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Proteolytic modification of pig and rat liver pyruvate kinase type l ec 2.7.1.40 including phosphorylatable site



Proteolytic modification of pig and rat liver pyruvate kinase type l ec 2.7.1.40 including phosphorylatable site



Biochimica et Biophysica Acta 532(2): 259-267



The phosphorylated or phosphate-accepting site of pyruvate kinase [EC 2.7.1.40] from pig and rat liver was removed without inactivation by incubation with subtilisin. At different time intervals the subtilisin was inactivated with phenylmethylsulfonyl fluoride and the amount of remaining phosphorylatable or phosphorylated sites of pyruvate kinase estimated by incubation with an excess of [32P]-ATP and protein kinase. To get the same rate of modification the subtilisin concentration required to modify unphosphorylated pyruvate kinase was approximately 10 times higher than that used for removal of the phosphorylated site of phosphorylated enzyme. The proteolytically-modified pyruvate kinase had an increased apparent Km for phosphoenolpyruvate without a change in V, when compared to unmodified unphosphorylated and phosphorylated pyruvate kinase. The removal of the phosphorylated site was not associated with loss of the allosteric sites for ATP and fructose-1,6-diphosphate. The possibility that phosphorylation of the pyruvate kinase increases its degradation rate in vivo is briefly discussed.

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Accession: 006215008

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