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Volumn 50, Issue 46, 2011, Pages 10091-10101

Substrate specificity of low-molecular mass bacterial dd -peptidases

Author keywords

[No Author keywords available]

Indexed keywords

ACTINOMADURA R39 DD-PEPTIDASE; ACTIVE SITE STRUCTURE; BACILLUS SUBTILIS; BORONATE; CELL WALL BIOSYNTHESIS; GONORRHOEAE; IN-VITRO; IN-VIVO; MEMBRANE-BOUND; NEISSERIA GONORRHOEAE; PENICILLIN-BINDING PROTEINS; PEPTIDE FRAGMENTS; PEPTIDE STRUCTURES; PEPTIDE SUBSTRATES; PEPTIDOGLYCANS; SITE-SPECIFIC; STEADY-STATE KINETICS; STREPTOCOCCUS PNEUMONIAE; SUBSTRATE SPECIFICITY; TRANSITION-STATE ANALOGUES; WATER-SOLUBLE ENZYMES;

EID: 81255129591     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi201326a     Document Type: Article
Times cited : (19)

References (75)
  • 1
    • 0037858060 scopus 로고    scopus 로고
    • Growth of the stress-bearing and shape-maintaining murein sacculus of Escherichia coli
    • Höltje, J.-V. (1998) Growth of the stress-bearing and shape-maintaining murein sacculus of Escherichia coli Microbiol. Mol. Biol. Rev. 62, 181-203 (Pubitemid 28130800)
    • (1998) Microbiology and Molecular Biology Reviews , vol.62 , Issue.1 , pp. 181-203
    • Holtje, J.-V.1
  • 2
    • 50049104157 scopus 로고    scopus 로고
    • Murein (peptidoglycan) structure, architecture and biosynthesis in Escherichia coli
    • Vollmer, W. and Bertsche, U. (2007) Murein (peptidoglycan) structure, architecture and biosynthesis in Escherichia coli Biochim. Biophys. Acta 1788, 1714-1733
    • (2007) Biochim. Biophys. Acta , vol.1788 , pp. 1714-1733
    • Vollmer, W.1    Bertsche, U.2
  • 3
    • 0021943163 scopus 로고
    • Penicillin-sensitive enzymes in peptidoglycan biosynthesis
    • Joris, B. and Frère, J.-M. (1988) Penicillin-sensitive enzymes in peptidoglycan biosynthesis CRC Crit. Rev. Microbiol. 11, 299-396
    • (1988) CRC Crit. Rev. Microbiol. , vol.11 , pp. 299-396
    • Joris, B.1    Frère, J.-M.2
  • 4
    • 0031945139 scopus 로고    scopus 로고
    • Resistant penicillin-binding proteins
    • DOI 10.1007/s000180050160
    • Hackenbeck, R. and Coyette, J. (1998) Resistant penicillin-binding proteins Cell. Mol. Life Sci. 54, 332-340 (Pubitemid 28192739)
    • (1998) Cellular and Molecular Life Sciences , vol.54 , Issue.4 , pp. 332-340
    • Hakenbeck, R.1    Coyette, J.2
  • 5
    • 65549165914 scopus 로고    scopus 로고
    • What antimicrobial resistance has taught us about horizontal gene transfer
    • Barlow, M. (2009) What antimicrobial resistance has taught us about horizontal gene transfer Methods Mol. Biol. 532, 397-411
    • (2009) Methods Mol. Biol. , vol.532 , pp. 397-411
    • Barlow, M.1
  • 7
    • 0028420272 scopus 로고
    • Resistance to antibiotics mediated by target alterations
    • Spratt, B. G. (1994) Resistance to antibiotics mediated by target alterations Science 264, 388-393 (Pubitemid 24986723)
    • (1994) Science , vol.264 , Issue.5157 , pp. 388-393
    • Spratt, B.G.1
  • 8
    • 65449169610 scopus 로고    scopus 로고
    • The antibiotic resistance profile of Streptococcus pneumoniae
    • Reinert, R. R. (2009) The antibiotic resistance profile of Streptococcus pneumoniae Clin. Microbiol. Infect. 15 (Suppl. 3) 7-11
    • (2009) Clin. Microbiol. Infect. , vol.15 , Issue.SUPPL. 3 , pp. 7-11
    • Reinert, R.R.1
  • 9
    • 0028041404 scopus 로고
    • Overproduction of a low-affinity penicillin-binding protein and high- level ampicillin resistance in Enterococcus faecium
    • Fontana, R., Aldegheri, M., Ligozzi, M., Lopez, H., Sucari, R., and Satta, G. (1994) Overproduction of a low-affinity penicillin-binding protein and high-level ampicillin resistance in Enterococcus faecium Antimicrob. Agents Chemother. 38, 1980-1983 (Pubitemid 24278788)
    • (1994) Antimicrobial Agents and Chemotherapy , vol.38 , Issue.9 , pp. 1980-1983
    • Fontana, R.1    Aldegheri, M.2    Ligozzi, M.3    Lopez, H.4    Sucari, A.5    Satta, G.6
  • 10
    • 34250186426 scopus 로고    scopus 로고
    • Neisseria gonorrhoeae isolates with reduced susceptibility to cefixime and ceftriaxone: Association with genetic polymorphisms in penA, mtrR, porB1b, and ponA
    • DOI 10.1128/AAC.01604-06
    • Lindberg, R., Fredlund, H., Nicholas, R., and Unemo, M. (2007) Neisseria gonorrhoeae isolates with reduced susceptibility to cefixime and ceftriaxone: Association with genetic polymorphisms in penA, mtrR, porB1b, and ponA Antimicrob. Agents Chemother. 51, 2117-2122 (Pubitemid 46903103)
    • (2007) Antimicrobial Agents and Chemotherapy , vol.51 , Issue.6 , pp. 2117-2122
    • Lindberg, R.1    Fredlund, H.2    Nicholas, R.3    Unemo, M.4
  • 12
    • 67651180741 scopus 로고    scopus 로고
    • β-Lactams and β-lactamase inhibitors in current or potential clinical practice: A comprehensive update
    • Shahid, M., Sobia, F., Singh, A., Malik, A., Khan, H. M., Jonas, D., and Hawkey, P. M. (2009) β-Lactams and β-lactamase inhibitors in current or potential clinical practice: A comprehensive update Crit. Rev. Microbiol. 35, 81-108
    • (2009) Crit. Rev. Microbiol. , vol.35 , pp. 81-108
    • Shahid, M.1    Sobia, F.2    Singh, A.3    Malik, A.4    Khan, H.M.5    Jonas, D.6    Hawkey, P.M.7
  • 13
    • 0026049801 scopus 로고
    • Serine β-lactamases and penicillin-binding proteins
    • Ghuysen, J.-M. (1991) Serine β-lactamases and penicillin-binding proteins Annu. Rev. Microbiol. 45, 37-67
    • (1991) Annu. Rev. Microbiol. , vol.45 , pp. 37-67
    • Ghuysen, J.-M.1
  • 14
    • 0347364718 scopus 로고    scopus 로고
    • Role of penicillin-binding proteins in bacterial cell morphogenesis
    • DOI 10.1016/j.mib.2003.10.002
    • Popham, D. L. and Young, K. D. (2003) Role of penicillin-binding proteins in bacterial cell morphogenesis Curr. Opin. Microbiol. 6, 594-599 (Pubitemid 38020056)
    • (2003) Current Opinion in Microbiology , vol.6 , Issue.6 , pp. 594-599
    • Popham, D.L.1    Young, K.D.2
  • 15
    • 46249130782 scopus 로고    scopus 로고
    • Physiological functions of d -alanine carboxypeptidases in Escherichia coli
    • Ghosh, A. S., Chowdhury, C., and Nelson, D. E. (2008) Physiological functions of d -alanine carboxypeptidases in Escherichia coli Trends Microbiol. 16, 309-317
    • (2008) Trends Microbiol. , vol.16 , pp. 309-317
    • Ghosh, A.S.1    Chowdhury, C.2    Nelson, D.E.3
  • 17
    • 0024996497 scopus 로고
    • Chromogenic depsipeptide substrates for β-lactamases and penicillin-sensitive DD-peptidases
    • Adam, M., Damblon, C., Plaitin, B., Christiaens, L., and Frère, J.-M. (1990) Chromogenic depsipeptide substrates for β-lactamases and penicillin-sensitive dd -peptidases Biochem. J. 270, 525-529 (Pubitemid 20273499)
    • (1990) Biochemical Journal , vol.270 , Issue.2 , pp. 525-529
    • Adam, M.1    Damblon, C.2    Plaitin, B.3    Christiaens, L.4    Frere, J.-M.5
  • 18
    • 0034633999 scopus 로고    scopus 로고
    • Dipeptide binding to the extended active site of the Streptomyces R61 d -alanyl- d -alanine peptidase: The path to a specific substrate
    • Anderson, J. W. and Pratt, R. F. (2000) Dipeptide binding to the extended active site of the Streptomyces R61 d -alanyl- d -alanine peptidase: The path to a specific substrate Biochemistry 39, 12200-12209
    • (2000) Biochemistry , vol.39 , pp. 12200-12209
    • Anderson, J.W.1    Pratt, R.F.2
  • 19
    • 0036965578 scopus 로고    scopus 로고
    • Structures of two kinetic intermediates reveal species specificity of penicillin-binding proteins
    • DOI 10.1016/S0022-2836(02)00742-8
    • McDonough, M. A., Anderson, J. W., Silvaggi, N. R., Pratt, R. F., and Kelly, J. A. (2002) Structures of two kinetic intermediates reveal species specificity of penicillin-binding proteins J. Mol. Biol. 322, 111-122 (Pubitemid 36132673)
    • (2002) Journal of Molecular Biology , vol.322 , Issue.1 , pp. 111-122
    • McDonough, M.A.1    Anderson, J.W.2    Silvaggi, N.R.3    Pratt, R.F.4    Knox, J.R.5    Kelly, J.A.6
  • 20
    • 23044433657 scopus 로고    scopus 로고
    • Transpeptidation reactions of a specific substrate catalyzed by the Streptomyces R61 DD-peptidase: The structural basis of acyl acceptor specificity
    • DOI 10.1021/bi0505417
    • Kumar, I. and Pratt, R. F. (2005) Transpeptidation reactions of a specific substrate catalyzed by the Streptomyces R61 dd -peptidase: The structural basis of acyl acceptor specificity Biochemistry 44, 9961-9970 (Pubitemid 41076792)
    • (2005) Biochemistry , vol.44 , Issue.30 , pp. 9961-9970
    • Kumar, I.1    Pratt, R.F.2
  • 21
    • 23044488660 scopus 로고    scopus 로고
    • Transpeptidation reactions of a specific substrate catalyzed by the Streptomyces R61 DD-peptidase: Characterization of a chromogenic substrate and acyl acceptor design
    • DOI 10.1021/bi050542z
    • Kumar, I. and Pratt, R. F. (2005) Transpeptidation reactions of a specific substrate catalyzed by the Streptomyces R61 dd -peptidase: Characterization of a chromogenic substrate and acyl acceptor design Biochemistry 44, 9971-9979 (Pubitemid 41076793)
    • (2005) Biochemistry , vol.44 , Issue.30 , pp. 9971-9979
    • Kumar, I.1    Pratt, R.F.2
  • 22
    • 27644543207 scopus 로고    scopus 로고
    • Specificity and reversibility of the transpeptidation reaction catalyzed by the Streptomyces R61 D-Ala-D-Ala peptidase
    • DOI 10.1110/ps.051641005
    • Rhazi, N., Delmarcelle, M., Sauvage, E., Jacquemotte, F., Devriendt, K., Tallon, V., Ghosez, L., and Frère, J.-M. (2005) Specificity and reversibility of the transpeptidation reaction catalyzed by the Streptomyces R61 d -Ala- d -Ala peptidase Protein Sci. 14, 2922-2928 (Pubitemid 41577274)
    • (2005) Protein Science , vol.14 , Issue.11 , pp. 2922-2928
    • Rhazi, N.1    Delmarcelle, M.2    Sauvage, E.3    Jacquemotte, F.4    Devriendt, K.5    Tallon, V.6    Ghosez, L.7    Frere, J.-M.8
  • 24
    • 0015937184 scopus 로고
    • Structure of the wall peptidoglycan of Streptomyces R39 and the specificity profile of its exocellular dd -carboxypeptidase-transpeptidase for peptide acceptors
    • Ghuysen, J.-M., Leyh-Bouille, M., Campbell, J. N., Moreno, R., Frère, J.-M., Duez, C., Nieto, M., and Perkins, H. R. (1973) Structure of the wall peptidoglycan of Streptomyces R39 and the specificity profile of its exocellular dd -carboxypeptidase-transpeptidase for peptide acceptors Biochemistry 12, 1243-1251
    • (1973) Biochemistry , vol.12 , pp. 1243-1251
    • Ghuysen, J.-M.1    Leyh-Bouille, M.2    Campbell, J.N.3    Moreno, R.4    Frère, J.-M.5    Duez, C.6    Nieto, M.7    Perkins, H.R.8
  • 25
    • 0016166233 scopus 로고
    • Effects of donor and acceptor peptides on concomitant hydrolysis and transfer reactions catalyzed by the exocellular dd -carboxypeptidase- transpeptidase from Streptomyces R39
    • Ghuysen, J.-M., Reynolds, P. E., Perkins, H. R., Frère, J.-M., and Moreno, R. (1974) Effects of donor and acceptor peptides on concomitant hydrolysis and transfer reactions catalyzed by the exocellular dd -carboxypeptidase-transpeptidase from Streptomyces R39 Biochemistry 13, 2539-2547
    • (1974) Biochemistry , vol.13 , pp. 2539-2547
    • Ghuysen, J.-M.1    Reynolds, P.E.2    Perkins, H.R.3    Frère, J.-M.4    Moreno, R.5
  • 26
    • 78751556860 scopus 로고    scopus 로고
    • Kinetics of reactions of the Actinomadura R39 dd -peptidase with specific substrates
    • Adediran, S. A., Kumar, I., Nagarajan, R., Sauvage, E., and Pratt, R. F. (2011) Kinetics of reactions of the Actinomadura R39 dd -peptidase with specific substrates Biochemistry 50, 376-387
    • (2011) Biochemistry , vol.50 , pp. 376-387
    • Adediran, S.A.1    Kumar, I.2    Nagarajan, R.3    Sauvage, E.4    Pratt, R.F.5
  • 27
    • 77955041712 scopus 로고    scopus 로고
    • Crystal structure of a complex between the Actinomadura R39 dd -peptidase and a peptidoglycan-mimetic boronate inhibitor: Interpretation of a transition state analogue in terms of catalytic mechanism
    • Dzhekieva, L., Rocaboy, M., Kerff, F., Charlier, P., Sauvage, E., and Pratt, R. F. (2010) Crystal structure of a complex between the Actinomadura R39 dd -peptidase and a peptidoglycan-mimetic boronate inhibitor: Interpretation of a transition state analogue in terms of catalytic mechanism Biochemistry 49, 6411-6419
    • (2010) Biochemistry , vol.49 , pp. 6411-6419
    • Dzhekieva, L.1    Rocaboy, M.2    Kerff, F.3    Charlier, P.4    Sauvage, E.5    Pratt, R.F.6
  • 28
    • 24744431864 scopus 로고    scopus 로고
    • Crystal structure of the Actinomadura R39 DD-peptidase reveals new domains in penicillin-binding proteins
    • DOI 10.1074/jbc.M503271200
    • Sauvage, E., Herman, R., Petrella, S., Duez, C., Bouillenne, F., Frère, J.-M., and Charlier, P. (2005) Crystal structure of the Actinomadura R39 dd -peptidase reveals new domains in penicillin binding proteins J. Biol. Chem. 280, 31249-31256 (Pubitemid 41291862)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.35 , pp. 31249-31256
    • Sauvage, E.1    Herman, R.2    Petrella, S.3    Duez, C.4    Bouillenne, F.5    Frere, J.-M.6    Charlier, P.7
  • 29
    • 0347362788 scopus 로고    scopus 로고
    • Crystal structures of wild-type penicillin-binding protein 5 from Escherichia coli
    • Nicholas, R. A., Krings, S., Tomberg, J., Nichola, G., and Davies, C. (2003) Crystal structures of wild-type penicillin-binding protein 5 from Escherichia coli J. Biol. Chem. 278, 52826-52833
    • (2003) J. Biol. Chem. , vol.278 , pp. 52826-52833
    • Nicholas, R.A.1    Krings, S.2    Tomberg, J.3    Nichola, G.4    Davies, C.5
  • 30
    • 0346850578 scopus 로고    scopus 로고
    • Neisseria gonorrhoeae Penicillin-Binding Protein 3 Exhibits Exceptionally High Carboxypeptidase and β-Lactam Binding Activities
    • DOI 10.1021/bi0350607
    • Stevanova, M. E., Tomberg, J., Olesky, M., Höltje, J.-V., Gutheil, W. G., and Nicholas, R. A. (2003) Neisseria gonorrhoeae penicillin-binding protein 3 exhibits exceptionally high carboxypeptidase and β-lactam binding activities Biochemistry 42, 14614-14625 (Pubitemid 37532008)
    • (2003) Biochemistry , vol.42 , Issue.49 , pp. 14614-14625
    • Stefanova, M.E.1    Tomberg, J.2    Olesky, M.3    Holtje, J.-V.4    Gutheil, W.G.5    Nicholas, R.A.6
  • 31
    • 1642580521 scopus 로고    scopus 로고
    • Overexpression and enzymatic characterization of Neisseria gonorrhoeae penicillin-binding protein
    • DOI 10.1046/j.1432-1033.2003.03886.x
    • Stefanova, M. E., Tomberg, J., Davies, C., Nicholas, R. A., and Gutheil, W. G. (2004) Overexpression and enzymatic characterization of Neisseria gonorrhoeae penicillin-binding protein 4 Eur. J. Biochem. 271, 23-32 (Pubitemid 38122162)
    • (2004) European Journal of Biochemistry , vol.271 , Issue.1 , pp. 23-32
    • Stefanova, M.E.1    Tomberg, J.2    Davies, C.3    Nicholas, R.A.4    Gutheil, W.G.5
  • 32
    • 0035110736 scopus 로고    scopus 로고
    • Purification and characterization of PBP4a, a new low-molecular-weight penicillin-binding protein from Bacillus subtilis
    • DOI 10.1128/JB.183.5.1595-1599.2001
    • Duez, C., Van Hove, M., Gallet, X., Bouillene, F., Docquier, J.-D., Brous, A., and Frère, J.-M. (2001) Purification and characterization of PBP4a, a new low molecular-weight penicillin-binding protein from Bacillus subtilis J. Bacteriol. 183, 1595-1599 (Pubitemid 32172302)
    • (2001) Journal of Bacteriology , vol.183 , Issue.5 , pp. 1595-1599
    • Duez, C.1    Vanhove, M.2    Gallet, X.3    Bouillenne, F.4    Docquier, J.-D.5    Brans, A.6    Frere, J.-M.7
  • 33
    • 18144413485 scopus 로고    scopus 로고
    • Crystal structure of a peptidoglycan synthesis regulatory factor (PBP3) from Streptococcus pneumoniae
    • DOI 10.1074/jbc.M408446200
    • Morlot, C., Pernot, L., Le Gouellec, A., Di Giulmi, A. M., Vernet, T., Dideberg, O., and Dessen, A. (2005) Crystal structure of a peptidoglycan synthesis regulatory factor (PBP3) from Streptococcus pneumoniae J. Biol. Chem. 280, 15984-15991 (Pubitemid 40616722)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.16 , pp. 15984-15991
    • Morlot, C.1    Pernot, L.2    Le Gouellec, A.3    Di Guilmi, A.M.4    Vernet, T.5    Dideberg, O.6    Dessen, A.7
  • 34
    • 0042068160 scopus 로고    scopus 로고
    • On the substrate specificity of bacterial DD-peptidases: Evidence from two series of peptidoglycan-mimetic peptides
    • DOI 10.1042/BJ20030217
    • Anderson, J. W., Adediran, S. A., Charlier, P., Nguyen-Distèche, M., Frère, J.-M., Nicholas, R. A., and Pratt, R. F. (2003) On the substrate specificity of bacterial dd -peptidases: Evidence from two series of peptidoglycan-mimetic peptides Biochem. J. 373, 949-955 (Pubitemid 36981106)
    • (2003) Biochemical Journal , vol.373 , Issue.3 , pp. 949-955
    • Anderson, J.W.1    Adediran, S.A.2    Charlier, P.3    Nguyen-Disteche, M.4    Frere, J.-M.5    Nicholas, R.A.6    Pratt, R.F.7
  • 35
    • 33845958152 scopus 로고    scopus 로고
    • Reactivity of penicillin-binding proteins with peptidoglycan-mimetic β-lactams: What's wrong with these enzymes?
    • DOI 10.1021/bi061804f
    • Josephine, H. R., Charlier, P., Davies, C., Nicholas, R. A., and Pratt, R. F. (2006) Reactivity of penicillin-binding proteins with peptidoglycan- mimetic β-lactams: What's wrong with these enzymes? Biochemistry 45, 15873-15883 (Pubitemid 46032508)
    • (2006) Biochemistry , vol.45 , Issue.51 , pp. 15873-15883
    • Josephine, H.R.1    Charlier, P.2    Davies, C.3    Nicholas, R.A.4    Pratt, R.F.5
  • 36
    • 0023656752 scopus 로고
    • Structure of the peptide network of pneumococcal peptidoglycan
    • Garcia-Bustos, J. F., Chait, B. T., and Tomasz, A. (1987) Structure of the peptide network of pneumococcal peptidoglycan J. Biol. Chem. 262, 15400-15405
    • (1987) J. Biol. Chem. , vol.262 , pp. 15400-15405
    • Garcia-Bustos, J.F.1    Chait, B.T.2    Tomasz, A.3
  • 37
    • 0030025463 scopus 로고    scopus 로고
    • Naturally occurring peptidoglycan variants of Streptococcus pneumoniae
    • Severin, A. and Tomasz, A. (1996) Naturally occurring peptidoglycan variants of Streptococcus pneumoniae J. Bacteriol. 178, 168-174 (Pubitemid 26006080)
    • (1996) Journal of Bacteriology , vol.178 , Issue.1 , pp. 168-174
    • Severin, A.1    Tomasz, A.2
  • 38
    • 0002279952 scopus 로고    scopus 로고
    • The cell wall of Streptococcus pneumoniae
    • In (Fischetti, V. A. Novick, R. P. Ferretti, J. J. Portnoy, D. A. and Rood, J. I. Eds.) 2nd ed. pp, American Society for Microbiology Press, Washington, DC.
    • Tomasz, A. and Fischer, W. (2006) The cell wall of Streptococcus pneumoniae. In Gram-positive Pathogens (Fischetti, V. A., Novick, R. P., Ferretti, J. J., Portnoy, D. A., and Rood, J. I., Eds.) 2nd ed., pp 230-240, American Society for Microbiology Press, Washington, DC.
    • (2006) Gram-positive Pathogens , pp. 230-240
    • Tomasz, A.1    Fischer, W.2
  • 39
    • 47049099816 scopus 로고    scopus 로고
    • Crystal structures of complexes of bacterial dd -peptidases with peptidoglycan-mimetic ligands; The substrate specificity puzzle
    • Sauvage, E., Powell, A. J., Heilemann, J., Josephine, H. R., Charlier, P., Davies, C., and Pratt, R. F. (2008) Crystal structures of complexes of bacterial dd -peptidases with peptidoglycan-mimetic ligands; the substrate specificity puzzle J. Mol. Biol. 381, 383-393
    • (2008) J. Mol. Biol. , vol.381 , pp. 383-393
    • Sauvage, E.1    Powell, A.J.2    Heilemann, J.3    Josephine, H.R.4    Charlier, P.5    Davies, C.6    Pratt, R.F.7
  • 40
    • 6344219872 scopus 로고    scopus 로고
    • Synthesis and evaluation of new substrate analogues of Streptomyces R61 DD-peptidase: Dissection of a specific ligand
    • DOI 10.1021/jo048885a
    • Nagarajan, R. and Pratt, R. F. (2004) Synthesis and evaluation of new substrate analogues of Streptomyces R61 dd -peptidase: Dissection of a specific ligand J. Org. Chem. 69, 7472-7478 (Pubitemid 39403332)
    • (2004) Journal of Organic Chemistry , vol.69 , Issue.22 , pp. 7472-7478
    • Nagarajan, R.1    Pratt, R.F.2
  • 42
  • 43
    • 38349156636 scopus 로고    scopus 로고
    • Trapping of an acyl-enzyme intermediate in a penicillin binding protein (PBP)-catalyzed reaction
    • Macheboeuf, P., Lemaire, D., Dos Santos Martins, A., Dideberg, O., Jamin, M., and Dessen, A. (2008) Trapping of an acyl-enzyme intermediate in a penicillin binding protein (PBP)-catalyzed reaction J. Mol. Biol. 376, 405-413
    • (2008) J. Mol. Biol. , vol.376 , pp. 405-413
    • MacHeboeuf, P.1    Lemaire, D.2    Dos Santos Martins, A.3    Dideberg, O.4    Jamin, M.5    Dessen, A.6
  • 44
    • 0032985757 scopus 로고    scopus 로고
    • Analysis of peptidoglycan structure from vegetative cells of Bacillus subtilis 168 and role of PBP 5 in peptidoglycan maturation
    • Atrih, A., Bacher, G., Allmaier, G., Williamson, M. P., and Foster, S. J. (1999) Analysis of peptidoglycan structure from vegetative cells of B. subtilis 168 and role of PBP5 in peptidoglycan maturation J. Bacteriol. 181, 3956-3966 (Pubitemid 29295913)
    • (1999) Journal of Bacteriology , vol.181 , Issue.13 , pp. 3956-3966
    • Atrih, A.1    Bacher, G.2    Allmaier, G.3    Williamson, M.P.4    Foster, S.J.5
  • 45
    • 0015237808 scopus 로고
    • Structure of the peptidoglycan from vegetative cell walls of Bacillus subtilis
    • Warth, A. D. and Strominger, J. L. (1971) Structure of the peptidoglycan from vegetative cell walls of Bacillus subtilis Biochemistry 10, 4349-4358
    • (1971) Biochemistry , vol.10 , pp. 4349-4358
    • Warth, A.D.1    Strominger, J.L.2
  • 46
    • 0031715449 scopus 로고    scopus 로고
    • Characterization of dacC, which encodes a new low-molecular- weight penicillin-binding protein in Bacillus subtilis
    • Pederson, L. B., Murray, T., Popham, D. L., and Setlow, P. (1998) Characterization of dacC, which encodes a new low-molecular-weight penicillin-binding protein in Bacillus subtilis J. Bacteriol. 180, 4967-4973 (Pubitemid 28429390)
    • (1998) Journal of Bacteriology , vol.180 , Issue.18 , pp. 4967-4973
    • Pedersen, L.B.1    Murray, T.2    Popham, D.L.3    Setlow, P.4
  • 47
    • 0014585139 scopus 로고
    • Structure of the peptidoglycan of bacterial spores: Occurrences of the lactam of muramic acid
    • Warth, A. D. and Strominger, J. L. (1969) Structure of the peptidoglycan of bacterial spores: Occurrences of the lactam of muramic acid Proc. Natl. Acad. Sci. U.S.A. 64, 528-535
    • (1969) Proc. Natl. Acad. Sci. U.S.A. , vol.64 , pp. 528-535
    • Warth, A.D.1    Strominger, J.L.2
  • 48
    • 78649658087 scopus 로고    scopus 로고
    • Bridging cell wall biosynthesis and bacterial morphogenesis
    • Mattei, P.-J., Neves, D., and Dessen, A. (2010) Bridging cell wall biosynthesis and bacterial morphogenesis Curr. Opin. Struct. Biol. 20, 749-755
    • (2010) Curr. Opin. Struct. Biol. , vol.20 , pp. 749-755
    • Mattei, P.-J.1    Neves, D.2    Dessen, A.3
  • 50
    • 67649199175 scopus 로고    scopus 로고
    • Neisseria gonorrhoeae penicillin-binding protein 3 demonstrates a pronounced preference for Nε-acylated substrates
    • Peddi, S., Nicholas, R. A., and Gutheil, W. G. (2009) Neisseria gonorrhoeae penicillin-binding protein 3 demonstrates a pronounced preference for Nε-acylated substrates Biochemistry 48, 5731-5737
    • (2009) Biochemistry , vol.48 , pp. 5731-5737
    • Peddi, S.1    Nicholas, R.A.2    Gutheil, W.G.3
  • 51
    • 31044432821 scopus 로고    scopus 로고
    • Crystal structure of penicillin binding protein 4 (dacB) from Escherichia coli, both in the native form and covalently linked to various antibiotics
    • DOI 10.1021/bi051533t
    • Kishida, H., Unzai, S., Roper, D. I., Lloyd, A., Park, S.-Y., and Tame, J. R. H. (2006) Crystal structure of penicillin-binding protein 4 (Dac B) from Escherichia coli, both in the native form and covalently linked to various antibiotics Biochemistry 45, 783-792 (Pubitemid 43122243)
    • (2006) Biochemistry , vol.45 , Issue.3 , pp. 783-792
    • Kishida, H.1    Unzai, S.2    Roper, D.I.3    Lloyd, A.4    Park, S.-Y.5    Tame, J.R.H.6
  • 52
    • 35648930904 scopus 로고    scopus 로고
    • Reactions of peptidoglycan-mimetic β-lactams with penicillin-binding proteins in vivo and in membranes
    • DOI 10.1021/cb7001347
    • Kumar, I., Josephine, H. R., and Pratt, R. F. (2007) Reactions of peptidoglycan-mimetic β-lactams with penicillin-binding proteins in vivo and in membranes ACS Chem. Biol. 2, 620-624 (Pubitemid 350019779)
    • (2007) ACS Chemical Biology , vol.2 , Issue.9 , pp. 620-624
    • Kumar, I.1    Josephine, H.R.2    Pratt, R.F.3
  • 53
    • 20444369942 scopus 로고    scopus 로고
    • Crystal structure of Escherichia coli penicillin-binding protein 5 bound to a tripeptide boronic acid inhibitor: A role for Ser-110 in deacylation
    • DOI 10.1021/bi0473004
    • Nicola, G., Peddi, S., Stefanova, M., Nicholas, R. A., Gutheil, W. G., and Davies, C. (2005) Crystal structure of Escherichia coli penicillin-binding protein 5 bound to a tripeptide boronic acid inhibitor: A role for Ser 110 in deacylation Biochemistry 44, 8207-8217 (Pubitemid 40799901)
    • (2005) Biochemistry , vol.44 , Issue.23 , pp. 8207-8217
    • Nicola, G.1    Peddi, S.2    Stefanova, M.3    Nicholas, R.A.4    Gutheil, W.G.5    Davies, C.6
  • 54
    • 0036279811 scopus 로고    scopus 로고
    • Contribution of membrane-binding and enzymatic domains of penicillin binding protein 5 to maintenance of uniform cellular morphology of Escherichia coli
    • DOI 10.1128/JB.184.13.3630-3639.2002
    • Nelson, D. R., Ghosh, A. S., Paulson, A. L., and Young, K. D. (2002) Contribution of membrane-binding and enzymatic domains of penicillin-binding proteins to maintenance of uniform cellular morphology in Escherichia coli J. Bacteriol. 184, 3630-3639 (Pubitemid 34625672)
    • (2002) Journal of Bacteriology , vol.184 , Issue.13 , pp. 3630-3639
    • Nelson, D.E.1    Ghosh, A.S.2    Paulson, A.L.3    Young, K.D.4
  • 56
    • 0029933671 scopus 로고    scopus 로고
    • Effective protein sequence comparison
    • DOI 10.1016/S0076-6879(96)66017-0
    • Pearson, W. R. (1996) Effective protein sequence comparison Methods Enzymol. 266, 227-258 (Pubitemid 26165871)
    • (1996) Methods in Enzymology , vol.266 , pp. 227-258
    • Pearson, W.R.1
  • 57
    • 0027991987 scopus 로고
    • Penicillin-binding protein 7/8 of Escherichia coli is a DD-endopeptidase
    • Romeis, T. and Holtje, J.-V. (1994) Penicillin-binding protein 7/8 of Escherichia coli is a dd -endopeptidase Eur. J. Biochem. 224, 597-604 (Pubitemid 24282845)
    • (1994) European Journal of Biochemistry , vol.224 , Issue.2 , pp. 597-604
    • Romeis, T.1    Holtje, J.-V.2
  • 58
    • 0019256424 scopus 로고
    • Purification and properties of penicillin-binding proteins 5 and 6 from Escherichia coli membranes
    • Amanuma, H. and Strominger, J. L. (1980) Purification and properties of penicillin-binding proteins 5 and 6 from Escherichia coli membranes J. Biol. Chem. 255, 11173-11180 (Pubitemid 11134233)
    • (1980) Journal of Biological Chemistry , vol.255 , Issue.23 , pp. 11173-11180
    • Amanuma, H.1    Strominger, J.L.2
  • 59
    • 0026471637 scopus 로고
    • Possible role of Escherichia coli PBP6 in stabilization of stationary phase peptidoglycan
    • Van der Linden, M. P. G., de Haan, L., Hoger, M. A., and Keck, W. (1992) Possible role of Escherichia coli PBP6 in stabilization of stationary phase peptidoglycan J. Bacteriol. 174, 7572-7578
    • (1992) J. Bacteriol. , vol.174 , pp. 7572-7578
    • Van Der Linden, M.P.G.1    De Haan, L.2    Hoger, M.A.3    Keck, W.4
  • 60
    • 74349093311 scopus 로고    scopus 로고
    • A weak dd -carboxypeptidase activity explains the inability of PBP6 to substitute for PBP5 in maintaining normal cell shape in Escherichia coli
    • Chowdhury, C., Nayak, T. R., Young, K. D., and Ghosh, A. S. (2010) A weak dd -carboxypeptidase activity explains the inability of PBP6 to substitute for PBP5 in maintaining normal cell shape in Escherichia coli FEMS Microbiol. Lett. 303, 76-83
    • (2010) FEMS Microbiol. Lett. , vol.303 , pp. 76-83
    • Chowdhury, C.1    Nayak, T.R.2    Young, K.D.3    Ghosh, A.S.4
  • 61
    • 79751527202 scopus 로고    scopus 로고
    • Differences in active site microarchitecture explain the dissimilar behaviors of PBP5 and PBP6 in Escherichia coli
    • Chowdhury, C. and Ghosh, A. (2011) Differences in active site microarchitecture explain the dissimilar behaviors of PBP5 and PBP6 in Escherichia coli J. Mol. Graphics Modell. 29, 650-656
    • (2011) J. Mol. Graphics Modell. , vol.29 , pp. 650-656
    • Chowdhury, C.1    Ghosh, A.2
  • 63
  • 64
    • 0344603819 scopus 로고    scopus 로고
    • Identification of two penicillin-binding multienzyme complexes in Haemophilus influenzae
    • DOI 10.1006/bbrc.1999.1509
    • Alaedini, A. and Day, R. A. (1999) Identification of two penicillin-binding multienzyme complexes in Haemophilus influenzae Biochem. Biophys. Res. Commun. 264, 191-195 (Pubitemid 29500486)
    • (1999) Biochemical and Biophysical Research Communications , vol.264 , Issue.1 , pp. 191-195
    • Alaedini, A.1    Day, R.A.2
  • 65
    • 0015243756 scopus 로고
    • Conformation of penicillin as a transition-state analog of the substrate of peptidoglycan transpeptidase
    • Lee, B. (1971) Conformation of penicillin as a transition-state analog of the substrate of peptidoglycan transpeptidase J. Mol. Biol. 61, 463-469
    • (1971) J. Mol. Biol. , vol.61 , pp. 463-469
    • Lee, B.1
  • 66
    • 47749153740 scopus 로고    scopus 로고
    • Substrate specificity of bacterial dd -peptidases (penicillin-binding proteins)
    • Pratt, R. F. (2008) Substrate specificity of bacterial dd -peptidases (penicillin-binding proteins) Cell. Mol. Life Sci. 65, 2138-2155
    • (2008) Cell. Mol. Life Sci. , vol.65 , pp. 2138-2155
    • Pratt, R.F.1
  • 67
    • 0032874101 scopus 로고    scopus 로고
    • The catalytic, glycosyl transferase and acyl transferase modules of the cell wall peptidoglycan-polymerizing penicillin-binding protein 1b of Escherichia coli
    • DOI 10.1046/j.1365-2958.1999.01612.x
    • Terrak, M., Ghosh, T. K., van Heijenoort, J., Van Beeumen, J., Lampilis, M., Aszodi, J., Ayala, J. A., Ghuysen, J.-M., and Nguyen-Distèche, M. (1999) The catalytic glycosyl transferase and acyl transferase modules of the cell wall peptidoglycan-polymerizing penicillin-binding protein 1b of Escherichia coli Mol. Microbiol. 34, 350-364 (Pubitemid 29486252)
    • (1999) Molecular Microbiology , vol.34 , Issue.2 , pp. 350-364
    • Terrak, M.1    Ghosh, T.K.2    Van Heijenoort, J.3    Van Beeumen, J.4    Lampilas, M.5    Aszodi, J.6    Ayala, J.A.7    Ghuysen, J.-M.8    Nguyen-Disteche, M.9
  • 68
    • 79960284952 scopus 로고    scopus 로고
    • Transpeptidase-mediated incorporation of d -amino acids into bacterial peptidoglycan
    • Lupoli, T. J., Tsukamoto, H., Doud, E. H., Wang, T.-S. A., Walker, S., and Kahne, D. (2011) Transpeptidase-mediated incorporation of d -amino acids into bacterial peptidoglycan J. Am. Chem. Soc. 133, 10748-10751
    • (2011) J. Am. Chem. Soc. , vol.133 , pp. 10748-10751
    • Lupoli, T.J.1    Tsukamoto, H.2    Doud, E.H.3    Wang, T.-S.A.4    Walker, S.5    Kahne, D.6
  • 70
    • 33745712495 scopus 로고    scopus 로고
    • Structural analysis of an "open" form of PBP 1b from Streptococcus pneumoniae
    • Lovering, A. L., DeCastro, L., Lim, D., and Strynadka, N. C. J. (2006) Structural analysis of an "open" form of PBP 1b from Streptococcus pneumoniae Protein Sci. 15, 1701-1709
    • (2006) Protein Sci. , vol.15 , pp. 1701-1709
    • Lovering, A.L.1    Decastro, L.2    Lim, D.3    Strynadka, N.C.J.4
  • 71
    • 0036829003 scopus 로고    scopus 로고
    • Structural basis for the β-lactam resistance of PBP2a from methicillin-resistant Staphylococcus aureus
    • Lim, D. and Strynadka, N. C. J. (2002) Structural basis for the β-lactam resistance of PBP 2a from methicillin-resistant Staphylococcus aureus Nat. Struct. Biol. 9, 870-876 (Pubitemid 35257789)
    • (2002) Nature Structural Biology , vol.9 , Issue.11 , pp. 870-876
    • Lim, D.1    Strynadka, N.C.J.2
  • 72
    • 4644366894 scopus 로고    scopus 로고
    • The basis for resistance to β-lactam antibiotics by penicillin-binding protein 2a of methicillin-resistant Staphylococcus aureus
    • DOI 10.1074/jbc.M403589200
    • Fuda, C., Savarov, M., Vakulenko, S. B., and Mobashery, S. (2004) The basis for resistance to β-lactam antibiotics by penicillin-binding protein 2a of methicillin-resistant Staphylococcus aureus J. Biol. Chem. 279, 40802-40806 (Pubitemid 39287677)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.39 , pp. 40802-40806
    • Fuda, C.1    Suvorov, M.2    Vakulenko, S.B.3    Mobashery, S.4
  • 73
    • 13944282888 scopus 로고    scopus 로고
    • Activation for catalysis of penicillin-binding protein 2a from methicillin-resistant Staphylococcus aureus by bacterial cell wall
    • DOI 10.1021/ja0434376
    • Fuda, C., Hesek, D., Lee, M., Morio, K., Thomas, N., and Mobashery, S. (2005) Activation for catalysis of penicillin-binding protein 2a from methicillin-resistant Staphylococcus aureus by bacterial cell wall J. Am. Chem. Soc. 127, 2056-2057 (Pubitemid 40270504)
    • (2005) Journal of the American Chemical Society , vol.127 , Issue.7 , pp. 2056-2057
    • Fuda, C.1    Hesek, D.2    Lee, M.3    Morio, K.-I.4    Nowak, T.5    Mobashery, S.6
  • 74
    • 0033558272 scopus 로고    scopus 로고
    • Hydrogen bonding and protein perturbation in β-lactam acyl-enzymes of Streptococcus pneumoniae penicillin-binding protein PBP2x
    • DOI 10.1042/0264-6021:3380153
    • Chittock, R. S., Ward, S., Wilkinson, A.-S., Caspers, P., Mensch, B., Page, M. G. P., and Wharton, C. W. (1999) Hydrogen-bonding and protein perturbation in β-lactam acyl-enzymes of Streptococcus pneumoniae penicillin-binding protein PBP2x Biochem. J. 338, 153-159 (Pubitemid 29097298)
    • (1999) Biochemical Journal , vol.338 , Issue.1 , pp. 153-159
    • Chittock, R.S.1    Ward, S.2    Wilkinson, A.-S.3    Caspers, P.4    Mensch, B.5    Page, M.G.P.6    Wharton, C.W.7


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