PMID:6693351
| Citation |
Park, W and Matsuhashi, M (1984) Staphylococcus aureus and Micrococcus luteus peptidoglycan transglycosylases that are not penicillin-binding proteins. J. Bacteriol. 157:538-44 |
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| Abstract |
Major peptidoglycan transglycosylase activities, which synthesize uncross-linked peptidoglycan from lipid-linked precursors, were solubilized from the membranes of Staphylococcus aureus and Micrococcus luteus and were partially purified. The transglycosylase activities were separated from penicillin-binding proteins by solubilization and by purification steps. Therefore, we concluded that these activities were not activities of the penicillin-binding proteins, which are the presumptive peptidoglycan transpeptidases in these gram-positive cocci. Unlike Escherichia coli, in which the network structure of peptidoglycan is synthesized by multiple two-headed penicillin-binding proteins with both transpeptidase and transglycosylase activities, these gram-positive cocci have cell wall peptidoglycan which seems to be synthesized by penicillin-binding protein transpeptidases and a separate transglycosylase. |
| Links | |
| Keywords |
Bacterial Proteins; Carboxypeptidases/metabolism; Carrier Proteins/metabolism; Chromatography, Affinity/methods; Chromatography, DEAE-Cellulose/methods; Hexosyltransferases/isolation & purification; Hexosyltransferases/metabolism; Kinetics; Micrococcus/enzymology; Molecular Weight; Muramoylpentapeptide Carboxypeptidase/metabolism; Penicillin-Binding Proteins; Peptidoglycan Glycosyltransferase; Peptidyl Transferases; Staphylococcus aureus/enzymology |
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