Abstract
Mutants of Escherichia coli with much decreased activity of D-alanine carboxypeptidase (peptidyl-D alanine hydrolase, EC 3.4.12.11) were found among E. coli K12 extensively mutagenized with nitrosoguanidine treatment by assaying individual colonies for the enzyme activity. One such mutant with only 10-12% residual activity was characterized extensively. The soluble carboxypeptidase activity (corresponding to D-alanine carboxypeptidase IC of Tamura T., Imae, Y. & Strominger, J.L. [(1976) J. Biol. Chem. 251, 414-423] was deleted. This enzyme activity in the particulate fraction was markedly reduced but transpeptidase activity was normal. However, penicillin-binding component IV was deleted from the particulate fraction. Both the physiology and penicillin sensitivity of the organism were relatively normal, except that mutant cells were markedly more stable to penicillin-induced lysis, suggesting the possibility that carboxypeptidase IC really functions as an endopeptidase. The possible relationship of the deleted carboxypeptidase activity and the deleted penicillin binding component are discussed.
MeSH Terms
Ampicillin/pharmacology
Carboxypeptidases/deficiency
Carrier Proteins
Chromosome Aberrations
Chromosome Deletion
Deoxycholic Acid/pharmacology
Escherichia coli/drug effects,enzymology,metabolism
Muramoylpentapeptide Carboxypeptidase/deficiency
Mutation
Penicillin G/metabolism
Subcellular Fractions/enzymology
Chemicals
Carrier Proteins
Deoxycholic Acid
Ampicillin
Carboxypeptidases
Muramoylpentapeptide Carboxypeptidase
Penicillin G
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Iwaya M
Strominger J L
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20 references, click to expand
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