Multi-site phosphorylation of bovine kidney branched-chain 2-oxoacid dehydrogenase complex.
The alpha-subunit of the E1 component of branched-chain 2-oxoacid dehydrogenase is phosphorylated at 3 sites by an endogenous kinase. Inactivation of the complex correlates with rapid phosphorylation of one of these sites. The similarities with the covalent regulation of pyruvate dehydrogenase complex are discussed.
D042942:3-Methyl-2-Oxobutanoate Dehydrogenase (Lipoamide); D000818:Animals; D001665:Binding Sites; D002417:Cattle; D007658:Ketone Oxidoreductases / Q000037:antagonists & inhibitors / Q000302:isolation & purification*; D007672:Kidney Cortex / Q000201:enzymology*; D009097:Multienzyme Complexes / Q000037:antagonists & inhibitors / Q000302:isolation & purification*; D010766:Phosphorylation; D011494:Protein Kinases / Q000378:metabolism
D009097:Multienzyme Complexes; D007658:Ketone Oxidoreductases; D042942:3-Methyl-2-Oxobutanoate Dehydrogenase (Lipoamide); D011494:Protein Kinases; C035627:(3-methyl-2-oxobutanoate dehydrogenase (lipoamide)) kinase