Pyruvate kinase catalyzed phosphorylation of glycolate

Rabbit muscle pyruvate kinase has been found to catalyze the phosphorylation of the hydroxyl group of glycolate by ATP. The products were characterized as P-glycolate and ADP by NMR spectroscopy and chromatography respectively. The maximal velocity is of the same order of magnitude as that for the phosphorylation of pyruvate, the “normal” reverse reaction of this enzyme. The apparent K M for glycolate is 2.3 mM and the reaction is apparently analogous to the other known side reactions of this enzyme. The product might be produced in any system with a moderate level of pyruvate kinase and low phosphatase activity.