The relationship between the rate of glutamate deamination and long-chain acyl-CoA accumulation in kidney cortex mitochondria of rabbit.
The effect of long-chain acyl-CoA on glutamate dehydrogenase activity was studied in uncoupled rabbit kidney cortex mitochondria incubated with glutamate and palmitoylcarnitine in the presence of arsenite. The mitochondrial long-chain acyl-CoA (about 2 nmol/mg of protein) accumulated in the presence of arsenite resulted in an inhibition of ammonia production from 4.1 to 1.2 nmol/min per mg of protein. Leucine and ADP, activators of glutamate dehydrogenase, did not release the inhibitory effect of long-chain acyl-CoA on glutamate deamination. In view of the presented data it seems that inhibitory effect of long-chain acyl-CoA on glutamate dehydrogenase activity may have a physiological significance.
D000214:Acyl Coenzyme A / Q000378:metabolism*; D000641:Ammonia / Q000378:metabolism; D000818:Animals; D001151:Arsenic / Q000494:pharmacology; D018053:Arsenites; D005969:Glutamate Dehydrogenase / Q000378:metabolism*; D005971:Glutamates / Q000378:metabolism*; D007672:Kidney Cortex / Q000378:metabolism*; D007700:Kinetics; D008297:Male; D008928:Mitochondria / Q000187:drug effects / Q000378:metabolism*; D010171:Palmitoyl Coenzyme A / Q000494:pharmacology; D011817:Rabbits
D000214:Acyl Coenzyme A; D018053:Arsenites; D005971:Glutamates; D010171:Palmitoyl Coenzyme A; D000641:Ammonia; D005969:Glutamate Dehydrogenase; C015001:arsenite; D001151:Arsenic