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Article

Crystal structure of a deacylation-defective mutant of penicillin-binding protein 5 at 2.3-A resolution.

The Journal of biological chemistry - 5 Jan 2001

Davies C, White S W, Nicholas R A

Abstract excerpt

Penicillin-binding protein 5 (PBP 5) of Escherichia coli functions as a d-alanine carboxypeptidase, cleaving the C-terminal d-alanine residue from cell wall peptides. Like all PBPs, PBP 5 forms a covalent acyl-enzyme complex with beta-lactam antibiotics; however, PBP 5 is distinguished by its high rate of deacylation of the acyl-enzyme complex (t(12) approximately 9 min). A Gly-105 --> Asp mutation in PBP 5...

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PMID: 10967102
DOI: 10.1074/jbc.M004471200

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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