Abstract
The cytosolic pyruvate kinase (PK c , EC 2.7.1.40) and phosphoenolpyruvate carboxylase (PEP-Case, EC 4.1.1.31) from cotyledons of 6-d-old castor seedlings (Ricinus communis L,) have been partially purified and characterized. PK c was purified 370-fold to a specific activity of 20 μmol.min -1 .(mg protein) -1 , and was shown to exist as a 237-kDa homotetramer. In addition, PK c displayed hyperbolic substrate saturation kinetics and demonstrated pH-dependent modulation by several metabolite effectors including glutamine, glutamate, arginine, malate and 2-oxoglutarate. Most were inhibitors at pH 6.9, while activation by glutamine, asparagine and arginine and only weak inhibition for the rest were observed at pH 7.5
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