doi: 10.1128/jb.168.1.199-206.1986.
Activity of penicillin-binding protein 3 from Escherichia coli
- PMID: 3531167
- PMCID: PMC213438
- DOI: 10.1128/jb.168.1.199-206.1986
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Activity of penicillin-binding protein 3 from Escherichia coli
J Bacteriol.
1986 Oct.
Abstract
The activity of penicillin-binding protein 3 of Escherichia coli has been studied both in vivo and in ether-permeabilized cells. The peptidoglycan transpeptidase activity of penicillin-binding protein 3 appears to use either nascent or exogenously added UDP-N-acetylmuramyl tripeptide-derived substrates as acceptors. By means of a defilamentation system which elicited the activity of penicillin-binding protein 3 in vivo, the structure of peptidoglycan made by this enzyme has been elucidated. This peptidoglycan, very probably of septal location, contained increased amounts of cross-linked peptidoglycan as well as a higher ratio of tripeptide-containing cross-linked subunits.
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