Relatedness of penicillin-binding proteins from various Listeria species.
The heterogeneity of penicillin-binding proteins (PBPs) of five Listeria species was investigated. Similarities in the overall PBP pattern were found between those of L. welshimeri and L. innocua, and between L. ivanovii and L. seeligeri, and all were distinct from the PBPs of L. monocytogenes. In all species, however, the primary target for beta-lactam antibiotics, as identified in L. monocytogenes recently, appeared highly conserved. In addition, the low-Mr PBP 5 was biochemically very similar in all strains and contained identical binding properties to beta-lactam compounds, suggesting that this protein may play an important role. All other PBPs varied considerably in their penicilloyl-peptide pattern, indicating differences in their amino acid sequences.
Hakenbeck
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Max-Planck Institut für molekulare Genetik, Berlin, F.R.G.
Hof
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D000900:Anti-Bacterial Agents / Q000378:metabolism; D001426:Bacterial Proteins; D002352:Carrier Proteins / Q000737:chemistry* / Q000378:metabolism; D004591:Electrophoresis, Polyacrylamide Gel; D006602:Hexosyltransferases; D007769:Lactams; D008087:Listeria / Q000737:chemistry*; D002267:Muramoylpentapeptide Carboxypeptidase / Q000737:chemistry* / Q000378:metabolism; D046915:Penicillin-Binding Proteins; D010406:Penicillins / Q000378:metabolism*; D010458:Peptidyl Transferases; D012697:Serine Endopeptidases; D013045:Species Specificity
D000900:Anti-Bacterial Agents; D001426:Bacterial Proteins; D002352:Carrier Proteins; D007769:Lactams; D046915:Penicillin-Binding Proteins; D010406:Penicillins; D010458:Peptidyl Transferases; D006602:Hexosyltransferases; D002267:Muramoylpentapeptide Carboxypeptidase; D012697:Serine Endopeptidases; C028344:glutamyl endopeptidase