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The kinetic mechanism of yeast phosphoenolpyruvate carboxykinase

descriptionPublicationkeyboard_double_arrow_right Article 01 Jan 1993Publisher:Elsevier BVJournal:Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, volume 1,161, pages 85-90 (issn: 0167-4838,

Authors: Ana María Jabalquinto; Emilio Cardemil;

doi: 10.1016/0167-4838(93)90200-b

pmid: 8422423

The kinetic mechanism of yeast phosphoenolpyruvate carboxykinase

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Abstract

The kinetic mechanism of yeast phosphoenolpyruvate carboxykinase, in the physiological direction, has been determined. Product inhibition using KHCO3 showed competitive inhibition, when both oxalacetate (OAA) and ATP were varied. Phosphoenolpyruvate showed noncompetitive inhibition against OAA, and competitive inhibition with respect to ATP. Conversely, ADP showed competitive inhibition against OAA and noncompetitive inhibition vs. ATP. Dead-end inhibition studies with beta-sulfopyruvate showed competitive inhibition against OAA and noncompetitive inhibition vs. ATP. Ethene-ATP exhibited competitive inhibition against ATP and noncompetitive inhibition with respect to OAA. These results are consistent with a random Bi-Ter mechanism with the formation of two abortive complexes: enzyme-ATP-ADP and enzyme-OAA-PEP.

Related Organizations

University of Santiago Chile
Chile

Keywords

Adenosine Diphosphate, Kinetics, Adenosine Triphosphate, Oxaloacetates, Phosphoenolpyruvate Carboxykinase (GTP), Saccharomyces cerevisiae, Binding, Competitive

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β-sulfopyruvate: Chemical and enzymatic syntheses and enzymatic assay
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Phosphoenolpyruvate carboxykinase (ATP)
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