2.3.1.1 1,3-diaminopropane 10 mM, 88% inhibition in the presence of 0.5 mM N-acetyl-L-glutamate 721 2.3.1.1 3-methylcrotonyl-CoA about 45% residual activity at 2.5 mM 2935 2.3.1.1 5,5'-dithiobis(2-nitrobenzoate) strong inhibition 303 2.3.1.1 acetyl-CoA substrate inhibition 29 2.3.1.1 acetyl-CoA - 29 2.3.1.1 AgNO3 0.1 mM, 70-90% inhibition 360 2.3.1.1 Arg activates 367 2.3.1.1 arginine 0.02 mM, 50% inhibition; L-arginine 532 2.3.1.1 arginine feed back inhibition, 0.16 mM, 50% inhibition; L-arginine 532 2.3.1.1 arginine 0.2 mM, 73% inhibition, 97% inhibition in the presence of 0.5 mM N-acetyl-L-glutamate 532 2.3.1.1 arginine - 532 2.3.1.1 arginine the arginine binding site is localized in the kinase domain. Arginine is an allosteric inhibitor of microbial NAGS as part of feedback regulation of arginine biosynthesis, arginine is also an inhibitor of plant NAGS, a partial inhibitor of fish NAGS, but an allosteric activator of mammalian NAGS 532 2.3.1.1 arginine 10 mM, 90% inhibition for wild-type enzyme and mutations affecting the putative arginine site, about 70-80% inhibition for mutations affecting the GCN5-related N-acetyltransferase domain, 98% inhibition for mutant E352D 532 2.3.1.1 BaCl2 1 mM, 30-50% inhibition 1275 2.3.1.1 butyryl-CoA about 30% residual activity at 2.5 mM 270 2.3.1.1 CaCl2 1 mM, 30-50% inhibition 218 2.3.1.1 cadaverine 10 mM, 80% inhibition in the presence of 0.5 mM N-acetyl-L-glutamate 533 2.3.1.1 Cd2+ 0.1 mM, 94% inhibition 52 2.3.1.1 CoA 50% activity reduction at 2.5 mM 18 2.3.1.1 CoCl2 0.1 mM, 30-50% inhibition 414 2.3.1.1 coenzyme A 2.5 mM, 50% inhibition 534 2.3.1.1 coenzyme A 1 mM, 20% inhibition 534 2.3.1.1 coenzyme A - 534 2.3.1.1 coenzyme A 1 mM, 30% inhibition 534 2.3.1.1 Cu2+ CuSO4, 0.1 mM, 70-90% inhibition 19 2.3.1.1 Cu2+ 0.1 mM, 68% inhibition 19 2.3.1.1 EDTA weak inhibition 21 2.3.1.1 FeCl3 0.1 mM, 30-50% inhibition 702 2.3.1.1 FeSO4 0.1 mM, 30-50% inhibition 655 2.3.1.1 glutaryl-CoA about 50% residual activity at 2.5 mM 656 2.3.1.1 Hg2+ Hg(CHCOO)2, 0.1 mM, 70-90% inhibition 33 2.3.1.1 Hg2+ 0.1 mM; 50% inhibition 33 2.3.1.1 high ionic strength - 3693 2.3.1.1 isobutylmethylxanthine and other oxypurines containing a 2,6-dione group interfere with the binding of glutamate to the active site of N-acetylglutamate synthetase, thereby decreasing synthesis of N-acetylglutamate, resulting in reduction of citrulline and urea synthesis. Isobutylmethylxanthine significantly increases the apparent Km for glutamate and decreases velocity of N-acetylglutamate synthetase, with little effect on carbamoylphosphate synthase-1. Inhibition is reversed by supplementation with N-carbamylglutamate 7213 2.3.1.1 isobutyryl-CoA about 45% residual activity at 2.5 mM 842 2.3.1.1 isovaleryl-CoA about 50% residual activity at 2.5 mM 784 2.3.1.1 K2SO4 - 2560 2.3.1.1 KCl 100 mM, 30% inhibition, 200 mM, 50% inhibition 79 2.3.1.1 KCl 100 mM, 36% inhibition after 1 h, 300 mM, 74% inhibition after 1 h, 500 mM, 87% inhibition after 1 h 79 2.3.1.1 L-alpha-Acetoxylglutamate 2 mM, 17% inhibition 93790 2.3.1.1 L-arginine 0.1 mM, 50% inhibition 123 2.3.1.1 L-arginine feedback inhibition, regulatory function, 50% inhibition at 0.026 mM, complete inhibition at 0.5 mM, negatively cooperative binding 123 2.3.1.1 L-arginine - 123 2.3.1.1 L-arginine allosteric inhibition 123 2.3.1.1 L-arginine 50% activity reduction at 2 mM 123 2.3.1.1 L-arginine partially inhibited by L-arginin 123 2.3.1.1 L-arginine L-arginine does not act as an allosteric inhibitor 123 2.3.1.1 L-arginine 1 mM, complete inhibition 123 2.3.1.1 L-citrulline 10 mM, 75% inhibition 938 2.3.1.1 L-glutamate - 41 2.3.1.1 L-glutamine substrate inhibition 102 2.3.1.1 L-Indospicine 0.2 mM; 50% inhibition 44317 2.3.1.1 methylmalonyl-CoA about 40% residual activity at 2.5 mM 790 2.3.1.1 MgCl2 1 mM, 30-50% inhibition 196 2.3.1.1 MnCl2 0.1 mM, 30-50% inhibition 307 2.3.1.1 additional information not inhibitory: N-acetyl-L-ornithine, L-ornithine, L-citrulline 2 2.3.1.1 additional information no inhibition by other proteinogenic L-amino acids 2 2.3.1.1 N-acetyl-D-glutamate 2 mM, 30% inhibition 44466 2.3.1.1 N-acetyl-DL-alpha-aminoadipate 2 mM, 78% inhibition 111329 2.3.1.1 N-acetyl-L-aspartate 2 mM, 25% inhibition 2276 2.3.1.1 N-acetyl-L-glutamate - 543 2.3.1.1 N-acetyl-L-glutamate 50% activity reduction at 25 mM 543 2.3.1.1 N-acetyl-L-glutamine 2 mM, 46% inhibition 5188 2.3.1.1 N-acetylglutamate - 3480 2.3.1.1 N-acetylglutamate 2 mM, 88% inhibition 3480 2.3.1.1 N-acetylglutamate 25 mM, 50% inhibition 3480 2.3.1.1 N-benzoyl-L-glutamate 2 mM, 29% inhibition 7244 2.3.1.1 N-Butyryl-L-glutamate 2 mM, 19% inhibition 30227 2.3.1.1 N-carbamoyl-L-glutamate 2 mM, 31% inhibition 44500 2.3.1.1 N-ethylmaleimide - 49 2.3.1.1 N-propionyl-L-glutamate 2 mM, 63% inhibition 30250 2.3.1.1 NaCl 200 mM NaCl inhibits the activity by about 22% 42 2.3.1.1 Ni(NO3)2 0.1 mM, 30-50% inhibition 94490 2.3.1.1 O-(L-Norvalyl-5)-isourea 0.02 mM, 50% inhibition 94516 2.3.1.1 oxaloacetate 1 mM, 68% inhibition 57 2.3.1.1 p-chloromercuribenzoate - 43 2.3.1.1 p-hydroxymercuribenzoate strong inhibition 98 2.3.1.1 p-hydroxymercuribenzoate - 98 2.3.1.1 Pb(NO3)2 0.1 mM, 70-90% inhibition 5596 2.3.1.1 polyamines - 2048 2.3.1.1 potassium phosphate - 1510 2.3.1.1 propionyl-CoA - 350 2.3.1.1 propionyl-CoA about 20% residual activity at 2.5 mM 350 2.3.1.1 putrescine 10 mM, 74% inhibition in the presence of 0.5 mM N-acetyl-L-glutamate 155 2.3.1.1 Sodium acetate 100 mM NaCl inhibits the activity by about 22% 1803 2.3.1.1 spermidine 1 mM, 78% inhibition in the presence of 0.5 mM N-acetyl-L-glutamate 148 2.3.1.1 spermine 1 mM, 88% inhibition in the presence of 0.5 mM N-acetyl-L-glutamate 197 2.3.1.1 succinate 2 mM, 21% inhibition 58 2.3.1.1 succinyl-CoA about 60% residual activity at 2.5 mM 224 2.3.1.1 uric acid significantly increases the apparent Km for glutamate and decreases velocity of N-acetylglutamate synthetase, with little effect on carbamoylphosphate synthase-1. Inhibition is reversed by supplementation with N-carbamylglutamate 1421 2.3.1.1 xanthine significantly increases the apparent Km for glutamate and decreases velocity of N-acetylglutamate synthetase, with little effect on carbamoylphosphate synthase-1. Inhibition is reversed by supplementation with N-carbamylglutamate 234 2.3.1.1 Zn2+ ZnCl2, 0.1 mM, 70-90% inhibition 14 2.3.1.1 Zn2+ 0.1 mM, 43% inhibition 14