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PMID: 6995448 Published · ppublish English Journal Article Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S.

A mutant of Escherichia coli defective in penicillin-binding protein 5 and lacking D-alanine carboxypeptidase IA.

Journal of bacteriology ·Vol. 143 ·No. 1 ·1980-07-00 ·Pages 531-4

Nishimura Y, Suzuki H, Hirota Y, Park JT

Abstract

A mutant of Escherichia coli defective in penicillin-binding protein 5 activity was isolated. The mutation (pfv) was shown to be located at 14.0 min on the E. coli chromosome map. Loss of penicillin-binding protein 5 in the pfv mutant was associated with the loss of D-alanine carboxypeptidase IA activity and increased sensitivity to beta-lactam antibiotics. We conclude that penicillin-binding protein 5 catalyzes the major D-alanine carboxypeptidase IA activity and that the enzyme activity, in vivo, protects E. coli cells from killing by low inhibitory concentrations of beta-lactam antibiotics.

MeSH Terms
Bacterial Proteins/genetics,physiology Carboxypeptidases/genetics Carrier Proteins/genetics,physiology Escherichia coli/genetics,metabolism Muramoylpentapeptide Carboxypeptidase/genetics,physiology Mutation Penicillin G/metabolism
Chemicals
Bacterial Proteins Carrier Proteins Carboxypeptidases Muramoylpentapeptide Carboxypeptidase Penicillin G
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Nishimura Y
Suzuki H
Hirota Y
Park J T
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21 references, click to expand
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Article Info
Journal
Journal of bacteriology
Abbr.
J Bacteriol
ISSN
0021-9193
DOI
10.1128/jb.143.1.531-534.1980
Published
1980-07-00
Pages
531-4
Language
English
Region
United States
NLM ID
2985120R
PMCID
PMC294284
Subset
IM
External Links
PubMed source DOI: 10.1128/jb.143.1.531-534.1980 PMC Full Text View journal details
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