Enzymes that metabolize acyl-coenzyme A in the monkey--their distribution, properties and roles in an alternative pathway for the excretion of nitrogen.

1. In various tissues from the monkey (Macaca fuscata), acyl-coenzyme A (CoA) hydrolase activities were found to be widely distributed within a 2-10 times range and present in liver cytosol having mol. wt of ca 60,000. 2. Acyl-CoA: amino acid N-acyltransferase activity were 4-250 times higher in liver and kidney than in other tissues, even no activity in heart, lung, and plasma. 3. The transferases abounded in liver mitochondria, being distributed evenly between the intracristate space, the inner membrane, and the matrix. 4. The partially purified transferases with benzoyl-CoA or phenylacetyl-CoA as substrates were shown to have mol. wt of ca 30,000 and reacted only with glycine or L-glutamine, respectively. 5. No amino acid tested had any effects on the enzyme as either inhibitors or activators. 6. These results suggest that the enzymes that metabolize acyl-CoA constitute an alternative pathway for the excretion of nitrogen.