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. 1974 Jun;139(3):499–508. doi: 10.1042/bj1390499

A kinetic study of pig liver pyruvate kinase activated by fructose diphosphate

Neil Macfarlane 1, Stanley Ainsworth 1
PMCID: PMC1166314  PMID: 4850216

Abstract

The paper reports a study of the reaction between phosphoenolpyruvate, ADP and Mg2+ catalysed by pig liver pyruvate kinase when activated by fructose diphosphate and K+. The experimental results are consistent with two non-sequential mechanisms in which the substrates and products of the reaction are phosphoenolpyruvate, ADP, Mg2+, pyruvate and MgATP. Pyruvate release occurs before ADP binding. Two Mg2+ ions are involved, though the two Mg2+-binding sites cannot be occupied simultaneously. An isomerized enzyme complex forms before release of MgATP. Values were determined for the Michaelis constants of the reaction. Apparent MgATP inhibition constants are also given.

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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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