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. 1991 Oct 1;279(Pt 1):111–114.

Interaction of beta-lactamases I and II from Bacillus cereus with semisynthetic cephamycins. Kinetic studies.

J Martin Villacorta 1, P Arriaga 1, J Laynez 1, M Menendez 1
PMCID: PMC1151553  PMID: 1930129

Abstract

The influence of C-6 alpha- or C-7 alpha-methoxylation of the beta-lactam ring in the catalytic action of class A and B beta-lactamases has been investigated. For this purpose the kinetic behaviour of beta-lactamases I (class A) and II (class B) from Bacillus cereus was analysed by using several cephamycins, moxalactam, temocillin and related antibiotics. These compounds behaved as poor substrates for beta-lactamase II, with high Km values and very low catalytic efficiencies. In the case of beta-lactamase I, the substitution of a methoxy group for a H atom at C-7 alpha or C-6 alpha decreased the affinity of the substrates for the enzyme. Furthermore, the acylation of cephamycins was completely blocked, whereas that of penicillins was slowed down by a factor of 10(4)-10(5), acylation being the rate-determining step of the process.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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