Multi-site phosphorylation of branched-chain 2-oxoacid dehydrogenase complex within mitochondria isolated from rat liver, kidney and heart.
The alpha subunit of the E1 component of branched-chain 2-oxoacid dehydrogenase complex becomes rapidly phosphorylated in rat liver, kidney and heart mitochondria incubated in the presence of succinate and [32P]phosphate. Peptide mapping of tryptic digests of the phosphorylated alpha subunit indicates that 3 distinct sites are phosphorylated, as has been reported previously by us for phosphorylation in vitro of highly purified complex.
D042942:3-Methyl-2-Oxobutanoate Dehydrogenase (Lipoamide); D000818:Animals; D002417:Cattle; D007658:Ketone Oxidoreductases / Q000302:isolation & purification / Q000378:metabolism*; D007668:Kidney / Q000201:enzymology*; D008928:Mitochondria / Q000201:enzymology*; D008929:Mitochondria, Heart / Q000201:enzymology*; D008930:Mitochondria, Liver / Q000201:enzymology*; D008970:Molecular Weight; D009097:Multienzyme Complexes / Q000302:isolation & purification / Q000378:metabolism*; D010761:Phosphorus Radioisotopes; D010766:Phosphorylation; D051381:Rats; D011919:Rats, Inbred Strains
D009097:Multienzyme Complexes; D010761:Phosphorus Radioisotopes; D007658:Ketone Oxidoreductases; D042942:3-Methyl-2-Oxobutanoate Dehydrogenase (Lipoamide)