On the Molecular Mechanism of Maize Phosphoenolpyruvate Carboxylase Activation by Thiol Compounds
- 1 August 1984
- journal article
- research article
- Published by Oxford University Press (OUP) in Plant Physiology
- Vol. 75 (4) , 983-987
- https://doi.org/10.1104/pp.75.4.983
Abstract
Incubation of purified phosphoenolpyruvate carboxylase from Zea mays L. leaves with dithiothreitol resulted in an almost 2-fold increase in the enzymic activity. The activated enzyme showed the same affinity for its substrates and the same sensitivity with respect to malate and oxalacetate inhibition. The activation induced by dithiothreitol was reversed by diamide, an oxidant of vicinal dithiols, suggesting that the redox state of disulfide bonds of the enzyme may be important in the expression of the maximal catalytic activity.This publication has 22 references indexed in Scilit:
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