3.5.3.6 (2S)-2-amino-5-(N''-cyanocarbamimidamido)pentanoic acid - 163506 3.5.3.6 3-aminoalanine 10 mM, 3% loss of activity. 200 mM, 28% loss of activity 153659 3.5.3.6 5,5'-dithiobis(2-nitrobenzoic acid) - 221 3.5.3.6 5,5'-dithiobis(2-nitrobenzoic acid) the reaction of 1 sulfhydryl group with 0.3 mM 5,5'-dithiobis-(2-nitrobenzoic acid) has a half-life of about 50 min at pH 8 221 3.5.3.6 6-diazo-5-oxo-norleucine - 20065 3.5.3.6 6-diazo-5-oxo-norleucine 1 mM, dextran-conjugated enzyme and native enzyme retain 10.1% and 1.5% of their initial activities 20065 3.5.3.6 Ag+ - 75 3.5.3.6 agmatine - 505 3.5.3.6 agmatine very weak, mixed-type inhibitor 505 3.5.3.6 agmatine 10 mM, 8% loss of activity. 200 mM, 28% loss of activity 505 3.5.3.6 Al3+ - 264 3.5.3.6 AlCl3 1 mM, dextran-conjugated enzyme and native enzyme retain 47% and 48% of their initial activities 1785 3.5.3.6 aminoguanidine - 1553 3.5.3.6 arcaine - 11115 3.5.3.6 ATP - 4 3.5.3.6 BaCl2 1 mM, dextran-conjugated enzyme and native enzyme retain 61.2% and 58.8% of their initial activities 1275 3.5.3.6 beta-amyloid peptide(1-28) not-containing arginine 144055 3.5.3.6 beta-amyloid peptide(1-42) containing arginine 144054 3.5.3.6 beta-amyloid peptide(22-35) not-containing arginine 144056 3.5.3.6 CaCl2 1 mM, dextran-conjugated enzyme and native enzyme retain 45.9% and 51.9% of their initial activities 218 3.5.3.6 Cd2+ 53% inhibition at 1 mM Cd2+ 52 3.5.3.6 CTP - 60 3.5.3.6 Cu2+ - 19 3.5.3.6 CuSO4 1 mM, dextran-conjugated enzyme and native enzyme retain 33% and 43.4% of their initial activities 263 3.5.3.6 D-Arg - 1349 3.5.3.6 D-arginine 10 mM, 4% loss of activity. 200 mM, 97% loss of activity 1255 3.5.3.6 DTNB 1 mM, dextran-conjugated enzyme and native enzyme retain 46.7% and 4.9% of their initial activities 554 3.5.3.6 Ethylguanidine - 16083 3.5.3.6 Fe2+ - 25 3.5.3.6 Fe3+ - 70 3.5.3.6 FeCl3 1 mM, dextran-conjugated enzyme and native enzyme retain 45% and 50% of their initial activities 702 3.5.3.6 Formamidinium ion 1 mM, irreversible inhibition within 1 min 93400 3.5.3.6 formylguanidine - 106074 3.5.3.6 gamma-guanidinobutyrate - 31815 3.5.3.6 guanidine - 2023 3.5.3.6 guanidine 10 mM, 9% loss of activity. 200 mM, 35% loss of activity 2023 3.5.3.6 H2O2 1 mM, dextran-conjugated enzyme and native enzyme retain 25.8% and 2.9% of their initial activities 22 3.5.3.6 Hg2+ - 33 3.5.3.6 HgCl2 1 mM, dextran-conjugated enzyme and native enzyme retain 40% and 13.4% of their initial activities 110 3.5.3.6 hydroxylamine - 85 3.5.3.6 hydroxylamine 1 mM, dextran-conjugated enzyme and native enzyme retain 24.5% and 2.3% of their initial activities 85 3.5.3.6 iodoacetate - 93 3.5.3.6 iodoacetate 1 mM, dextran-conjugated enzyme and native enzyme retain 23.9% and 2.6% of their initial activities 93 3.5.3.6 K2CrO4 1 mM, dextran-conjugated enzyme and native enzyme retain 42% and 36% of their initial activities 46296 3.5.3.6 KCl 1 mM, dextran-conjugated enzyme and native enzyme retain 97% and 98% of their initial activities 79 3.5.3.6 L-Alpha-amino-beta-guanidinopropionic acid competitive 20328 3.5.3.6 L-Alpha-amino-beta-guanidinopropionic acid - 20328 3.5.3.6 L-Alpha-amino-gamma-guanidinobutyric acid competitive 30112 3.5.3.6 L-alpha-aminobutyrate - 1873 3.5.3.6 L-canavanine - 1143 3.5.3.6 L-canavanine a time-controlled, competitive, mechanism-based inhibitor, the close structural similarity between L-arginine and L-canavanine suggests that an analogous pathway is responsible for the inactivation-reactivation cycle; slow substrate inhibitor that functions by covalent modification of the active-site Cys406 residue in the form of a thiouranoim salt 1143 3.5.3.6 L-canavanine two competing pathways, slow substrate inhibition or irreversible inhibition, branch at the Cys-alkylthiouronium ion intermediate: one pathway leads to direct formation of O-ureido-L-homoserine via a reactive thiouronium intermediate. The other pathway leads to an inactive form of the enzyme, a Cys-alkylisothiourea adduct, mechanism and structure, overview 1143 3.5.3.6 L-canavanine competitive; two competing pathways, slow substrate inhibition or irreversible inhibition, branch at the Cys-alkylthiouronium ion intermediate: one pathway leads to direct formation of O-ureido-L-homoserine via a reactive thiouronium intermediate. The other pathway leads to an inactive form of the enzyme, a Cys-alkylisothiourea adduct, mechanism and structure, overview 1143 3.5.3.6 L-canavanine 10 mM, 45% loss of activity. 60 mM, 99% loss of activity 1143 3.5.3.6 L-citrulline - 938 3.5.3.6 L-glutamate - 41 3.5.3.6 L-homoarginine competitive 2084 3.5.3.6 L-homoarginine - 2084 3.5.3.6 L-homoarginine 10 mM, 2% loss of activity. 200 mM, 25% loss of activity 2084 3.5.3.6 L-lysine - 134 3.5.3.6 L-norvaline noncompetitive 691 3.5.3.6 L-ornithine - 192 3.5.3.6 L-ornithine noncompetitive 192 3.5.3.6 L-ornithine 10 mM, 12% loss of activity. 200 mM, 24% loss of activity 192 3.5.3.6 L-Pro - 1089 3.5.3.6 Lys - 649 3.5.3.6 MBTH 1 mM, dextran-conjugated enzyme and native enzyme retain 20.5% and 2.6% of their initial activities 240154 3.5.3.6 Mersalyl - 1982 3.5.3.6 methylguanidine - 7235 3.5.3.6 MgCl2 1 mM, dextran-conjugated enzyme and native enzyme retain 49% and 14.3% of their initial activities 196 3.5.3.6 additional information PEG binding does not affect the enzyme activity, but does improve pharmocodynamics and pharmacokinetics 2 3.5.3.6 additional information Nomega-cyano-L-arginine does not inhibit Giardia lamblia arginine deiminase 2 3.5.3.6 additional information dextran conjugation slightly protects the reactive amino and thiols groups of surface amino acids of the enzyme from amino acids suicide inhibitors 2 3.5.3.6 N-[(1S)-1-(2-tert-butyl-2H-tetrazol-5-yl)-4-[(2-fluoroethanimidoyl)amino]butyl]benzamide preferentially inhibits protein-arginine deiminase 2 by 3fold with the highest selectivity being observed for PAD2 over PAD4. Highly selective protein-arginine deiminase 2 inhibitor relative to the other protein-arginine deiminases 238881 3.5.3.6 N-[(1S)-1-(2-tert-butyl-2H-tetrazol-5-yl)-4-[(2-fluoroethanimidoyl)amino]butyl][1,1'-biphenyl]-4-carboxamide preferentially inhibits protein-arginine deiminase 2 by 25fold with the highest selectivity being observed for PAD2 over PAD4. Highly selective protein-arginine deiminase 2 inhibitor relative to the other protein-arginine deiminases 238882 3.5.3.6 Na2WO4 1 mM, dextran-conjugated enzyme and native enzyme retain 30% and 26.9% of their initial activities 12623 3.5.3.6 NaCl 1 mM, dextran-conjugated enzyme and native enzyme retain 13% and 11% of their initial activities 42 3.5.3.6 NaIO3 1 mM, dextran-conjugated enzyme and native enzyme retain 41% and 34% of their initial activities 206465 3.5.3.6 NEM - 89 3.5.3.6 nitroguanidine - 106852 3.5.3.6 p-hydroxymercuribenzoate - 98 3.5.3.6 PCMB - 78 3.5.3.6 PEG modifiying ADI with PEG leads to reduced activity of the complex of 400 kDa MW 34904 3.5.3.6 PMSF 1 mM, dextran-conjugated enzyme and native enzyme retain 1.1% and 1.2% of their initial activities 248 3.5.3.6 Polyethylene glycol binding of 12 kDa and of 20 kDa MW inhibits the enzyme activity, but does not alter the pH-dependence of the enzyme and increases the enzyme stability during storage slightly, with PEG 12k showing the higher effect 2868 3.5.3.6 propargylglycine - 2353 3.5.3.6 putrescine - 155 3.5.3.6 putrescine 10 mM, 6% loss of activity. 200 mM, 11% loss of activity 155 3.5.3.6 S-nitroso-L-homocysteine active site directed, irreversible inhibitor 9907 3.5.3.6 Sn2+ - 413 3.5.3.6 Urea - 116 3.5.3.6 Urea 1 mM, dextran-conjugated enzyme and native enzyme retain 46.5% and 36% of their initial activities 116 3.5.3.6 Zn2+ - 14 3.5.3.6 Zn2+ at 1 mM Zn2+, the enzyme activity is inhibited by 26% 14 3.5.3.6 ZnCl2 1 mM, dextran-conjugated enzyme and native enzyme retain 12% and 10% of their initial activities 271