2.7.2.8	2-oxoglutarate	complete inhibition at 0.5 mM	34	
2.7.2.8	ADP	-	13	
2.7.2.8	ADP	inhibitor of complex formation with PII protein	13	
2.7.2.8	arginine	feedback regulation of enzyme and N-acetylglutamate synthase is mutually interdependent, enzymes form a complex	532	
2.7.2.8	arginine	pH-optimum for inhibition is 7.5	532	
2.7.2.8	arginine	allosteric enzyme which is inhibited by arginine	532	
2.7.2.8	arginine	enzyme has no allosteric properties and its activity is influenced neither by arginine nor by any of the intermediates of the arginine biosynthetic pathway	532	
2.7.2.8	arginine	feedback inhibition is markedly dependent on pH, above pH 9 no inhibition	532	
2.7.2.8	arginine	1 mM, 96% inhibition	532	
2.7.2.8	arginine	feedback inhibition	532	
2.7.2.8	arginine	-	532	
2.7.2.8	ATP	-	4	
2.7.2.8	L-arginine	pH and temperature dependent, sigmoidal dependence on concentration of arginine, Hill coefficient of 4, 1 mM, 37°C, 95% inhibition	123	
2.7.2.8	L-arginine	only for N-acetylglutamate synthase activity	123	
2.7.2.8	L-arginine	less inhibitory in the presence of the PII protein	123	
2.7.2.8	L-arginine	sigmoidal arginine inhibition kinetics, feedback inhibition, indentification of the N-terminal arginine site, mutational analysis, the mobile alphaH-beta16 loop of the arginine site is the modulatory signal receiver, overview	123	
2.7.2.8	L-arginine	-	123	
2.7.2.8	L-arginine	complete inhibition at 3-5 mM, PII-mediated relief from L-arginine inhibition is antagonized by 2-oxoglutarate	123	
2.7.2.8	L-arginine	complete inhibition at 0.1-1.0 mM, PII-mediated relief from L-arginine inhibition is antagonized by 2-oxoglutarate	123	
2.7.2.8	L-arginine	an allosteric inhibitor of mmNAGS/K, mechanism of allosteric inhibition of mmNAGS/K by L-arginine. L-Arginine is an allosteric inhibitor of NAGS/K but an allosteric activator of mammalian NAGS. In contrast to the structure of mmNAGS/K in the absence of L-arginine where there are conformational differences between the four subunits in the asymmetric unit, all four subunits in the L-arginine liganded structure have very similar conformations. In this conformation, the AcCoA binding site in the N-acetyltransferase domain is blocked by a loop from the amino acid kinase domain, as a result of a domain rotation that occurs when L-arginine binds	123	
2.7.2.8	L-arginine	feedback inhibition. SYPA5-5 N-acetylglutamate kinase feedback inhibition by L-arginine can be deregulated by introducing point mutations, H268N or R209A	123	
2.7.2.8	L-arginine	feedback inhibition, almost complete inhibition at 10 mM	123	
2.7.2.8	L-arginine	wild type enzyme activity drastically decreases by addition of 0.2 mM L-Arg, and consequently decreases when L-Arg concentration is increased, indicating that the enzyme activity is subject to feedback inhibition by L-Arg. Enzyme activity is almost lost in the presence of 1.0 mM L-Arg	123	
2.7.2.8	L-arginine methyl ester	1 mM, 80% inhibition	6543	
2.7.2.8	L-canavanine	-	1143	
2.7.2.8	L-citrulline	-	938	
2.7.2.8	MgCl2	inhibition above 20 mM	196	
2.7.2.8	MgCl2	30 mM, slight inhibition	196	
2.7.2.8	additional information	not inhibitory: D-arginine, agmatine, citrulline, L-canavanine, L-lysine, L-ornithine, guanidinium ions, urea at 1 mM, 37°C	2	
2.7.2.8	additional information	the enzyme is L-arginine-insensitive	2	
2.7.2.8	trichloroacetic acid	complete inactivation at 30%	48176