Regulation of activity and synthesis of N-acetylglutamate synthase from Saccharomyces cerevisiae.
Feedback inhibition of N-acetylgutamate synthase in a particulate fraction from Saccharomyces cerevisiae by L-arginine was synergistically enhanced by N-actylglutamate, whereas coenzyme A let to an additive enhancement of arginine inhibition. N-acetylglutamate synthase was not inhibited by polyamines, nor was the enzyme inactivated by incubation in the presence of coenzyme A and zinc ions. Evidence was obtained for the involvement of at least three different regulatory mechanisms in the expression of N-acetylglutamate synthase: arginine-specific repression, glucose repression and general amino acid control. The combined action of these control mechanisms led to a 90-fold variation in the specific activity of the enzyme.
D000105:Acetyl Coenzyme A; D000123:Acetyltransferases / Q000096:biosynthesis / Q000378:metabolism*; D000596:Amino Acids / Q000378:metabolism; D001120:Arginine / Q000494:pharmacology; D002474:Cell-Free System; D003065:Coenzyme A / Q000494:pharmacology*; D004357:Drug Synergism; D004794:Enzyme Repression; D005947:Glucose / Q000378:metabolism; D005971:Glutamates / Q000494:pharmacology; D009952:Ornithine; D012441:Saccharomyces cerevisiae / Q000201:enzymology* / Q000378:metabolism; D013237:Stereoisomerism; D013439:Sulfhydryl Reagents / Q000494:pharmacology
D000596:Amino Acids; D005971:Glutamates; D013439:Sulfhydryl Reagents; D000105:Acetyl Coenzyme A; D001120:Arginine; D009952:Ornithine; D000123:Acetyltransferases; D005947:Glucose; D003065:Coenzyme A