title: Alpha-keto acid dehydrogenase complexes. X. Regulation of the activity of the pyruvate dehydrogenase complex from beef kidney mitochondria by phosphorylation and dephosphorylation.
abstract: This paper reports the discovery that the activity of the multienzyme pyruvate dehydrogenase complex from beef kidney mitochondria is regulated by a phosphorylation-dephosphorylation reaction sequence. The site of this regulation is the pyruvate dehydrogenase component of the complex. Phosphorylation and concomitant inactivation of pyruvate dehydrogenase are catalyzed by an ATP-specific kinase (i.e., a pyruvate dehydrogenase kinase), and dephosphorylation and concomitant reactivation are catalyzed by a phosphatase (i.e., a pyruvate dehydrogenase phosphatase). The kinase and the phosphatase appear to be regulatory subunits of the pyruvate dehydrogenase complex.
mesh_terms: D000818:Animals; D002384:Catalysis; D002417:Cattle; D007668:Kidney / Q000201:enzymology*; D008274:Magnesium; D010085:Oxidative Phosphorylation; D010744:Phosphoric Monoester Hydrolases; D010770:Phosphotransferases; D011771:Pyruvate Oxidase / Q000378:metabolism*; D014461:Ultracentrifugation
chemical_list: D011771:Pyruvate Oxidase; D010770:Phosphotransferases; D010744:Phosphoric Monoester Hydrolases; D008274:Magnesium