Branched chain alpha-keto acid dehydrogenase in tissues from rainbow trout (Salmo gairdnerii).
Mitochondria isolated from skeletal red muscle of rainbow trout (Salmo gairdnerii) have remarkably high activity of branched chain alpha-keto acid dehydrogenase as measured with alpha-keto isocaproic acid as substrate. The activity of the dehydrogenase increases several-fold after preincubation of the mitochondria with an uncouple and oligomycin. The accumulation of the first product, isovaleryl-CoA is strongly stimulated by high concentrations of CoASH. In the crude mitochondrial lysates we have used, an unknown compound accumulates with time, during incubation with alpha-keto isocaproic acid, CoASH and NAD. The compound, probably a CoA derivative, is more hydrophobic than isovaleryl-CoA.
D042942:3-Methyl-2-Oxobutanoate Dehydrogenase (Lipoamide); D000818:Animals; D007658:Ketone Oxidoreductases / Q000378:metabolism*; D007668:Kidney / Q000201:enzymology*; D007700:Kinetics; D008928:Mitochondria / Q000201:enzymology*; D008930:Mitochondria, Liver / Q000378:metabolism*; D008931:Mitochondria, Muscle / Q000201:enzymology*; D009097:Multienzyme Complexes / Q000378:metabolism*; D009928:Organ Specificity; D014337:Trout
D009097:Multienzyme Complexes; D007658:Ketone Oxidoreductases; D042942:3-Methyl-2-Oxobutanoate Dehydrogenase (Lipoamide)