Bovine Kidney Pyruvate Dehydrogenase Complex. Isolation of the Component Enzymes after Limited Proteolysis with Papain
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چکیده
منابع مشابه
Pyruvate dehydrogenase kinase activity of pig heart pyruvate dehydrogenase (E1 component of pyruvate dehydrogenase complex).
The pyruvate dehydrogenase (E1) and acetyltransferase (E2) components of pig heart and ox kidney pyruvate dehydrogenase (PDH) complex were separated and purified. The E1 component was phosphorylated (alpha-chain) and inactivated by MgATP. Phosphorylation was mainly confined to site 1. Addition of E2 accelerated phosphorylation of all three sites in E1 alpha and inactivation of E1. On the basis ...
متن کاملRapid intersite transfer of acetyl groups and movement of pyruvate dehydrogenase component in the kidney pyruvate dehydrogenase complex.
Two sites per subunit of the dihydrolipoyl transacetylase component of the kidney pyruvate dehydrogenase complex can be acetylated, and high levels of acetylation can be achieved under conditions in which only a few subunits of the pyruvate dehydrogenase component are functional (Cate, R. L., and Roche, T. E. (1979) J. Biol. Chem 254, 1659-1665). These obsewations suggest intersite transfer of ...
متن کاملSubunit structure of dihydrolipoyl transacetylase component of pyruvate dehydrogenase complex from bovine heart.
Limited tryptic digestion of dihydrolipoyl transacetylase, the core enzyme of the bovine heart pyruvate dehydrogenase complex, cleaves the transacetylase subunits (Mr =: 52,000) into two large fragments, designated the subunit-binding domain and the lipoyl domain. The subunit-binding domain has a compact structure with M, = 26,000 as determined by sedimentation equilibrium analysis, and it poss...
متن کاملEffects of alpha-ketoisovalerate on bovine heart pyruvate dehydrogenase complex and pyruvate dehydrogenase kinase.
The regulatory effects of alpha-ketoisovalerate on purified bovine heart pyruvate dehydrogenase complex and endogenous pyruvate dehydrogenase kinase were investigated. Incubation of pyruvate dehydrogenase complex with 0.125 to 10 mM alpha-ketoisovalerate caused an initial lag in enzymatic activity, followed by a more linear but inhibited rate of NADH production. Incubation with 0.0125 or 0.05 m...
متن کاملSelective proteolysis of the protein X subunit of the bovine heart pyruvate dehydrogenase complex. Effects on dihydrolipoamide dehydrogenase (E3) affinity and enzymic properties of the complex.
Selective proteolysis of the protein X subunit of native bovine heart pyruvate dehydrogenase complex may be accomplished without loss of overall complex activity. Partial loss of function occurs if Mg2+ and thiamin pyrophosphate are not present during proteinase arg C treatment as these cofactors are necessary to prevent cleavage of the E1 alpha subunit. Specific degradation of component X lead...
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ژورنال
عنوان ژورنال: European Journal of Biochemistry
سال: 1980
ISSN: 0014-2956,1432-1033
DOI: 10.1111/j.1432-1033.1980.tb04510.x