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PMID: 331322 Published · ppublish English Journal Article

Mutants of Escherichia coli lacking in highly penicillin-sensitive D-alanine carboxypeptidase activity.

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 74 ·No. 7 ·1977-07-00 ·Pages 2976-9

Matsuhashi M, Takagaki Y, Maruyama IN, Tamaki S, Nishimura Y, Suzuki H, Ogino U, Hirota Y

Abstract

Mutants of Escherichia coli lacking in the highly penicillin-sensitive enzyme activities of D-carboxy-peptidase, transpeptidase, and endopeptidase, and with the concomitant absence of penicillin-binding protein 4 of B.G. Spratt and A.B. Pardee [(1975) Nature 254, 516-517] were isolated. The defect of these mutants is ascribed to the lack of an enzyme, D-alanine carboxypeptidase Ib. Genetic mapping studies show the mutation (dacB) to be located at 68 min on the E. coli chromosome map. The dacB mutation results in the simultaneous loss of D-alanine carboxypeptidase and penicillin-binding protein 4. The mutants grew normally under a wide range of growth conditions. We conclude that the enzyme is not a necessary component for normal peptidoglycan biosynthesis in E. coli.

MeSH Terms
Alanine Carboxypeptidases/antagonists & inhibitors,deficiency Carrier Proteins/deficiency Chromosome Mapping Escherichia coli/enzymology,metabolism Genes Mutation Penicillin G/metabolism,pharmacology Peptidoglycan/biosynthesis Temperature
Chemicals
Carrier Proteins Peptidoglycan Carboxypeptidases Alanine Penicillin G
Authors & Affiliations
8 authors, click to expand affiliations / ORCID
Matsuhashi M
Takagaki Y
Maruyama I N
Tamaki S
Nishimura Y
Suzuki H
Ogino U
Hirota Y
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
DOI
10.1073/pnas.74.7.2976
Published
1977-07-00
Pages
2976-9
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC431370
Subset
IM
External Links
PubMed source DOI: 10.1073/pnas.74.7.2976 PMC Full Text View journal details
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