUERA, G.2    HARDISSON, C.3
  • 96
    • 0032741590 scopus 로고    scopus 로고
    • Alteration of a single amino acid residue reverses fosfomycin resistance of recombinant MurA from Mycobacterium tuberculosis
    • DE SMET KA, KEMPSELL KE, GALLAGHER A, DUNCAN K, YOUNG DB: Alteration of a single amino acid residue reverses fosfomycin resistance of recombinant MurA from Mycobacterium tuberculosis. Microbiology (1999) 145:3177- 3184.
    • (1999) Microbiology , vol.145 , pp. 3177-3184
    • DE SMET, K.A.1    KEMPSELL, K.E.2    GALLAGHER, A.3    DUNCAN, K.4    YOUNG, D.B.5
  • 97
    • 0020636139 scopus 로고
    • Fosfomycin inactivates its target enzyme in Escherichia coli cells carrying a fosfomycin resistance plasmid
    • LEON J, GARCIA-LOBO JM, ORTIZ JM: Fosfomycin inactivates its target enzyme in Escherichia coli cells carrying a fosfomycin resistance plasmid. Antimicrob. Agents Chemother. (1983) 24:276-278.
    • (1983) Antimicrob. Agents Chemother , vol.24 , pp. 276-278
    • LEON, J.1    GARCIA-LOBO, J.M.2    ORTIZ, J.M.3
  • 98
    • 0034770091 scopus 로고    scopus 로고
    • Identification and Characterization of New Inhibitors of the Escherichia coli MurA Enzyme
    • BAUM EZ, MONTENEGRO DA, LICATA L et al.: Identification and Characterization of New Inhibitors of the Escherichia coli MurA Enzyme. Antimicrob. Agents Chemother. (2001) 45:3182-3188.
    • (2001) Antimicrob. Agents Chemother , vol.45 , pp. 3182-3188
    • BAUM, E.Z.1    MONTENEGRO, D.A.2    LICATA, L.3
  • 99
    • 0035852821 scopus 로고    scopus 로고
    • Asparagine 23 and aspartate 305 are essential residues in the active site of UDP-N-acetylglucosamine enolpyruvyl transferase from Enterobacter cloacae
    • SAMLAND AK, ETEZADY-ESFARJANI T, AMRHEIN N, MACHEROUX P: Asparagine 23 and aspartate 305 are essential residues in the active site of UDP-N-acetylglucosamine enolpyruvyl transferase from Enterobacter cloacae. Biochemistry (2001) 40:1550-1559.
    • (2001) Biochemistry , vol.40 , pp. 1550-1559
    • SAMLAND, A.K.1    ETEZADY-ESFARJANI, T.2    AMRHEIN, N.3    MACHEROUX, P.4
  • 100
    • 0030587522 scopus 로고    scopus 로고
    • Crystal structure of UDP-N-acetylglucosamine enolpyruvyltransferase, the target of the antibiotic fosfomycin
    • SCHONBRUNN E, SACK S, ESCHENBURG S et al.: Crystal structure of UDP-N-acetylglucosamine enolpyruvyltransferase, the target of the antibiotic fosfomycin. Structure (1996) 4:1065-1075.
    • (1996) Structure , vol.4 , pp. 1065-1075
    • SCHONBRUNN, E.1    SACK, S.2    ESCHENBURG, S.3
  • 101
    • 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, ESCHENBURG S, LUGER K, KABSCH W, AMRHEIN N: Structural basis for the interaction of the fluorescence probe 8-anilino-1-naphthalene sulfonate (ANS) with the antibiotic target MurA. Proc. Natl. Acad. Sci. USA (2000) 97:6345-6349.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 6345-6349
    • SCHONBRUNN, E.1    ESCHENBURG, S.2    LUGER, K.3    KABSCH, W.4    AMRHEIN, N.5
  • 102
    • 0032562223 scopus 로고    scopus 로고
    • Stereochemical course of enzymatic enolpyruvyl transfer and catalytic conformation of the active site revealed by the crystal structure of the fluorinated analogue of the reaction tetrahedral intermediate bound to the active site of the C115A mutant of MurA
    • SKARZYNSKI T, KIM DH, LEES WJ, WALSH CT, DUNCAN K: Stereochemical course of enzymatic enolpyruvyl transfer and catalytic conformation of the active site revealed by the crystal structure of the fluorinated analogue of the reaction tetrahedral intermediate bound to the active site of the C115A mutant of MurA. Biochemistry (1998) 37:2572-2577.
    • (1998) Biochemistry , vol.37 , pp. 2572-2577
    • SKARZYNSKI, T.1    KIM, D.H.2    LEES, W.J.3    WALSH, C.T.4    DUNCAN, K.5
  • 103
    • 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, MISTRY A, WONACOTT A, HUTCHINSON SE, KELLY VA, DUNCAN K: 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 (1996) 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
  • 104
    • 0035852821 scopus 로고    scopus 로고
    • Asparagine 23 and aspartate 305 are essential residues in the active site of UDP-N- acetylglucosamine enolpyruvyl transferase from Enterobacter cloacae
    • SAMLAND AK, ETEZADY ESFARJANIT, AMRHEIN N, MACHEROUX P: Asparagine 23 and aspartate 305 are essential residues in the active site of UDP-N- acetylglucosamine enolpyruvyl transferase from Enterobacter cloacae. Biochemistry (2001) 40:1550-1559.
    • (2001) Biochemistry , vol.40 , pp. 1550-1559
    • SAMLAND, A.K.1    ETEZADY-ESFARJANI, T.2    AMRHEIN, N.3    MACHEROUX, P.4
  • 105
    • 0027512265 scopus 로고
    • Overexpression, purification, and mechanistic study of UDP-N- acetylenolpyruvylglucosamine reductase
    • BENSON TE, MARQUARDT JL, MARQUARDT AC, ETZKORN FA, WALSH CT: Overexpression, purification, and mechanistic study of UDP-N- acetylenolpyruvylglucosamine reductase. Biochemistry (1993) 32:2024-2030.
    • (1993) Biochemistry , vol.32 , pp. 2024-2030
    • BENSON, T.E.1    MARQUARDT, J.L.2    MARQUARDT, A.C.3    ETZKORN, F.A.4    WALSH, C.T.5
  • 107
    • 0029056202 scopus 로고
    • An enzyme-substrate complex involved in bacterial cell wall biosynthesis
    • BENSON TE, FILMAN DJ, WALSH CT, HOGLE JM: An enzyme-substrate complex involved in bacterial cell wall biosynthesis. Nat. Struct. Biol. (1995) 2:644-653.
    • (1995) Nat. Struct. Biol , vol.2 , pp. 644-653
    • BENSON, T.E.1    FILMAN, D.J.2    WALSH, C.T.3    HOGLE, J.M.4
  • 108
    • 0031054015 scopus 로고    scopus 로고
    • X-ray crystal structures of the S229A mutant and wild type MurB in the presence of the substrate enolpyruvyl-UDP-N- acetylglucosamine at 1.8-Å resolution
    • BENSON TE, WALSH CT, HOGLE JM: X-ray crystal structures of the S229A mutant and wild type MurB in the presence of the substrate enolpyruvyl-UDP-N- acetylglucosamine at 1.8-Å resolution. Biochemistry (1997) 36:806-811.
    • (1997) Biochemistry , vol.36 , pp. 806-811
    • BENSON, T.E.1    WALSH, C.T.2    HOGLE, J.M.3
  • 109
    • 0030801002 scopus 로고    scopus 로고
    • Gapped BLAST and PSI-BLAST: A new generation of protein database search programs
    • ALTSCHUL SF, MADDEN TL, SCHAFFER AA et al.: Gapped BLAST and PSI-BLAST: a new generation of protein database search programs. Nucleic Acids Res. (1997) 25:3389-3402.
    • (1997) Nucleic Acids Res , vol.25 , pp. 3389-3402
    • ALTSCHUL, S.F.1    MADDEN, T.L.2    SCHAFFER, A.A.3
  • 110
    • 0035957048 scopus 로고    scopus 로고
    • BENSON TE, HARRIS MS, CHOI GH et al.: A structural variation for MurB: x-ray crystal structure of Staphylococcus aureus UDP-N-acetylenolpyruvylglucosamine reductase (MurB). Biochemistry (2001) 40:2340-2350. • Good example of how protein structure can be used to identify differences among target enzymes in developing antibacterial agents with broad spectrum.
    • BENSON TE, HARRIS MS, CHOI GH et al.: A structural variation for MurB: x-ray crystal structure of Staphylococcus aureus UDP-N-acetylenolpyruvylglucosamine reductase (MurB). Biochemistry (2001) 40:2340-2350. • Good example of how protein structure can be used to identify differences among target enzymes in developing antibacterial agents with broad spectrum.
  • 111
    • 0034678644 scopus 로고    scopus 로고
    • 4-Thiazolidinones: Novel inhibitors of the bacterial enzyme MurB
    • ANDRES CJ, BRONSON JJ, D'ANDREA SV et al.: 4-Thiazolidinones: novel inhibitors of the bacterial enzyme MurB. Bioorg. Med. Chem. Lett. (2000) 10:715-717.
    • (2000) Bioorg. Med. Chem. Lett , vol.10 , pp. 715-717
    • ANDRES, C.J.1    BRONSON, J.J.2    D'ANDREA, S.V.3
  • 112
    • 0034283162 scopus 로고    scopus 로고
    • Open' structures of MurD: Domain movements and structural similarities with folylpolyglutamate synthetase
    • BERTRAND JA, FANCHON E, MARTIN L et al.: 'Open' structures of MurD: domain movements and structural similarities with folylpolyglutamate synthetase. J. Mol. Biol. (2000) 301:1257-1266.
    • (2000) J. Mol. Biol , vol.301 , pp. 1257-1266
    • BERTRAND, J.A.1    FANCHON, E.2    MARTIN, L.3
  • 113
    • 0030927105 scopus 로고    scopus 로고
    • Crystal structure of UDP-N-acetylmuramoyl-L-alanine:D-glutamate ligase from Escherichia coli
    • BERTRAND JA, AUGER G, FANCHON E et al.: Crystal structure of UDP-N-acetylmuramoyl-L-alanine:D-glutamate ligase from Escherichia coli. EMBO J. (1997) 16:3416-3425.
    • (1997) EMBO J , vol.16 , pp. 3416-3425
    • BERTRAND, J.A.1    AUGER, G.2    FANCHON, E.3
  • 114
    • 0033546272 scopus 로고    scopus 로고
    • Determination of the MurD mechanism through crystallographic analysis of enzyme complexes
    • BERTRAND JA, AUGER G, MARTIN L et al.: Determination of the MurD mechanism through crystallographic analysis of enzyme complexes. J. Mol. Biol. (1999) 289:579-590.
    • (1999) J. Mol. Biol , vol.289 , pp. 579-590
    • BERTRAND, J.A.1    AUGER, G.2    MARTIN, L.3
  • 115
    • 0035815667 scopus 로고    scopus 로고
    • Crystal structure of UDP-N-acetylmuramoyl-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-acetylmuramoyl-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
  • 116
    • 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
  • 117
    • 0033592452 scopus 로고    scopus 로고
    • Role of the ortholog and paralog amino acid invariants in the active site of the UDP-MurNAc-L-alanine:D- glutamate ligase (MurD)
    • BOUHSS A, DEMENTIN S, PARQUET C et al.: Role of the ortholog and paralog amino acid invariants in the active site of the UDP-MurNAc-L-alanine:D- glutamate ligase (MurD). Biochemistry (1999) 38:12240-12247.
    • (1999) Biochemistry , vol.38 , pp. 12240-12247
    • BOUHSS, A.1    DEMENTIN, S.2    PARQUET, C.3
  • 118
    • 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
  • 119
    • 0030471790 scopus 로고    scopus 로고
    • Kinetic mechanism of the Escherichia coli UDP-MurNAc-tripeptide D-alanyl-D-alanine-adding enzyme: Use of a glutathione S-transferase fusion
    • ANDERSON MS, EVELAND SS, ONISHI HR, POMPLIANO DL: Kinetic mechanism of the Escherichia coli UDP-MurNAc-tripeptide D-alanyl-D-alanine-adding enzyme: use of a glutathione S-transferase fusion. Biochemistry 1996, 35:16264-16269.
    • (1996) Biochemistry , vol.35 , pp. 16264-16269
    • ANDERSON, M.S.1    EVELAND, S.S.2    ONISHI, H.R.3    POMPLIANO, D.L.4
  • 120
    • 0025210655 scopus 로고
    • Purification and characterization of the D-alanyl-D-alanine-adding enzyme from Escherichia coli
    • DUNCAN K, VAN HEIJENOORT J, WALSH CT: Purification and characterization of the D-alanyl-D-alanine-adding enzyme from Escherichia coli. Biochemistry (1990) 29:2379-2386.
    • (1990) Biochemistry , vol.29 , pp. 2379-2386
    • DUNCAN, K.1    VAN HEIJENOORT, J.2    WALSH, C.T.3
  • 121
    • 0030474933 scopus 로고    scopus 로고
    • Kinetic and crystallographic studies of Escherichia coli UDP-N-acetylmuramate:L-alanine ligase
    • EMANUELE JJ JR., JIN H, JACOBSON BL, CHANG CY, EINSPAHR HM, VILLAFRANCA JJ: Kinetic and crystallographic studies of Escherichia coli UDP-N-acetylmuramate:L-alanine ligase. Prot. Sci. (1996) 5:2566-2574.
    • (1996) Prot. Sci , vol.5 , pp. 2566-2574
    • EMANUELE JJ JR, J.H.1    JACOBSON, B.L.2    CHANG, C.Y.3    EINSPAHR, H.M.4    VILLAFRANCA, J.J.5
  • 122
    • 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 HT: 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
  • 123
    • 0029760460 scopus 로고    scopus 로고
    • Study of the overproduced uridine-diphosphate-N-acetylmuramate:L-alanine ligase from Escherichia coli
    • LIGER D, MASSON A, BLANOT D, VAN HEIJENOORT J, PARQUET C: Study of the overproduced uridine-diphosphate-N-acetylmuramate:L-alanine ligase from Escherichia coli. Microb. Drug. Resist. (1996) 2:25-27.
    • (1996) Microb. Drug. Resist , vol.2 , pp. 25-27
    • LIGER, D.1    MASSON, A.2    BLANOT, D.3    VAN HEIJENOORT, J.4    PARQUET, C.5
  • 124
    • 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
  • 126
    • 0035044363 scopus 로고    scopus 로고
    • Synthesis and biochemical evaluation of some novel N-acyl phosphono- and phosphinoalanine derivatives as potential inhibitors of the D-glutamic acid-adding enzyme
    • GOBEC S, URLEB U, AUGER G, BLANOT D: Synthesis and biochemical evaluation of some novel N-acyl phosphono- and phosphinoalanine derivatives as potential inhibitors of the D-glutamic acid-adding enzyme. Pharmazie (2001) 56:295-297.
    • (2001) Pharmazie , vol.56 , pp. 295-297
    • GOBEC, S.1    URLEB, U.2    AUGER, G.3    BLANOT, D.4
  • 127
    • 0032567399 scopus 로고    scopus 로고
    • A phosphinate inhibitor of the mesodiaminopimelic acid-adding enzyme (MurE) of peptidoglycan biosynthesis
    • ZENG B, WONG KK, POMPLIANO DL, REDDY S, TANNER ME: A phosphinate inhibitor of the mesodiaminopimelic acid-adding enzyme (MurE) of peptidoglycan biosynthesis. J. Org. Chem. (1998) 63:10081-10086.
    • (1998) J. Org. Chem , vol.63 , pp. 10081-10086
    • ZENG, B.1    WONG, K.K.2    POMPLIANO, D.L.3    REDDY, S.4    TANNER, M.E.5
  • 128
    • 0032583606 scopus 로고    scopus 로고
    • Engineering a cell-free murein biosynthetic pathway: Combinatorial enzymology in drug discovery
    • WONG KK, KUO DW, CHABIN RM et al.: Engineering a cell-free murein biosynthetic pathway: combinatorial enzymology in drug discovery. J. Am. Chem. Soc. (1998) 120:13527-13528.
    • (1998) J. Am. Chem. Soc , vol.120 , pp. 13527-13528
    • WONG, K.K.1    KUO, D.W.2    CHABIN, R.M.3
  • 129
    • 0028361885 scopus 로고
    • Replacement of diaminopimelic acid by cystathionine or lanthionine in the peptidoglycan of Escherichia coli
    • MENGIN-LECREULX D, BLANOT D, VAN HEIJENOORT J: Replacement of diaminopimelic acid by cystathionine or lanthionine in the peptidoglycan of Escherichia coli. J. Bacteriol. (1994) 176:4321-4327.
    • (1994) J. Bacteriol , vol.176 , pp. 4321-4327
    • MENGIN-LECREULX, D.1    BLANOT, D.2    VAN HEIJENOORT, J.3
  • 130
    • 0032823023 scopus 로고    scopus 로고
    • Expression of the Staphylococcus aureus UDP-N-acetylmuramoyl- L-alanyl-D-glutamate:L-lysine ligase in Escherichia coli and effects on peptidoglycan biosynthesis and cell growth
    • MENGIN-LECREULX D, FALLA T, BLANOT D, VAN HEIJENOORT J, ADAMS DJ, CHOPRA I: Expression of the Staphylococcus aureus UDP-N-acetylmuramoyl- L-alanyl-D-glutamate:L-lysine ligase in Escherichia coli and effects on peptidoglycan biosynthesis and cell growth. J. Bacteriol. (1999) 181:5909-5914.
    • (1999) J. Bacteriol , vol.181 , pp. 5909-5914
    • MENGIN-LECREULX, D.1    FALLA, T.2    BLANOT, D.3    VAN HEIJENOORT, J.4    ADAMS, D.J.5    CHOPRA, I.6
  • 131
    • 0034698781 scopus 로고    scopus 로고
    • Synthesis of the nucleoside moiety of liposidomycins: Elucidation of the pharmacophore of this family of MraY inhibitors
    • DINI C, COLLETTE P, DROCHON N et al.: Synthesis of the nucleoside moiety of liposidomycins: elucidation of the pharmacophore of this family of MraY inhibitors. Bioorg. Med. Chem. Lett. (2000) 10:1839-1843.
    • (2000) Bioorg. Med. Chem. Lett , vol.10 , pp. 1839-1843
    • DINI, C.1    COLLETTE, P.2    DROCHON, N.3
  • 132
    • 0035952253 scopus 로고    scopus 로고
    • Synthesis of analogues of the O-beta-D-ribofuranosyl nucleoside moiety of liposidomycins. Part 1: Contribution of the amino group and the uracil moiety upon the inhibition of MraY
    • DINI C, DROCHON N, FETEANU S, GUILLOT JC, PEKOTO C, ASZODI J: Synthesis of analogues of the O-beta-D-ribofuranosyl nucleoside moiety of liposidomycins. Part 1: contribution of the amino group and the uracil moiety upon the inhibition of MraY. Bioorg. Med. Chem. Lett. (2001) 11:529-531.
    • (2001) Bioorg. Med. Chem. Lett , vol.11 , pp. 529-531
    • DINI, C.1    DROCHON, N.2    FETEANU, S.3    GUILLOT, J.C.4    PEKOTO, C.5    ASZODI, J.6
  • 133
    • 0035952292 scopus 로고    scopus 로고
    • Synthesis of analogues of the O-beta-D-ribofuranosyl nucleoside moiety of liposidomycins. Part 2: Role of the hydroxyl groups upon the inhibition of MraY
    • DINI C, DROCHON N, GUILLOT JC, MAUVAIS P, WALTER P, ASZODI J: Synthesis of analogues of the O-beta-D-ribofuranosyl nucleoside moiety of liposidomycins. Part 2: role of the hydroxyl groups upon the inhibition of MraY. Bioorg. Med. Chem. Lett. (2001) 11:533-536.
    • (2001) Bioorg. Med. Chem. Lett , vol.11 , pp. 533-536
    • DINI, C.1    DROCHON, N.2    GUILLOT, J.C.3    MAUVAIS, P.4    WALTER, P.5    ASZODI, J.6
  • 134
    • 0032746748 scopus 로고    scopus 로고
    • Topological analysis of the MraY protein catalysing the first membrane step of peptidoglycan synthesis
    • BOUHSS A, MENGIN-LECREULX D, LE BELLER D, VAN HEIJENOORT J: Topological analysis of the MraY protein catalysing the first membrane step of peptidoglycan synthesis. Mol. Microbiol. (1999) 34:576-585.
    • (1999) Mol. Microbiol , vol.34 , pp. 576-585
    • BOUHSS, A.1    MENGIN-LECREULX, D.2    LE BELLER, D.3    VAN HEIJENOORT, J.4
  • 135
  • 136
    • 0035115653 scopus 로고    scopus 로고
    • CHANDRAKALAB, ELIAS BC, MEHRA U et al.: Novel scintillation proximity assay for measuring membrane-associated steps of peptidoglycan biosynthesis in Escherichia coli. Antimicrob. Agents Chemother. (2001) 45:768-775.
    • CHANDRAKALAB, ELIAS BC, MEHRA U et al.: Novel scintillation proximity assay for measuring membrane-associated steps of peptidoglycan biosynthesis in Escherichia coli. Antimicrob. Agents Chemother. (2001) 45:768-775.
  • 137
    • 0014198674 scopus 로고
    • STROMINGERJL: Biosythesis of the peptidoglycan of bacterial cell walls. II. Phospholipid carriers in the reaction sequence
    • ANDERSON JS, MATSUHASHI M, HASKIN MA, STROMINGERJL: Biosythesis of the peptidoglycan of bacterial cell walls. II. Phospholipid carriers in the reaction sequence. J. Biol. Chem. (1967) 242:3180-3190.
    • (1967) J. Biol. Chem , vol.242 , pp. 3180-3190
    • ANDERSON, J.S.1    MATSUHASHI, M.2    HASKIN, M.A.3
  • 138
    • 0034640026 scopus 로고    scopus 로고
    • A new mechanism of action proposed for ramoplanin
    • LO M-C, MEN H, BRANSTROM A, et al.: A new mechanism of action proposed for ramoplanin. J. Am. Chem. Soc. (2000) 122:3540-3541.
    • (2000) J. Am. Chem. Soc , vol.122 , pp. 3540-3541
    • LO M-C, M.H.1    BRANSTROM, A.2
  • 139
    • 0033595530 scopus 로고    scopus 로고
    • HA S, CHANG E, LO M-C et al.: The kinetic characterization of Escherichia coli MurG using synthetic substrate analogues. J. Am. Chem. Soc. (1999) 122:8415-8426. •• Good description of using innovative approaches to overcome technical obstacles associated with working with enzymes in peptidoglycan biosynthesis.
    • HA S, CHANG E, LO M-C et al.: The kinetic characterization of Escherichia coli MurG using synthetic substrate analogues. J. Am. Chem. Soc. (1999) 122:8415-8426. •• Good description of using innovative approaches to overcome technical obstacles associated with working with enzymes in peptidoglycan biosynthesis.
  • 140
    • 0032542717 scopus 로고    scopus 로고
    • Substrate synthesis and activity assay for MurG
    • MEN H, PARK P, GE M, WALKER S: Substrate synthesis and activity assay for MurG. J. Am. Chem. Soc. (1998) 120:2484-2485.
    • (1998) J. Am. Chem. Soc , vol.120 , pp. 2484-2485
    • MEN, H.1    PARK, P.2    GE, M.3    WALKER, S.4
  • 141
    • 0033623762 scopus 로고    scopus 로고
    • The 1.9 Å crystal structure of Escherichia coli MurG, a membrane-associated glycosyltransferase involved in peptidoglycan biosynthesis
    • HA S, WALKER D, SHI Y, WALKER S: The 1.9 Å crystal structure of Escherichia coli MurG, a membrane-associated glycosyltransferase involved in peptidoglycan biosynthesis. Protein Sci. (2000) 9:1045-1052.
    • (2000) Protein Sci , vol.9 , pp. 1045-1052
    • HA, S.1    WALKER, D.2    SHI, Y.3    WALKER, S.4
  • 142
    • 0034076849 scopus 로고    scopus 로고
    • Bacterial diaminopimelate metabolism as a target for antibiotic design
    • COX RJ, SUTHERLAND A, VEDERAS JC: Bacterial diaminopimelate metabolism as a target for antibiotic design. Bioorg. Med. Chem. Lett. (2000) 8:843-871.
    • (2000) Bioorg. Med. Chem. Lett , vol.8 , pp. 843-871
    • COX, R.J.1    SUTHERLAND, A.2    VEDERAS, J.C.3
  • 143
    • 0035831448 scopus 로고    scopus 로고
    • FemABX family members are novel nonribosomal peptidyltransferases and important pathogen-specific drug targets
    • HEGDE SS, SHRADER TE: FemABX family members are novel nonribosomal peptidyltransferases and important pathogen-specific drug targets. J. Biol. Chem. (2001) 276:6998-7003.
    • (2001) J. Biol. Chem , vol.276 , pp. 6998-7003
    • HEGDE, S.S.1    SHRADER, T.E.2
  • 144
    • 0029678335 scopus 로고    scopus 로고
    • Synthesis and evaluation of inhibitors of bacterial D-alanine:D-alanine ligases
    • ELLSWORTH BA, TOM NJ, BARTLETT PA: Synthesis and evaluation of inhibitors of bacterial D-alanine:D-alanine ligases. Chem Biol (1996) 3:37-44.
    • (1996) Chem Biol , vol.3 , pp. 37-44
    • ELLSWORTH, B.A.1    TOM, N.J.2    BARTLETT, P.A.3
  • 145
    • 0023689077 scopus 로고
    • Phosphinic acid inhibitors of D-alanyl-D-alanine ligase
    • PARSONS WH, PATCHETT AA, BULL HG et al.: Phosphinic acid inhibitors of D-alanyl-D-alanine ligase. J. Med Chem. (1988) 31:1772-1778.
    • (1988) J. Med Chem , vol.31 , pp. 1772-1778
    • PARSONS, W.H.1    PATCHETT, A.A.2    BULL, H.G.3
  • 146
    • 0345313624 scopus 로고    scopus 로고
    • Use of genomics to identify bacterial undecaprenyl pyrophosphate synthetase: Cloning, expression, and characterization of the essential uppS gene
    • APFEL CM, TAKACS B, FOUNTOULAKIS M, STIEGER M, KECK W: Use of genomics to identify bacterial undecaprenyl pyrophosphate synthetase: cloning, expression, and characterization of the essential uppS gene. J. Bacteriol. (1999) 181:483-492.
    • (1999) J. Bacteriol , vol.181 , pp. 483-492
    • APFEL, C.M.1    TAKACS, B.2    FOUNTOULAKIS, M.3    STIEGER, M.4    KECK, W.5
  • 147
    • 0032935778 scopus 로고    scopus 로고
    • The Escherichia coli homologue of yeast RER2, a key enzyme of dolichol synthesis, is essential for carrier lipid formation in bacterial cell wall synthesis
    • KATO J, FUJISAKI S, NAKAJIMA K, NISHIMURA Y, SATO M, NAKANO A: The Escherichia coli homologue of yeast RER2, a key enzyme of dolichol synthesis, is essential for carrier lipid formation in bacterial cell wall synthesis. J. Bacteriol. (1999) 181:2733-2738.
    • (1999) J. Bacteriol , vol.181 , pp. 2733-2738
    • KATO, J.1    FUJISAKI, S.2    NAKAJIMA, K.3    NISHIMURA, Y.4    SATO, M.5    NAKANO, A.6
  • 149
    • 12944335304 scopus 로고    scopus 로고
    • Drug target validation: Lethal infection blocked by inducible peptide
    • TAO J, WENDLER P, CONNELLY G et al.: Drug target validation: Lethal infection blocked by inducible peptide. PNAS (2000) 97:783-786.
    • (2000) PNAS , vol.97 , pp. 783-786
    • TAO, J.1    WENDLER, P.2    CONNELLY, G.3
  • 151
    • 34249338717 scopus 로고    scopus 로고
    • base
    • http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=Protein Entrez protein data base.
    • Entrez protein data
  • 152
    • 3042800461 scopus 로고    scopus 로고
    • base
    • http://www.rcsb.org/pdb/index.html Protein data base.
    • Protein data


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.