Plant Physiol. Drug Metab Dispos
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Plant Physiology 86:325-328 (1988)
© 1988 American Society of Plant Biologists

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Metabolism and Enzymology

A Simple and Accurate Spectrophotometric Assay for Phosphoenolpyruvate Carboxylase Activity 1

Christopher R. Meyer, Pierre Rustin2 and Randolph T. Wedding

Department of Biochemistry, University of California, Riverside, California 92521

The rate of phosphoenolpyruvate carboxylase activity measured through the conventional coupled assay with malate dehydrogenase is underestimated due to the instability of oxaloacetate, which undergoes partial decarboxylation into pyruvate in the presence of metal ions. The addition of lactate dehydrogenase to the conventional assay allows the reduction of pyruvate formed from oxaloacetate to lactate with the simultaneous oxidation of NADH. Then, the enzymic determination of substrate and products shows that the combined activities of malate dehydrogenase and lactate dehydrogenase account for all the phosphoenolpyruvate consumed. The net result of the improved assay is a higher Vmax with no apparent effect on Km. The free divalent cation concentration appears to be the major factor in the control of the rate of oxaloacetate decarboxylation.

2 Permanent address: Laboratoire de Biologie Vegetale IV (CNRS, UA 1180), Universite Pierre et Marie Curie, Paris 75005, France. Recipient of a CNAM/CAB/NATO grant.

1 Supported in part by National Science Foundation grant (DMB 85-15181).




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