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PMID: 949323 Published · ppublish English Journal Article

Mode of interaction between beta-lactam antibiotics and the exocellular DD-carboxypeptidase--transpeptidase from Streptomyces R39.

The Biochemical journal ·Vol. 155 ·No. 3 ·1976-06-01 ·Pages 623-9

Fuad N, Frère JM, Ghuysen JM, Duez C, Iwatsubo M

Abstract

The exocellular DD-carboxypeptidase-transpeptidase of Streptomyces R39 is inhibited by beta-lactam antibiotics according to the same general scheme of reaction as the exocellular DD-carboxypeptidase-transpeptidase of Streptomyces R61. However, the values for the kinetic constants involved in the reaction are very different for the two enzymes and provide an explanation for the observation that the R39 enzyme is more sensitive to beta-lactam antibiotics than the R61 enzyme. Further, particular beta-lactams influence the kinetic constants to different extents depending on the source of the enzyme, so that a physical basis for the spectrum of antibiotic activity against particular enzyme systems is provided.

MeSH Terms
Carboxypeptidases/antagonists & inhibitors Cephalexin/pharmacology Cephalosporins/pharmacology Fluorescence Kinetics Muramoylpentapeptide Carboxypeptidase/antagonists & inhibitors Penicillins/pharmacology Spectrum Analysis Streptomyces/enzymology
Chemicals
Cephalosporins Penicillins Carboxypeptidases Muramoylpentapeptide Carboxypeptidase Cephalexin
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
Fuad N
Frère J M
Ghuysen J M
Duez C
Iwatsubo M
References (13)
13 references, click to expand
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Article Info
Journal
The Biochemical journal
Abbr.
Biochem J
ISSN
0264-6021
Published
1976-06-01
Pages
623-9
Language
English
Region
England
NLM ID
2984726R
PMCID
PMC1172885
Subset
IM
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