DD-carboxypeptidase-transpeptidase and killing site of beta-lactam antibiotics in Streptomyces strains R39, R61, and K11.

Antimicrobial agents and chemotherapy ·Vol. 3 ·No. 2 ·1973-02-00 ·Pages 181-7

Dusart J, Marquet A, Ghuysen JM, Frère JM, Moreno R, Leyh-Bouille M, Johnson K, Lucchi C, Perkins HR, Nieto M

Abstract

Additional evidence is given that in Streptomyces strains R39, R61, and K11 the same enzyme performs dd-carboxypeptidase and transpeptidase activities and that this enzyme is the killing site of beta-lactam antibiotics. With strain R61, it was found that the exocellular enzyme has a sensitivity towards some antibiotics different from that of the membrane-bound enzyme. Under the growth conditions used in the present investigations, beta-lactamase activity was not involved in susceptibility to beta-lactam antibiotics.

MeSH Terms

Acyltransferases/metabolism Anti-Bacterial Agents/pharmacology Carboxypeptidases/antagonists & inhibitors,metabolism Penicillinase/metabolism Streptomyces/drug effects,enzymology beta-Lactams/pharmacology

Chemicals

Anti-Bacterial Agents beta-Lactams Acyltransferases Carboxypeptidases Penicillinase

Authors & Affiliations

10 authors, click to expand affiliations / ORCID

Dusart J

Marquet A

Ghuysen J M

Frère J M

Moreno R

Leyh-Bouille M

Johnson K

Lucchi C

Perkins H R

Nieto M

References (12)

12 references, click to expand

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Penicillin: its basic site of action as an inhibitor of a peptide cross-linking reaction in cell wall mucopeptide synthesis.
Proc Natl Acad Sci U S A. 1965 Jul;54(1):75-81 PMID: 5216369
Exocellular beta-lactamases of Streptomyces albus G and strains R39 and K11.
Antimicrob Agents Chemother. 1973 Feb;3(2):289-98 PMID: 4494518
Penicillin-sensitive DD-carboxypeptidases from Streptomyces strains R39 and K11.
Biochemistry. 1972 Mar 28;11(7):1290-8 PMID: 5012980
The inhibition of mucopeptide synthesis by benzylpenicillin in relation to irreversible fixation of the antibiotic by staphylococci.
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Penicillin-sensitive DD-carboxypeptidase from Streptomyces strain R 61.
Biochemistry. 1971 May 25;10(11):2163-70 PMID: 4998135
Inactivation of D-alanine carboxypeptidase by penicillins and cephalosporins is not lethal in Bacillus subtilis.
Proc Natl Acad Sci U S A. 1971 Nov;68(11):2814-7 PMID: 4330943
Transpeptidase activity of Streptomyces D-alanyl-D carboxypeptidases.
Proc Natl Acad Sci U S A. 1972 Mar;69(3):662-6 PMID: 4501580
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J Cell Physiol. 1970 Dec;76(3):397-403 PMID: 4993702
Screening bacterial colonies for penicillinase production.
Nature. 1962 Jul 21;195:287-8 PMID: 13893830
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Article Info

Journal

Antimicrobial agents and chemotherapy

Abbr.

Antimicrob Agents Chemother

ISSN

0066-4804

DOI

10.1128/AAC.3.2.181

Published

1973-02-00

Pages

181-7

Language

English

Region

United States

NLM ID

0315061

PMCID

PMC444384

Subset

External Links

PubMed source DOI: 10.1128/AAC.3.2.181 PMC Full Text View journal details

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DD-carboxypeptidase-transpeptidase and killing site of beta-lactam antibiotics in Streptomyces strains R39, R61, and K11.

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