Abstract
An enzymatic activity to synthesize N-acetyl-L-glutamate, known as an essential allosteric activator of the ammonia-dependent carbamyl phosphate synthetase, from L-glutamate and acetyl-CoA was demonstrated in the extracts of rat and mouse liver mitochondria. A partially purified enzyme had a strict substrate specificity: various amino acids and acyl-CoA analogues could not substitute for the both substrates. A notable finding is that the enzyme activity was markedly stimulated by L-arginine. The effect of arginine was specific, and all other amino acids tested, including usual components of proteins and intermediates of urea cycle as well as several guanidino compounds were totally ineffective. Arginine also stimulated the acetylglutamate synthesis in intact mitochondria. The occurrence of an enzyme specific for acetylglutamate synthesis and control of its activity by arginine may provide an important regulatory mechanism for the production of carbamyl phosphate as the first step of urea biosynthesis.
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