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Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1976 Apr;73(4):1048–1052. doi: 10.1073/pnas.73.4.1048

Acquisition of substrate-specific parameters during the catalytic reaction of penicillinase.

N Citri, A Samuni, N Zyk
PMCID: PMC430197  PMID: 817286

Abstract

The progress of the catalytic reaction of penicillinase (EC 3.5.2.6; penicillin amido-beta-lactamhydrolase) depends on the structure of the side-chain in derivatives of 6-aminopenicillanic acid (the parent substrate). Side-chains of one class promote the rate of the reaction and cause no deviation from the linear kinetics observed with the parent compound. By contrast, side-chains of the other class induce a time-dependent, reversible change in the parameters of the catalytic reaction. The rate decelerates considerably and then becomes constant; the decrease in kcat is accompanied by a corresponding decrease in Km. The initial parameters of the biphasic reaction, determined by stopped-flow spectrophotometry, approach those of the unsubstituted 6-aminopenicillanic acid. The final parameters, which are specific for each derivative, are not acquired when the native conformation of the enzyme is stabilized by homologous antibodies.

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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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