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Volumn 34, Issue 2, 1999, Pages 350-364

The catalytic, glycosyl transferase and acyl transferase modules of the cell wall peptidoglycan-polymerizing penicillin-binding protein 1b of Escherichia coli

Author keywords

[No Author keywords available]

Indexed keywords

ACYLTRANSFERASE; BACTERIAL ENZYME; BACTERIAL PROTEIN; CELL MEMBRANE PROTEIN; GLYCOSYLTRANSFERASE; PENICILLIN BINDING PROTEIN; PEPTIDOGLYCAN; TRANSFERASE;

EID: 0032874101     PISSN: 0950382X     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1365-2958.1999.01612.x     Document Type: Article
Times cited : (150)

References (39)
  • 1
    • 0025944297 scopus 로고
    • Acyltransferase activities of the high-molecular-mass essential penicillin-binding proteins
    • Adam, M., Damblon, C., Jamin, M., Zorzi, W., Dusart, V., Galleni, M., et al. (1991) Acyltransferase activities of the high-molecular-mass essential penicillin-binding proteins. Biochem J 279: 601-604.
    • (1991) Biochem J , vol.279 , pp. 601-604
    • Adam, M.1    Damblon, C.2    Jamin, M.3    Zorzi, W.4    Dusart, V.5    Galleni, M.6
  • 2
    • 9044250489 scopus 로고    scopus 로고
    • Identification and overexpression in Escherichia coli of a Mycobacterium leprae gene, pon1, encoding a high-molecular-mass class A penicillin-binding protein, PBP1
    • Basu, J., Mahapatra, S., Kundu, M., Mukhopadhyay, S., Nguyen-Distèche, M., Dubois, P., et al. (1996) Identification and overexpression in Escherichia coli of a Mycobacterium leprae gene, pon1, encoding a high-molecular-mass class A penicillin-binding protein, PBP1. J Bacteriol 178: 1707-1711.
    • (1996) J Bacteriol , vol.178 , pp. 1707-1711
    • Basu, J.1    Mahapatra, S.2    Kundu, M.3    Mukhopadhyay, S.4    Nguyen-Distèche, M.5    Dubois, P.6
  • 3
    • 0021948440 scopus 로고
    • The nucleotide sequences of the ponA and ponB genes encoding penicillin-binding proteins 1A and 1B of Escherichia coli K12
    • Broome-Smith, J.K., Edelman, A., Yousif, S., and Spratt, B.G. (1985) The nucleotide sequences of the ponA and ponB genes encoding penicillin-binding proteins 1A and 1B of Escherichia coli K12. Eur J Biochem 147: 437-446.
    • (1985) Eur J Biochem , vol.147 , pp. 437-446
    • Broome-Smith, J.K.1    Edelman, A.2    Yousif, S.3    Spratt, B.G.4
  • 4
    • 0018575015 scopus 로고
    • Affinities of penicillins and cephalosporins for the penicillin-binding proteins of Escherichia coli K12 and their antibacterial activity
    • Curtis, N.A.C., Orr, D., Ross, G.W., and Boulton, M.G. (1979) Affinities of penicillins and cephalosporins for the penicillin-binding proteins of Escherichia coli K12 and their antibacterial activity. Antimicrob Agents Chemother 16: 533-539.
    • (1979) Antimicrob Agents Chemother , vol.16 , pp. 533-539
    • Curtis, N.A.C.1    Orr, D.2    Ross, G.W.3    Boulton, M.G.4
  • 5
    • 0031771077 scopus 로고    scopus 로고
    • Identification, purification, and characterization of transpeptidase and glycosyltransferase domains of Streptococcus pneumoniae penicillin-binding protein 1a
    • Di Guilmi, A.M., Mouz, N., Andrieu, J.P., Hoskins, J., Jaskunas, S.R., Gagnon, J., et al. (1998) Identification, purification, and characterization of transpeptidase and glycosyltransferase domains of Streptococcus pneumoniae penicillin-binding protein 1a. J Bacteriol 180: 5652-5659.
    • (1998) J Bacteriol , vol.180 , pp. 5652-5659
    • Di Guilmi, A.M.1    Mouz, N.2    Andrieu, J.P.3    Hoskins, J.4    Jaskunas, S.R.5    Gagnon, J.6
  • 6
    • 0023370184 scopus 로고
    • Use of a β-lactamase fusion vector to investigate the organization of penicillin-binding protein 1B in the cytoplasmic membrane of Escherichia coli
    • Edelman, A., Bowler, L, Broome-Srnith, J.K., and Spratt, B.G. (1987) Use of a β-lactamase fusion vector to investigate the organization of penicillin-binding protein 1B in the cytoplasmic membrane of Escherichia coli. Mol Microbiol 1: 101-106.
    • (1987) Mol Microbiol , vol.1 , pp. 101-106
    • Edelman, A.1    Bowler, L.2    Broome-Srnith, J.K.3    Spratt, B.G.4
  • 7
    • 0027952718 scopus 로고
    • Engineering and overexpression of periplasmic forms of the penicillin-binding protein 3 of Escherichia coli
    • Fraipont, C., Adam, M., Nguyen-Distèche, M., Keck, W., Van Beeumen, J., Ayala, J.A., et al. (1994) Engineering and overexpression of periplasmic forms of the penicillin-binding protein 3 of Escherichia coli. Biochem J 298: 189-195.
    • (1994) Biochem J , vol.298 , pp. 189-195
    • Fraipont, C.1    Adam, M.2    Nguyen-Distèche, M.3    Keck, W.4    Van Beeumen, J.5    Ayala, J.A.6
  • 8
    • 0001930562 scopus 로고
    • Mode of action: Interaction with the penicillin-binding proteins
    • Page, M.I. (ed.). London: Blackie Academic and Professional
    • Frère, J.M., Nguyen-Distèche, M., Coyette, J., and Joris, B. (1992) Mode of action: interaction with the penicillin-binding proteins. In The Chemistry of β-Lactams. Page, M.I. (ed.). London: Blackie Academic and Professional, pp. 148-197.
    • (1992) The Chemistry of β-Lactams , pp. 148-197
    • Frère, J.M.1    Nguyen-Distèche, M.2    Coyette, J.3    Joris, B.4
  • 9
    • 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
  • 10
    • 0023677844 scopus 로고
    • The composition of the murein of Escherichia coli
    • Glauner, B., Höltje, J.V., and Schwarz, U. (1988) The composition of the murein of Escherichia coli. J Biol Chem 263: 10088-10095.
    • (1988) J Biol Chem , vol.263 , pp. 10088-10095
    • Glauner, B.1    Höltje, J.V.2    Schwarz, U.3
  • 11
    • 0031736387 scopus 로고    scopus 로고
    • Multimodular penicillin-binding proteins: An enigmatic family of orthologs and paralogs
    • Goffin, C., and Ghuysen, J.M. (1998) Multimodular penicillin-binding proteins: an enigmatic family of orthologs and paralogs. Microbiol Mol Biol Rev 62: 1079-1093.
    • (1998) Microbiol Mol Biol Rev , vol.62 , pp. 1079-1093
    • Goffin, C.1    Ghuysen, J.M.2
  • 12
    • 0021062307 scopus 로고
    • Absence of oligomeric murein intermediates in Escherichia coli
    • Goodell, E.W., Markiewicz, Z., and Schwarz, U. (1983) Absence of oligomeric murein intermediates in Escherichia coli. J Bacteriol 156: 130-135.
    • (1983) J Bacteriol , vol.156 , pp. 130-135
    • Goodell, E.W.1    Markiewicz, Z.2    Schwarz, U.3
  • 13
    • 0028672898 scopus 로고
    • Serine-type D-Ala-D-Ala peptidases and penicillin-binding proteins
    • Granier, B., Jamin, M., Adam, M., Galleni, M., Lakaye, B., Zorzi, W., et al. (1994) Serine-type D-Ala-D-Ala peptidases and penicillin-binding proteins. Methods Enzymol 244: 249-266.
    • (1994) Methods Enzymol , vol.244 , pp. 249-266
    • Granier, B.1    Jamin, M.2    Adam, M.3    Galleni, M.4    Lakaye, B.5    Zorzi, W.6
  • 14
    • 0028020739 scopus 로고
    • Crystal structure of the mutant D52S hen egg white lysozyme with an oligosaccharide product
    • Hadfield, A.T., Harvey, D.J., Archer, D.B., MacKenzie, D.A., Jeenes, D.J., Radford, S.E., et al. (1994) Crystal structure of the mutant D52S hen egg white lysozyme with an oligosaccharide product. J Mol Biol 243: 856-872.
    • (1994) J Mol Biol , vol.243 , pp. 856-872
    • Hadfield, A.T.1    Harvey, D.J.2    Archer, D.B.3    MacKenzie, D.A.4    Jeenes, D.J.5    Radford, S.E.6
  • 15
    • 0021760880 scopus 로고
    • A novel glycan polymerase that synthesizes uncross-linked peptidoglycan in Escherichia coli
    • Hara, H., and Suzuki, H. (1984) A novel glycan polymerase that synthesizes uncross-linked peptidoglycan in Escherichia coli. FEBS Lett 168: 155-160.
    • (1984) FEBS Lett , vol.168 , pp. 155-160
    • Hara, H.1    Suzuki, H.2
  • 16
    • 0000996675 scopus 로고    scopus 로고
    • Murein synthesis
    • Neidhardt, F.C. (ed.).Washington, DC: American Society for Microbiology Press
    • van Heijenoort, J. (1996) Murein synthesis. In Escherichia coli and Salmonella. Neidhardt, F.C. (ed.).Washington, DC: American Society for Microbiology Press, pp. 1025-1034.
    • (1996) Escherichia Coli and Salmonella , pp. 1025-1034
    • Van Heijenoort, J.1
  • 17
    • 0026623124 scopus 로고
    • Membrane intermediates in the peptidoglycan metabolism of Escherichia coli: Possible roles of PBP1b and PBP3
    • van Heijenoort, Y., Gomez, M., Derrien, M., Ayala, J., and van Heijenoort, J. (1992) Membrane intermediates in the peptidoglycan metabolism of Escherichia coli: possible roles of PBP1b and PBP3. J Bacteriol 174: 3549-3557.
    • (1992) J Bacteriol , vol.174 , pp. 3549-3557
    • Van Heijenoort, Y.1    Gomez, M.2    Derrien, M.3    Ayala, J.4    Van Heijenoort, J.5
  • 18
    • 0028082052 scopus 로고
    • Artifactual processing of penicillin-binding proteins 7 and 1b by the OmpT protease of Escherichia coli
    • Henderson, T.A., Dombrosky, P.M., and Young, K.D. (1994) Artifactual processing of penicillin-binding proteins 7 and 1b by the OmpT protease of Escherichia coli. J Bacteriol 176: 256-259.
    • (1994) J Bacteriol , vol.176 , pp. 256-259
    • Henderson, T.A.1    Dombrosky, P.M.2    Young, K.D.3
  • 19
    • 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.
    • (1998) Microbiol Mol Biol Rev , vol.62 , pp. 181-203
    • Höltje, J.V.1
  • 20
    • 0019289889 scopus 로고
    • Dual enzyme activities of cell wall peptidoglycan synthesis, peptidoglycan transglycosylase and penicillin-sensitive transpeptidase, in purified preparations of Escherichia coli penicillin-binding protein 1A
    • Ishino, F., Mitsui, K., Tamaki, S., and Matsuhashi, M. (1980) Dual enzyme activities of cell wall peptidoglycan synthesis, peptidoglycan transglycosylase and penicillin-sensitive transpeptidase, in purified preparations of Escherichia coli penicillin-binding protein 1A. Biochem Biophys Res Commun 97: 287-293.
    • (1980) Biochem Biophys Res Commun , vol.97 , pp. 287-293
    • Ishino, F.1    Mitsui, K.2    Tamaki, S.3    Matsuhashi, M.4
  • 21
    • 0025952119 scopus 로고
    • Accumulation of acyl-enzyme in DD-peptidase-catalysed reactions with analogues of peptide substrates
    • Jamin, M., Adam, M., Damblon, C., Christiaens, L., and Frère, J.M. (1991) Accumulation of acyl-enzyme in DD-peptidase-catalysed reactions with analogues of peptide substrates. Biochem J 280: 499-506.
    • (1991) Biochem J , vol.280 , pp. 499-506
    • Jamin, M.1    Adam, M.2    Damblon, C.3    Christiaens, L.4    Frère, J.M.5
  • 22
    • 0021198846 scopus 로고
    • Overlapping of the coding regions for α and γ components of penicillin-binding protein 1b in Escherichia coli
    • Kato, J., Suzuki, H., and Hirota, Y. (1984) Overlapping of the coding regions for α and γ components of penicillin-binding protein 1b in Escherichia coli. Mol Gen Genet 196: 449-457.
    • (1984) Mol Gen Genet , vol.196 , pp. 449-457
    • Kato, J.1    Suzuki, H.2    Hirota, Y.3
  • 23
    • 0021862671 scopus 로고
    • Dispensability of either penicillin-binding protein 1a or 1b involved in the essential process for cell elongation in Escherichia coli
    • Kato, J., Suzuki, H., and Hirota, Y. (1985) Dispensability of either penicillin-binding protein 1a or 1b involved in the essential process for cell elongation in Escherichia coli. Mol Gen Genet 200: 272-277.
    • (1985) Mol Gen Genet , vol.200 , pp. 272-277
    • Kato, J.1    Suzuki, H.2    Hirota, Y.3
  • 24
    • 1842411838 scopus 로고    scopus 로고
    • Topographical and functional investigation of Escherichia coli penicillin-binding protein 1b by alanine stretch scanning mutagenesis
    • Lefèvre, F., Rémy, M.H., and Masson, J.M. (1997) Topographical and functional investigation of Escherichia coli penicillin-binding protein 1b by alanine stretch scanning mutagenesis. J Bacteriol 179: 4761-4767.
    • (1997) J Bacteriol , vol.179 , pp. 4761-4767
    • Lefèvre, F.1    Rémy, M.H.2    Masson, J.M.3
  • 25
    • 0030856585 scopus 로고    scopus 로고
    • Dual multimodular class A penicillin-binding proteins in Mycobacterium leprae
    • Lepage, S., Dubois, P., Ghosh, T.K., Joris, B., Mahapatra, S., Kundu, M., et al. (1997) Dual multimodular class A penicillin-binding proteins in Mycobacterium leprae. J Bacteriol 179: 4627-4630.
    • (1997) J Bacteriol , vol.179 , pp. 4627-4630
    • Lepage, S.1    Dubois, P.2    Ghosh, T.K.3    Joris, B.4    Mahapatra, S.5    Kundu, M.6
  • 29
    • 0021690285 scopus 로고
    • Functional biosynthesis of cell wall peptidoglycan by polymorphic bifunctional polypeptides
    • Nakagawa, J., Tamaki, S., Tomioka, S., and Matsuhashi, M. (1984) Functional biosynthesis of cell wall peptidoglycan by polymorphic bifunctional polypeptides. J Biol Chem 259: 13937-13946.
    • (1984) J Biol Chem , vol.259 , pp. 13937-13946
    • Nakagawa, J.1    Tamaki, S.2    Tomioka, S.3    Matsuhashi, M.4
  • 31
    • 0027469853 scopus 로고
    • Penicillin-binding protein 1B from Escherichia coli contains a membrane association site in addition to its transmembrane anchor
    • Nicholas, R.A., Lamson, D.R., and Schultz, D.E. (1993) Penicillin-binding protein 1B from Escherichia coli contains a membrane association site in addition to its transmembrane anchor. J Biol Chem 268: 5632-5641.
    • (1993) J Biol Chem , vol.268 , pp. 5632-5641
    • Nicholas, R.A.1    Lamson, D.R.2    Schultz, D.E.3
  • 32
    • 0005118683 scopus 로고
    • pIN-III-ompA secretion vectors: Modification of the ompA signal peptide sequence for easier insert cloning
    • Rentier-Delrue, F., Swennen, D., and Martial, J. (1988) pIN-III-ompA secretion vectors: modification of the ompA signal peptide sequence for easier insert cloning. Nucleic Acids Res 16: 8726.
    • (1988) Nucleic Acids Res , vol.16 , pp. 8726
    • Rentier-Delrue, F.1    Swennen, D.2    Martial, J.3
  • 33
    • 0030058939 scopus 로고    scopus 로고
    • Monofunctional biosynthetic peptidoglycan transglycosylases
    • Spratt, B.G., Zhou, J., Taylor, M., and Merrick, M.J. (1996) Monofunctional biosynthetic peptidoglycan transglycosylases. Mol Microbiol 19: 639-647.
    • (1996) Mol Microbiol , vol.19 , pp. 639-647
    • Spratt, B.G.1    Zhou, J.2    Taylor, M.3    Merrick, M.J.4
  • 34
    • 0023189083 scopus 로고
    • Multicopy expression vectors carrying the lac repressor gene for regulated high-level expression of genes in Escherichia coli
    • Stark, M.J.R. (1987) Multicopy expression vectors carrying the lac repressor gene for regulated high-level expression of genes in Escherichia coli. Gene 51: 255-267.
    • (1987) Gene , vol.51 , pp. 255-267
    • Stark, M.J.R.1
  • 35
    • 0017803849 scopus 로고
    • On the process of cellular division in Escherichia coli: A series of mutants of E. coli altered in the penicillin-binding proteins
    • Suzuki, H., Nishimura, Y., and Hirota, Y. (1978) On the process of cellular division in Escherichia coli: a series of mutants of E. coli altered in the penicillin-binding proteins. Proc Natl Acad Sci USA 75: 664-668.
    • (1978) Proc Natl Acad Sci USA , vol.75 , pp. 664-668
    • Suzuki, H.1    Nishimura, Y.2    Hirota, Y.3
  • 36
    • 0018855285 scopus 로고
    • In vitro peptidoglycan polymerization catalysed by penicillin binding protein 1b of Escherichia coli K12
    • Suzuki, H., van Heijenoort, Y., Tamura, T., Mizoguchi, J., Hirota, Y., and van Heijenoort, J. (1980) In vitro peptidoglycan polymerization catalysed by penicillin binding protein 1b of Escherichia coli K12. FEBS Lett 110: 245-249.
    • (1980) FEBS Lett , vol.110 , pp. 245-249
    • Suzuki, H.1    Van Heijenoort, Y.2    Tamura, T.3    Mizoguchi, J.4    Hirota, Y.5    Van Heijenoort, J.6
  • 37
    • 0029052863 scopus 로고
    • The catalytic domain of a bacterial lytic transglycosylase defines a novel class of lysozymes
    • Thunnissen, A.M.W.H., Isaacs, N.W., and Dijkstra, W. (1995) The catalytic domain of a bacterial lytic transglycosylase defines a novel class of lysozymes. Proteins: Struct Funct Genet 22: 245-258.
    • (1995) Proteins: Struct Funct Genet , vol.22 , pp. 245-258
    • Thunnissen, A.M.W.H.1    Isaacs, N.W.2    Dijkstra, W.3
  • 38
    • 0029888520 scopus 로고    scopus 로고
    • Localization of a putative second membrane association site in penicillin-binding 1B of Escherichia coli
    • Wang, C.C., Schultz, D.E., and Nicholas, R.A. (1996) Localization of a putative second membrane association site in penicillin-binding 1B of Escherichia coli. Biochem J 316: 149-156.
    • (1996) Biochem J , vol.316 , pp. 149-156
    • Wang, C.C.1    Schultz, D.E.2    Nicholas, R.A.3
  • 39
    • 0015737203 scopus 로고
    • The direction of glycan synthesis in a bacterial peptidoglycan
    • Ward, J.B., and Perkins, H.R. (1973) The direction of glycan synthesis in a bacterial peptidoglycan. Biochem J 135: 721-728.
    • (1973) Biochem J , vol.135 , pp. 721-728
    • Ward, J.B.1    Perkins, H.R.2


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