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. 1980 Jun 1;187(3):797–802. doi: 10.1042/bj1870797

Kinetics of inactivation of beta-lactamase I by 6 beta-bromopenicillanic acid.

V Knott-Hunziker, B S Orlek, P G Sammes, S G Waley
PMCID: PMC1162464  PMID: 6331385

Abstract

The kinetics of the inactivation of beta-lactamase I from Bacillus cereus 569 by preparations of 6 alpha-bromopenicillanic acid showed unexpected features. These can be quantitatively accounted for on the basis of the inactivator being the epimer, 6 beta-bromopenicillanic acid. At pH 9.2, the rate-determining step in the inactivation is the formation of the inactivator. When pure 6 beta-bromopenicillanic acid is used to inactivate beta-lactamase I, simple second-order kinetics are observed. The inactivated enzyme has a new absorption peak at 326 nm. The rate constant for inactivation has the same value as the rate constant for appearance of absorption at 326 nm; the rate-determining step may thus be fission of the beta-lactam ring of 6 beta-bromopenicillanic acid. Inactivation is slower in the presence of substrate, and the observed kinetics can be quantitatively accounted for on a simple competitive model. The results strongly suggest that inactivation is a consequence of reaction at the active site.

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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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