2.7.3.3 (2S)-2-[[2-[[(2R)-2-[(2-phenoxyacetyl)amino]-3-phenylpropanoyl]amino]acetyl]amino]propanoic acid ZINC12654467, probably competitive inhibitor identified by in silico screening 256841 2.7.3.3 2-oxoglutarate the enzyme activity is inhibited by 10 mM 2-oxoglutarate 34 2.7.3.3 2-oxoglutarate the enzyme activity is inhibited at 10-200 mM 34 2.7.3.3 4-[[4-(1,3-benzodioxol-5-ylmethyl)piperazin-1-yl]methyl]-6,8-dimethyl-chromen-2-one ZINC20412486, probably competitive inhibitor identified by in silico screening 255670 2.7.3.3 5,5'-dithiobis(2-nitrobenzoic acid) - 221 2.7.3.3 5,5'-dithiobis-(2-nitrobenzoic acid) modification and inactivation course with DTNB and the reactivation course of DTNB-modified enzyme. Modified enzyme can be reactivated by an excess concentration of dithiothreitol in a monophasic kinetic course 2053 2.7.3.3 5,5'-dithiobis-2-nitrobenzoic acid - 5368 2.7.3.3 5,7-dihydroxy-2-phenyl-6,8-bis(1-piperidylmethyl)chromen-4-one i.e. ZINC08836734, probably competitive inhibitor identified by in silico screening 255688 2.7.3.3 Ag+ dose-dependent, reversible, non-competitive inhibition, complete inhibition at 0.1 mM Ag+ 75 2.7.3.3 agmatine 5fold higher concentration than L-Arg, 20% inhibition 505 2.7.3.3 agmatine 10 mM, 79.3% inhibition 505 2.7.3.3 agmatine 65% inhibition at 2 mM 505 2.7.3.3 agmatine 61% enzyme inhibition at 2 mM 505 2.7.3.3 aminoguanidine 10 mM, 2.6% inhibition 1553 2.7.3.3 apoferritin mixed inhibition 256837 2.7.3.3 apoferritin-Ag nanoparticle interaction with arginine kinase leads to more than 70% reduction in the enzyme activity, mixed inhibition 256838 2.7.3.3 apoferritin-Au nanoparticle interaction with arginine kinase leads to more than 70% reduction in the enzyme activity, mixed inhibition 256839 2.7.3.3 apoferritin-Pt nanoparticle interaction with arginine kinase leads to more than 70% reduction in the enzyme activity, mixed inhibition 256840 2.7.3.3 aspartate 0.02-0.15 mM, causes inactivation and unfolding of arginine kinase 724 2.7.3.3 ATP product inhibition, competitive with ADP, noncompetitive with L-Arg 4 2.7.3.3 ATP the enzyme is inhibited by 200 mM ATP 4 2.7.3.3 ATP the enzyme activity is inhibited at 100 mM 4 2.7.3.3 Borate - 1395 2.7.3.3 Ca2+ - 15 2.7.3.3 canavanine 5fold higher concentration than L-Arg, 50% inhibition 3332 2.7.3.3 canavanine 10 mM, 54.6% inhibition 3332 2.7.3.3 canavanine 81% inhibition at 2 mM 3332 2.7.3.3 canavanine 79% enzyme inhibition at 2 mM 3332 2.7.3.3 chloride 9% inhibition at 50 mM 298 2.7.3.3 chloride 7% inhibition at 50 mM 298 2.7.3.3 chloride 50 mM, 7% inhibition 298 2.7.3.3 citrulline 17% inhibition at 2 mM 1464 2.7.3.3 citrulline 21% enzyme inhibition at 2 mM 1464 2.7.3.3 Cl- - 141 2.7.3.3 Creatine 10 mM, 12.7% inhibition 433 2.7.3.3 Creatine 11% inhibition at 2 mM 433 2.7.3.3 Creatine 9% enzyme inhibition at 2 mM 433 2.7.3.3 Cu2+ - 19 2.7.3.3 Cu2+ strong inhibition 19 2.7.3.3 D-Arg product inhibition, competitive with arginine phosphate and noncompetitive withg ADP 1349 2.7.3.3 D-Arg competitive to L-arginine 1349 2.7.3.3 D-arginine competitive 1255 2.7.3.3 D-glucose the enzyme is inhibited by 50 mM D-glucose, almost all arginine kinase activity is lost after treatment with 200 mM D-glucose 35 2.7.3.3 dithiothreitol conformational change and inactivation 45 2.7.3.3 DTNB the arginine kinase modified by DTNB can be fully reactivated by dithiothreitol in a monophasic kinetic course. This reactivation can be slowed down in the presence of ATP, suggesting that the essential Cys is located near the ATP binding site 554 2.7.3.3 Ethylguanidine 5fold higher concentration than L-Arg, 22% inhibition 16083 2.7.3.3 Fe2+ - 25 2.7.3.3 glutamate 15% inhibition at 2 mM 297 2.7.3.3 glutamate 21% enzyme inhibition at 2 mM 297 2.7.3.3 glycine 10% inhibition at 2 mM 72 2.7.3.3 glycine 15% enzyme inhibition at 2 mM 72 2.7.3.3 guanidine 10% inhibition at 2 mM 2023 2.7.3.3 guanidine 12% enzyme inhibition at 2 mM 2023 2.7.3.3 guanidine butyrate 10 mM, 4.3% inhibition 127456 2.7.3.3 guanidine hydrochloride 0.2 mM, about 90% loss of activity 1048 2.7.3.3 guanidine hydrochloride 1 mM 1048 2.7.3.3 His 5fold higher concentration than L-Arg, 50% inhibition 1062 2.7.3.3 homoarginine 10 mM, 38.2% inhibition 4255 2.7.3.3 Iodide 13% inhibition at 50 mM 636 2.7.3.3 Iodide 3% inhibition at 50 mM 636 2.7.3.3 Iodide 50 mM, 3% inhibition 636 2.7.3.3 iodoacetamide - 67 2.7.3.3 isoleucine 10% inhibition at 2 mM 1028 2.7.3.3 isoleucine 9% enzyme inhibition at 2 mM 1028 2.7.3.3 K+ 200 mM, 50% inhibition 39 2.7.3.3 L-arginine - 123 2.7.3.3 L-arginine arginine kinase AK3 shows substrate inhibition. Residue S79 is essential for this phenomenon 123 2.7.3.3 L-arginine after primary arginine substrate binding (ES complex formation), the binding of another arginine at the secondarily induced inhibitory site is accelerated to form the SES complex, causing substrate inhibition. S79 and V81 in the Paramecium AK3 are the key residues involved in substrate inhibition 123 2.7.3.3 L-arginine methyl ester competitive to L-Arg 6543 2.7.3.3 L-Asp 5fold higher concentration than L-Arg, 25% inhibition 294 2.7.3.3 L-canavanine competitive to L-Arg 1143 2.7.3.3 L-canavanine - 1143 2.7.3.3 L-Glu 5fold higher concentration than L-Arg, 31% inhibition 202 2.7.3.3 L-Glucose AK-1 activity does not show significant variation after supplementation with 10 mM L-glucose. However, AK-1 activity decreases significantly when L-glucose concentration is higher than 50 mM and almost all MrAK-1 activity is lost after treatment with 200 mM L-glucose 4066 2.7.3.3 L-histidine 10 mM, 2.4% inhibition 349 2.7.3.3 L-homoarginine 5fold higher concentration than L-Arg, 33% inhibition 2084 2.7.3.3 L-Lys 5fold higher concentration than L-Arg, 25% inhibition 502 2.7.3.3 L-nitroarginine 5fold higher concentration than L-Arg, 28% inhibition 21624 2.7.3.3 L-nitroarginine 10 mM, 52.6% inhibition 21624 2.7.3.3 lysine 31% inhibition at 2 mM 1107 2.7.3.3 lysine 3% enzyme inhibition at 2 mM 1107 2.7.3.3 Mg2+ at high concentrations noncompetitive inhibition of MgATP2- 6 2.7.3.3 MgADP- inhibition is potentiated by NO3- 795 2.7.3.3 MgATP2- enzyme form AK2 is strongly inhibited at high concentrations 108 2.7.3.3 Mn2+ at high concentrations noncompetitive inhibition of MgATP2- 11 2.7.3.3 additional information not inhibited by 50 mM acetate 2 2.7.3.3 additional information arginine kinase activity does not show significant variation after incubated with 10-200 mM L-citrulline, L-ornaline, and glycerol 2 2.7.3.3 N-methyl-L-Arg 5fold higher concentration than L-Arg, 28% inhibition 113957 2.7.3.3 N-[2-(1H-imidazol-4-yl)ethyl]-3-[1-(2-methoxyethyl)indol-3-yl]propanamide i.e. ZINC79191494, probably competitive inhibitor identified by in silico screening 256176 2.7.3.3 Na+ 200 mM, 50% inhibition 59 2.7.3.3 NADH noncompetitive 8 2.7.3.3 NH4+ 200 mM, 50% inhibition 54 2.7.3.3 nitrate - 308 2.7.3.3 nitrate 88% inhibition at 50 mM 308 2.7.3.3 nitrate 99% inhibition at 50 mM 308 2.7.3.3 nitrate 50 mM, 99% inhibition 308 2.7.3.3 nitrite 76% inhibition at 50 mM 168 2.7.3.3 nitrite 96% inhibition at 50 mM 168 2.7.3.3 nitrite 50 mM, 96% inhibition 168 2.7.3.3 nitroarginine 30% inhibition at 2 mM 101191 2.7.3.3 nitroarginine 30% enzyme inhibition at 2 mM 101191 2.7.3.3 ornithine 27% inhibition at 2 mM 576 2.7.3.3 ornithine 31% enzyme inhibition at 2 mM 576 2.7.3.3 p-hydroxymercuribenzoate - 98 2.7.3.3 Phenylglyoxal the enzyme loses 84.7% of its initial activity after incubation for 90 min with 0.0009 mM phenyllyoxal 301 2.7.3.3 putrescine 15% inhibition at 2 mM 155 2.7.3.3 putrescine 10% enzyme inhibition at 2 mM 155 2.7.3.3 quercetin - 137 2.7.3.3 rutin noncompetitive inhibitor, i.e. 2-(3,4-dihydroxyphenyl)-5,7-dihydroxy-3-[(2S,3R,4S,5S,6R)-3,4,5-trihydroxy-6-[[(2R,3R,4R,5R,6S)-3,4,5-trihydroxy-6-methyloxan-2-yl]oxymethyl]oxan-2-yl]oxychromen-4-one, about 20% residual activity at 0.02-0.06 mM rutin 1095 2.7.3.3 rutin - 1095 2.7.3.3 SDS complete inactivation at 1.0 mM, the inactivation is a first-order reaction, with the kinetic processes shifting from a monophase to biphase as SDS concentrations increase. SDS concentrations lower than 5 mM do not induce conspicuous changes in tertiary structures, while higher concentrations of SDS exposedhydrophobic surfaces and induce conformational changes 124 2.7.3.3 SO42- - 245 2.7.3.3 thiocyanate 16% inhibition at 50 mM 931 2.7.3.3 thiocyanate 21% inhibition at 50 mM 931 2.7.3.3 thiocyanate 50 mM, 21% inhibition 931 2.7.3.3 Urea 10% inhibition at 2 mM 116 2.7.3.3 Urea 13% enzyme inhibition at 2 mM 116 2.7.3.3 Zn2+ - 14 2.7.3.3 Zn2+ strong inhibition 14