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PMID: 6984651 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

Interaction of clavulanate with the beta-lactamases of Streptomyces albus G and Actinomadura R39.

The Biochemical journal ·Vol. 207 ·No. 3 ·1982-12-01 ·Pages 429-36

Frère JM, Dormans C, Lenzini VM, Duyckaerts C

Abstract

The reactions of beta-lactamases of Actinomadura R39 and Streptomyces albus G with clavulanate proceed along branched pathways. Both enzymes perform the hydrolysis of this beta-lactam with rather high efficiencies (kcat. = 18s-1 and 52s-1 respectively). If large clavulanate/enzyme ratios are used, complete inactivation of the enzymes is observed. At lower ratios, inactivation is only partial. Irreversible inactivation occurs after 400 and 20000 turnovers for the A. R39 and S. albus G enzymes respectively. With the A. R39 beta-lactamase, a transiently inhibited complex is also formed that remains undetectable with the S. albus G beta-lactamase. Kinetic models are presented and studied for the interaction between clavulanate and both enzymes. A tentative general reaction scheme is also discussed.

MeSH Terms
Actinomycetaceae/enzymology Clavulanic Acid Clavulanic Acids/metabolism Hydrolysis Kinetics Models, Biological Streptomyces/enzymology beta-Lactamase Inhibitors
Chemicals
Clavulanic Acids beta-Lactamase Inhibitors Clavulanic Acid
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Frère J M
Dormans C
Lenzini V M
Duyckaerts C
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20 references, click to expand
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Article Info
Journal
The Biochemical journal
Abbr.
Biochem J
ISSN
0264-6021
DOI
10.1042/bj2070429
Published
1982-12-01
Pages
429-36
Language
English
Region
England
NLM ID
2984726R
PMCID
PMC1153882
Subset
IM
Grants
NIAID NIH HHS · 2 R01 AI 13364-05 · United States
External Links
PubMed source DOI: 10.1042/bj2070429 PMC Full Text View journal details
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