Wieland O, Siess E
Proc Natl Acad Sci U S A. 1970 Apr;65(4):947-54. doi: 10.1073/pnas.65.4.947.
Pyruvate dehydrogenase from pig heart exists in active and inactive forms. Interconversion from the active (dephospho) form into the inactive (phospho) form is catalyzed by an ATP-dependent kinase. Conversely the enzyme is reactivated by a phosphatase which removes the phosphate group from the protein. By gradient centrifugation pyruvate dehydrogenase was prepared free of phosphatase but still containing the kinase. Reactivation of pyruvate dehydrogenase is stimulated by adenosine 3',5'-cyclic phosphate. There is incorporation of (32)P from gamma-(32)P-ATP into the protein fraction containing the phosphatase and this phosphorylation reaction is also stimulated by adenosine 3',5'-cyclic phosphate. The participation of this phosphate in the pyruvate dehydrogenase interconversion system suggests that, in heart muscle, pyruvate oxidation may be under hormonal control by a mechanism similar to that involved in the regulation of glycogen synthesis and breakdown.
猪心丙酮酸脱氢酶存在活性和非活性两种形式。从活性（去磷酸化）形式到非活性（磷酸化）形式的相互转化由一种依赖ATP的激酶催化。相反，该酶可被一种磷酸酶重新激活，该磷酸酶能从蛋白质上去除磷酸基团。通过梯度离心制备了不含磷酸酶但仍含有激酶的丙酮酸脱氢酶。3',5'-环磷酸腺苷可刺激丙酮酸脱氢酶的重新激活。γ-(32)P-ATP中的(32)P会掺入到含有磷酸酶的蛋白质组分中，并且这种磷酸化反应也受到3',5'-环磷酸腺苷的刺激。这种磷酸在丙酮酸脱氢酶相互转化系统中的参与表明，在心肌中，丙酮酸氧化可能受激素控制，其机制类似于参与糖原合成与分解调节的机制。
