Interconversion of phospho- and dephospho- forms of pig heart pyruvate dehydrogenase.
نویسندگان
چکیده
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.
منابع مشابه
Studies of the effects of beta-adrenergic agonists on the regulation of pyruvate dehydrogenase in the perfused rat heart.
The effects of &adrenergic agonists (e.g. epinephrine and isoproterenol) on the metabolic flux through, and the activation state of the pyruvate dehydrogenase multienzyme complex, were investigated in the isolated perfused rat heart. Infusion of epinephrine caused an inhibition of pyruvate decarboxylation at low (0.1 m ~ ) pyruvate concentrations in the perfusion medium, a stimulation of flux a...
متن کاملPurification and properties of the phospho and dephospho forms of yeast NAD-dependent glutamate dehydrogenase.
متن کامل
Control by phosphorylation.
The two examples of phospho and dephospho proteins for which structural data were previously available (glycogen phosphorylase and isocitrate dehydrogenase) demonstrated two different mechanisms for control. In glycogen phosphorylase, activation by phosphorylation results in long-range allosteric changes. In isocitrate dehydrogenase, inhibition by phosphorylation is achieved by an electrostatic...
متن کاملRole of Ca2+ in pyruvate dehydrogenase interconversion in brain mitochondria and synaptosomes.
The steady-state content of active (dephospho) pyruvate dehydrogenase (PDHA) of suspensions of coupled rat brain mitochondria oxidizing succinate was found to be markedly increased with increasing free Ca2+ ion concentration of the medium, with a half-maximal effect at 10(-6.43) M Ca2+. Other ions were present in these studies at concentrations appropriate for the cytosol. Depolarization of the...
متن کاملPhosphorylation of additional sites on pyruvate dehydrogenase inhibits its re-activation by pyruvate dehydrogenase phosphate phosphatase.
The phosphorylation of sites additional to an inactivating site inhibits the formation of active pig heart pyruvate dehydrogenase complex from inactive pyruvate dehydrogenase phosphate complex by pig heart pyruvate dehydrogenase phosphate phosphatase.
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید
ثبت ناماگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید
ورودعنوان ژورنال:
- Proceedings of the National Academy of Sciences of the United States of America
دوره 65 4 شماره
صفحات -
تاریخ انتشار 1970