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. 1972 Oct;129(5):1035–1047. doi: 10.1042/bj1291035

A kinetic study of baker's-yeast pyruvate kinase activated by fructose 1,6-diphosphate

Neil Macfarlane 1, Stanley Ainsworth 1
PMCID: PMC1174261  PMID: 4571175

Abstract

The paper reports a study of the kinetics of the reaction between phosphoenolpyruvate, ADP and Mg2+ catalysed by yeast pyruvate kinase when activated by fructose 1,6-diphosphate and K+. The experimental results indicate that the reaction mechanism is of the Ordered Tri Bi type with the substrates binding in the order phosphoenolpyruvate, ADP and Mg2+. Direct phosphoryl transfer takes place in the quaternary complex, with pyruvate released before MgATP. A dead-end enzyme–pyruvate complex is also indicated. Values have been determined for the Michaelis, dissociation and inhibition constants of the reaction. Several of the rate constants involved have also been evaluated.

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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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