Oxaloglycolate reductive decarboxylase catalyzes the formation of d-glycerate from dihydroxyfumarate and TPNH or DPNH. The keto form of dihydroxyfumarate, oxaloglycolate, is presumed to be the actual substrate. The enzyme also catalyzes the formation of d-glycerate from hydroxypyruvate and of glycolate from glyoxylate; both reactions require reduced pyridine nucleotide. The enzyme has been obtained in a homogeneous state and has a molecular weight of 63,000.
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Kohn et al. (1968) studied this question.
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