2.5.1.47 (1R,2R)-1-(4-chlorobenzyl)-2-phenylcyclopropanecarboxylic acid - 213018 2.5.1.47 (1R,2R)-1-(4-methylbenzyl)-2-phenylcyclopropanecarboxylic acid - 213015 2.5.1.47 (1R,2R)-1-benzyl-2-phenylcyclopropanecarboxylic acid - 213012 2.5.1.47 (1R,2S)-1-ethyl-2-phenylcyclopropanecarboxylic acid - 213008 2.5.1.47 (1S,2R)-1-ethyl-2-phenylcyclopropanecarboxylic acid - 213009 2.5.1.47 (1S,2S)-1-(4-chlorobenzyl)-2-phenylcyclopropanecarboxylic acid - 213017 2.5.1.47 (1S,2S)-1-(4-methylbenzyl)-2-phenylcyclopropanecarboxylic acid - 213014 2.5.1.47 (1S,2S)-1-benzyl-2-phenylcyclopropanecarboxylic acid - 213011 2.5.1.47 (2E)-3-chloropent-2-enedioic acid - 212985 2.5.1.47 (NH4)6Mo7O24 1 mM, 97% inhibition 9298 2.5.1.47 (NH4)6Mo7O24 1 mM, 61% loss of activity 9298 2.5.1.47 1,1'-(1,3-propanediyl)bis(5-benzyl-6-methylsulfanyl-4,5-dihydro-1H-pyrazolo[3,4-d]pyrimidin-4-one) - 212968 2.5.1.47 1,1'-(1,3-propanediyl)bis(5-ethyl-6-methylthio-4,5-dihydro-1H-pyrazolo[3,4-d]pyrimidin-4-one) - 212967 2.5.1.47 1,1'-(1,3-propanediyl)bis(5-methyl-6-methylthio-4,5-dihydro-1H-pyrazolo[3,4-d]pyrimidin-4-one) - 212966 2.5.1.47 1,10-phenanthroline 14% inhibition at 1 mM 62 2.5.1.47 1,3-bis(4,6-diethylthio-1H-pyrazolo[3,4-d]pyrimidin-1-yl)propane - 212964 2.5.1.47 1,3-bis(4-ethoxy-6-methyl-sulfanyl-1H-pyrazolo[3,4-d]pyrimidin-1-yl)propane - 212965 2.5.1.47 1-(2-naphthylsulfonyl)-3-phenyl-1H-pyrazolo[3,4-d]pyrimidin-4-amine - 212961 2.5.1.47 1-(4,6-dimethylsulfanyl-1H-pyrazolo[3,4-d]pyrimidin-1-yl)-3-(5-methyl-6-methylsulfanyl-4-oxo-1,5-dihydropyrazolo[3,4-d]pyrimidin-1-yl)propane - 212969 2.5.1.47 1-(4-chlorophenyl)-1H-pyrazole-5-carboxylic acid 9% inhibition at 1 microM, 56% inhibition at 1 mM 251732 2.5.1.47 1-(4-fluorophenyl)-1H-pyrazole-5-carboxylic acid 8% inhibition at 1 microM, 95% inhibition at 1 mM; 8% inhibition at 1 microM, 95% inhibition at 1 mM 251734 2.5.1.47 1-ethyl-4-nitro-1H-pyrazole-5-carboxylic acid - 212995 2.5.1.47 1-N,4-N-bis[3-(1Hbenzimidazol-2-yl) phenyl]benzene-1,4-dicarboxamide determined as potential inhibitor via computational inhibitor screening, molecular dynamics simulation and homology modeling 212996 2.5.1.47 1-phenyl-1H-pyrazole-5-carboxylic acid 11% inhibition at 1 microM, 65% inhibition at 1 mM 251760 2.5.1.47 1-[(2,5-dichlorophenyl)sulfonyl]-3-phenyl-1Hpyrazolo[3,4-d]pyrimidine-4-amine - 212960 2.5.1.47 1-[(4-chlorophenyl)sulfonyl]-3-phenyl-1H-pyrazolo[3,4-d]pyrimidine-4-amine - 212959 2.5.1.47 1-[(4-nitrophenyl)sulfonyl]-3-phenyl-1H-pyrazolo[3,4-d]pyrimidine-4-amine - 212556 2.5.1.47 1H-pyrazole-5-carboxylic acid 9% inhibition at 1 microM, 94% inhibition at 1 mM 251805 2.5.1.47 2,2'-(1,2,4-thiadiazole-3,5-diyldisulfanediyl)diacetic acid - 212988 2.5.1.47 2,2'-(5-ethyl-5-nitrodihydropyrimidine-1,3(2H,4H)-diyl)diacetic acid - 212993 2.5.1.47 2-phenylbutanedioic acid - 212976 2.5.1.47 2-[(1-methyl-1H-tetrazol-5-yl)sulfanyl]pyridine-3-carboxylic acid - 212986 2.5.1.47 2-[(5-methyl-1,3,4-thiadiazol-2-yl)carbamoyl]-3-nitrobenzoic acid - 212982 2.5.1.47 3,3'-[(phenylsulfonyl)imino]dipropanoic acid (non-preferred name) - 212991 2.5.1.47 3-(morpholin-4-ylmethyl)furan-2-carboxylic acid - 212983 2.5.1.47 3-phenyl-1-(methylsulfonyl)-1H-pyrazolo[3,4-d]pyrimidine-4-amine - 212963 2.5.1.47 3-phenyl-1-(phenylsulfonyl)-1H-pyrazolo[3,4-d]pyrimidine-4-amine - 212962 2.5.1.47 3-phenyl-1-tosyl-1H-pyrazolo[3,4-d] pyrimidin-4-amine - 212957 2.5.1.47 3-phenyl-1H-pyrazolo[3,4-d]pyrimidin-4-amine - 212956 2.5.1.47 3-[[(3,4-dichlorophenyl)carbamoyl]amino]benzoic acid inhibits both isoforms CysK1 and CysK2 and O-phosphoserine sulfhydrylase CysM 209144 2.5.1.47 3-[[([1,1'-biphenyl]-3-yl)carbamoyl]amino]benzoic acid inhibits both isoforms CysK1 and CysK2 and O-phosphoserine sulfhydrylase CysM 226904 2.5.1.47 4,6-bis(methylsulfanyl)-1-phthalimidopropyl-1H-pyrazolo[3,4-d]-pyrimidine - 212970 2.5.1.47 4-(2-methylphenyl)-8-nitro-2-thioxo-2,3,4,4a-tetrahydro-5H-pyrimido[5,4-e][1,3]thiazolo[3,2-a]pyrimidin-5-one minimum inhibitory concentration against Mycobacterium tuberculosis 0.0335 mM, cytotoxicity against HEK 293T cell 3.6% at 0.025 mM 88692 2.5.1.47 4-(4-methoxyphenyl)-8-nitro-2-thioxo-2,3,4,4a-tetrahydro-5H-pyrimido[5,4-e][1,3]thiazolo[3,2-a]pyrimidin-5-one minimum inhibitory concentration against Mycobacterium tuberculosis 0.0321 mM, cytotoxicity against HEK 293T cell 0.2% at 0.025 mM 88691 2.5.1.47 4-(methylsulfinyl)-2-[(phenylsulfonyl)amino]butanoic acid - 212994 2.5.1.47 4-hydroxy-2-[2-(1H-indol-3-yl)-2-oxoethyl]sulfanyl-1H-pyrimidin-6-one inhibitor identified by molecular docking. Conserved residues involved in hydrogen bonding interaction include T85, S86, Q159, G87, R116, and G236. The compound displays a binding affinity of 8.05 microM and inhibits about 73% activity at 0.1 mM 172033 2.5.1.47 4-[[(3,4-dichlorophenyl)carbamoyl]amino]-2-hydroxybenzoic acid selective for isoform CysK1, IC50 value for isoform CysK2 above 300 microM 252180 2.5.1.47 4-[[([1,1'-biphenyl]-3-yl)carbamoyl]amino]-2-hydroxybenzoic acid inhibits both isoforms CysK1 and CysK2 and O-phosphoserine sulfhydrylase CysM 227016 2.5.1.47 5,5'-dithiobis(2-nitrobenzoic acid) non-competitive 221 2.5.1.47 5,5'-dithiobis(2-nitrobenzoic acid) 1 mM, 92% inactivation 221 2.5.1.47 5-[[(3,4-dichlorophenyl)carbamoyl]amino]-2-hydroxybenzoic acid inhibits both isoforms CysK1 and CysK2 227110 2.5.1.47 5-[[([1,1'-biphenyl]-3-yl)carbamoyl]amino]-2-hydroxybenzoic acid inhibits both isoforms CysK1 and CysK2 and O-phosphoserine sulfhydrylase CysM 227111 2.5.1.47 6-(1,3,4-thiadiazol-2-ylcarbamoyl)cyclohex-3-ene-1-carboxylic acid - 212974 2.5.1.47 6-methyl-4,5,6,7-tetrahydro-1,2-benzoxazole-5,6-dicarboxylic acid - 212990 2.5.1.47 6-methyl-7-oxo-6-azabicyclo[3.2.1]oct-2-ene-2,8-dicarboxylic acid - 212987 2.5.1.47 6-methylsulfanyl-1-(3-phenylpropyl)-4,5-dihydro-1H-pyrazolo[3,4-d]pyrimidin-4-one - 212972 2.5.1.47 6-methylsulfanyl-1-phthalimidopropyl-4(pyrrolidin-1-yl)-1H-pyrazolo[3,4-d]pyrimidine - 212971 2.5.1.47 6-[(pyridin-4-ylmethyl)carbamoyl]cyclohex-3-ene-1-carboxylic acid - 212978 2.5.1.47 8-nitro-4-(2-nitrophenyl)-2-thioxo-2,3,4,4a-tetrahydro-5H-pyrimido[5,4-e][1,3]thiazolo[3,2-a]pyrimidin-5-one minimum inhibitory concentration against Mycobacterium tuberculosis 0.0309 mM, cytotoxicity against HEK 293T cell 1% at 0.025 mM 88690 2.5.1.47 8-nitro-4-[2-(trifluoromethyl)phenyl]-4,4a-dihydro-2H-pyrimido[5,4-e][1,3]thiazolo[3,2-a]pyrimidine-2,5(3H)-dione minimum inhibitory concentration against Mycobacterium tuberculosis 0.0076 mM, cytotoxicity against HEK 293T cell 5.7% at 0.025 mM 88693 2.5.1.47 acetate - 47 2.5.1.47 acetyl-CoA - 29 2.5.1.47 aggreticin - 213001 2.5.1.47 AgNO3 1 mM, 22% inhibition 360 2.5.1.47 AgNO3 1 mM, complete loss of activity 360 2.5.1.47 Aminooxyacetate 57% and 64% inhibition at 1 mM, isoenzymes 1 and 2, respectively 1374 2.5.1.47 Aminooxyacetate 10 mM, 76% inhibition 1374 2.5.1.47 cadmium chloride plants grown in the presence of 0.0178 mM cadmium chloride show 141% increase in activity in leaves, and 189% increase in activity in root, respectively 37806 2.5.1.47 cadmium chloride plants grown in the presence of 0.0178 mM cadmium chloride show 150% increase in activity in leaves; plants grown in the presence of 0.0178 mM cadmium chloride show 260% increase in activity in leaves, and 222% increase in activity in root, respectively 37806 2.5.1.47 Cd2+ 55% inhibition at 1 mM 52 2.5.1.47 chloroalanine substrate inhibition 6173 2.5.1.47 Cl- HgCl2 141 2.5.1.47 Cl- - 141 2.5.1.47 Co2+ complete inhibition at 1 mM 23 2.5.1.47 copper sulfate plants grown in the presence of 0.78 mM copper sulfate show 102% increase in activity in leaves, and 98% increase in activity in root, respectively 25472 2.5.1.47 copper sulfate plants grown in the presence of 0.78 mM copper sulfate show 20% increase in activity in leaves, and 110% increase in activity in root, respectively; plants grown in the presence of 0.78 mM copper sulfate show 56% increase in activity in leaves 25472 2.5.1.47 Cu2+ - 19 2.5.1.47 CuSO4 1 mM, 99% loss of activity 263 2.5.1.47 Cys - 553 2.5.1.47 cystathionine competitive to sulfide 3197 2.5.1.47 cystathionine - 3197 2.5.1.47 cystathionine 91% inhibition at 10 mM 3197 2.5.1.47 cystine competitive versus O-acetyl-L-serine, the cystine-binding residues are highly conserved in all OASS proteins; competitive versus O-acetyl-L-serine, the cystine-binding residues are highly conserved in all OASS proteins. Active site of CysK2–cystine binding structure, overview. Cystine occupies the substrate/product binding site of the enzyme 1967 2.5.1.47 D-cycloserine 82% loss of activity at 5 mM 874 2.5.1.47 deacetylkinamycin C - 213002 2.5.1.47 deoxyfrenolicin - 213003 2.5.1.47 DYVI a peptide based on the C-terminus of the partner serine acetyltransferase with which the enzyme forms a complex, competitive inhibition 88689 2.5.1.47 EDTA 1 mM, 16% inhibition 21 2.5.1.47 exophillic acid from Exophiala sp.FKI-7082 , specific for isozyme CS1 212998 2.5.1.47 FeSO4 1 mM, 96% inhibition 655 2.5.1.47 FeSO4 1 mM, 99% loss of activity 655 2.5.1.47 Hg2+ - 33 2.5.1.47 hydroxylamine - 85 2.5.1.47 hydroxylamine 31% inhibition at 1 mM 85 2.5.1.47 hydroxylamine complete inhibition at 10 mM, isoenzymes 1 and 2, 90% inhibition at 10 mM, isoenzyme 3 85 2.5.1.47 hydroxylamine 35% and 48% inhibition at 5 mM, isoenzymes 1 and 2, respectively 85 2.5.1.47 hydroxylamine 57% loss of activity at 10 mM, isoenzyme 1' 85 2.5.1.47 hydroxylamine 10 mM, 71.2% inhibition 85 2.5.1.47 iodoacetamide 1 mM, 48% loss of activity 67 2.5.1.47 KCN 15.6% inhibition by 1 mM 161 2.5.1.47 kerriamycin B - 212999 2.5.1.47 kerriamycin C - 213000 2.5.1.47 L-cysteine not inhibitory up to 3.7 mM 74 2.5.1.47 L-cysteine non-competitive 74 2.5.1.47 L-cysteine - 74 2.5.1.47 L-cysteine 66% inhibition at 10 mM 74 2.5.1.47 L-cysteine 35% inhibition at 4.5 mM 74 2.5.1.47 L-cysteine 28-41% inhibition at 4.5 mM, isoenzyme-dependent 74 2.5.1.47 L-cysteine 50% inhibition at 5 mM, only isoenzyme 1 74 2.5.1.47 L-cysteine substrate inhibition 74 2.5.1.47 L-homocysteine competitive to sulfide 305 2.5.1.47 L-homoserine - 345 2.5.1.47 L-homoserine non-competitive 345 2.5.1.47 lead nitrate plants grown in the presence of 2.4 mM lead nitrate plus 5 mM EDTA show 197% increase in activity in leaves, and 201% increase in activity in root, respectively 22325 2.5.1.47 lead nitrate plants grown in the presence of 2.4 mM lead nitrate plus 5 mM EDTA show 176% increase in activity in leaves; plants grown in the presence of 2.4 mM lead nitrate plus 5 mM EDTA show 302% increase in activity in leaves, and 300% increase in activity in root, respectively 22325 2.5.1.47 methionine competitive to sulfide 692 2.5.1.47 methionine slight inhibition 692 2.5.1.47 methionine - 692 2.5.1.47 methionine 46% and 37% inhibition at 1 mM, isoenzymes 1 and 2, respectively 692 2.5.1.47 metronidazole - 5374 2.5.1.47 MNDGI pentapeptide inhibitor; the C-terminal pentapeptide of serine acetyltransferase penetrates into the active site and competes with the substrate O3-acetyl-L-serine, thus inhibiting L-cysteine formation, essential contributor to the binding is the terminal Ile267 (80% interaction energy), Asn266 and Leu265 contribute 10% interaction energy each, pentapeptides of the structure MNxxI (xx are 2 exchangeable amino acids) have inhibitory action 39782 2.5.1.47 MNEGI pentapeptide inhibitor; the C-terminal pentapeptide of serine acetyltransferase penetrates into the active site and competes with the substrate O3-acetyl-L-serine, thus inhibiting L-cysteine formation, essential contributor to the binding is the terminal Ile267 (80% interaction energy), Asn266 and Leu265 contribute 10% interaction energy each, pentapeptides of the structure MNxxI (xx are 2 exchangeable amino acids) have inhibitory action 39783 2.5.1.47 MNENI pentapeptide inhibitor; the C-terminal pentapeptide of serine acetyltransferase penetrates into the active site and competes with the substrate O3-acetyl-L-serine, thus inhibiting L-cysteine formation, essential contributor to the binding is the terminal Ile267 (80% interaction energy), Asn266 and Leu265 contribute 10% interaction energy each, pentapeptides of the structure MNxxI (xx are 2 exchangeable amino acids) have inhibitory action 39778 2.5.1.47 MNETI pentapeptide inhibitor; the C-terminal pentapeptide of serine acetyltransferase penetrates into the active site and competes with the substrate O3-acetyl-L-serine, thus inhibiting L-cysteine formation, essential contributor to the binding is the terminal Ile267 (80% interaction energy), Asn266 and Leu265 contribute 10% interaction energy each, pentapeptides of the structure MNxxI (xx are 2 exchangeable amino acids) have inhibitory action 39785 2.5.1.47 MNKGI pentapeptide inhibitor; the C-terminal pentapeptide of serine acetyltransferase penetrates into the active site and competes with the substrate O3-acetyl-L-serine, thus inhibiting L-cysteine formation, essential contributor to the binding is the terminal Ile267 (80% interaction energy), Asn266 and Leu265 contribute 10% interaction energy each, pentapeptides of the structure MNxxI (xx are 2 exchangeable amino acids) have inhibitory action 39788 2.5.1.47 MNKVI pentapeptide inhibitor; the C-terminal pentapeptide of serine acetyltransferase penetrates into the active site and competes with the substrate O3-acetyl-L-serine, thus inhibiting L-cysteine formation, essential contributor to the binding is the terminal Ile267 (80% interaction energy), Asn266 and Leu265 contribute 10% interaction energy each, pentapeptides of the structure MNxxI (xx are 2 exchangeable amino acids) have inhibitory action 39787 2.5.1.47 MNLGI pentapeptide inhibitor; the C-terminal pentapeptide of serine acetyltransferase penetrates into the active site and competes with the substrate O3-acetyl-L-serine, thus inhibiting L-cysteine formation, essential contributor to the binding is the terminal Ile267 (80% interaction energy), Asn266 and Leu265 contribute 10% interaction energy each, pentapeptides of the structure MNxxI (xx are 2 exchangeable amino acids) have inhibitory action 39781 2.5.1.47 MNLNI pentapeptide inhibitor; wild type pentapeptide of serine acetyltransferase 39775 2.5.1.47 MNPHI pentapeptide inhibitor; the C-terminal pentapeptide of serine acetyltransferase penetrates into the active site and competes with the substrate O3-acetyl-L-serine, thus inhibiting L-cysteine formation, essential contributor to the binding is the terminal Ile267 (80% interaction energy), Asn266 and Leu265 contribute 10% interaction energy each, pentapeptides of the structure MNxxI (xx are 2 exchangeable amino acids) have inhibitory action 39786 2.5.1.47 MNVPI pentapeptide inhibitor; the C-terminal pentapeptide of serine acetyltransferase penetrates into the active site and competes with the substrate O3-acetyl-L-serine, thus inhibiting L-cysteine formation, essential contributor to the binding is the terminal Ile267 (80% interaction energy), Asn266 and Leu265 contribute 10% interaction energy each, pentapeptides of the structure MNxxI (xx are 2 exchangeable amino acids) have inhibitory action 39784 2.5.1.47 MNWNI pentapeptide inhibitor; the C-terminal pentapeptide of serine acetyltransferase penetrates into the active site and competes with the substrate O3-acetyl-L-serine, thus inhibiting L-cysteine formation, essential contributor to the binding is the terminal Ile267 (80% interaction energy), Asn266 and Leu265 contribute 10% interaction energy each, pentapeptides of the structure MNxxI (xx are 2 exchangeable amino acids) have inhibitory action 39776 2.5.1.47 MNYDI pentapeptide inhibitor; the C-terminal pentapeptide of serine acetyltransferase penetrates into the active site and competes with the substrate O3-acetyl-L-serine, thus inhibiting L-cysteine formation, essential contributor to the binding is the terminal Ile267 (80% interaction energy), Asn266 and Leu265 contribute 10% interaction energy each, pentapeptides of the structure MNxxI (xx are 2 exchangeable amino acids) have inhibitory action 39777 2.5.1.47 MNYDI interaction of the inhibitory pentapeptide MNYDI with CysK OASS isozyme from Salmonella typhimurium, the MNYDI peptide interacts with the HiCysK active site mainly through H-bonds involving its C-terminal carboxylate and hydrophobic interactions involving the side chains of Ile5 and Tyr3, saturation transfer-difference NMR spectroscopy and docking study, docking simulations and molecular modelling, overview 39777 2.5.1.47 MNYDI interaction of the inhibitory pentapeptide MNYDI with CysK OASS isozyme from Salmonella typhimurium, the MNYDI peptide interacts with the HiCysK active site mainly through H-bonds involving its C-terminal carboxylate and hydrophobic interactions involving the side chains of Ile5 and Tyr3, saturation transfer-difference NMR spectroscopy and docking study, docking simulations and molecular modelling, overview; interaction of the inhibitory pentapeptide MNYDI with CysM OASS isozyme from Salmonella typhimurium, saturation transfer-difference NMR spectroscopy and docking study, docking simulations and molecular modelling, overview. In isozyme CysM multiple H-bond interactions are made by Asn2 side chain with S205 side chain and I206 and I209 backbone carbonyl groups 39777 2.5.1.47 MNYFI pentapeptide inhibitor; the C-terminal pentapeptide of serine acetyltransferase penetrates into the active site and competes with the substrate O3-acetyl-L-serine, thus inhibiting L-cysteine formation, essential contributor to the binding is the terminal Ile267 (80% interaction energy), Asn266 and Leu265 contribute 10% interaction energy each, pentapeptides of the structure MNxxI (xx are 2 exchangeable amino acids) have inhibitory action 39780 2.5.1.47 MNYSI pentapeptide inhibitor; the C-terminal pentapeptide of serine acetyltransferase penetrates into the active site and competes with the substrate O3-acetyl-L-serine, thus inhibiting L-cysteine formation, essential contributor to the binding is the terminal Ile267 (80% interaction energy), Asn266 and Leu265 contribute 10% interaction energy each, pentapeptides of the structure MNxxI (xx are 2 exchangeable amino acids) have inhibitory action 39779 2.5.1.47 Monoiodoacetic acid 1 mM, complete inactivation 2275 2.5.1.47 additional information partial inhibition of enzyme upon complex formation with serine acetyltransferase 2 2.5.1.47 additional information presence of 4% NaCl is not inhibitory 2 2.5.1.47 additional information activity is inhibited by the interaction with serine acetyltransferase, the preceding enzyme in the metabolic pathway. Inhibition is exerted by the insertion of serine acetyltransferase C-terminal peptide into the enzyme's active site. The active site determinants that modulate the interaction specificity are investigated by comparing the binding affinity of thirteen pentapeptides, derived from the C-terminal sequences of serine acetyltransferase of closely related species. Subtle changes in protein active sites have profound effects on protein-peptide recognition. Affinity is strongly dependent on the pentapeptide sequence, signaling the relevance of P3-P4-P5 for the strength of binding, and P1-P2 mainly for specificity. The presence of an aromatic residue at P3 results in high affinity peptides with K(diss) in the micromolar and submicromolar range, regardless of the species. An acidic residue, like aspartate at P4, further strengthens the interaction 2 2.5.1.47 additional information CysK is competitively inhibited within the cysteine synthase complex 2 2.5.1.47 additional information molecular dynamic simulation and inhibitor prediction of cysteine synthase 2 2.5.1.47 additional information anions, like sulfate, significantly reduce the affinity of peptides for CysK 2 2.5.1.47 additional information identification and evaluation of natural inhibitors of Entamoeba histolytica cysteine synthase from microbial secondary metabolites, high-throughput screening. Terreinol and citromycetin are poor inhibitors; identification and evaluation of natural inhibitors of Entamoeba histolytica cysteine synthase from microbial secondary metabolites, high-throughput screening. Terreinol and citromycetin are poor inhibitors, no inhibition of isozyme CS3 by exophillic acid from Exophiala sp.FKI-7082, which is specific for isozyme CS1 2 2.5.1.47 additional information rational structure-guided design of nanomolar thiazolidine inhibitors of Mycobacterium tuberculosis CysK1 O-acetyl serine sulfhydrylase, discovered using the crystal structure of a CysK1-peptide inhibitor complex as template, pharmacophore modeling and in vitro screening, overview. Chemical synthesis leads to improved thiazolidine inhibitors with an IC50 value of 19 nM for the best compound, a 150fold higher potency than the natural peptide inhibitor with IC50 of 0.0029 mM 2 2.5.1.47 additional information computational and spectroscopic approaches to rationally design, synthesize, and test a series of substituted 2-phenylcyclopropane carboxylic acids that bind to the two Salmonella typhymurium OASS isoforms at nanomolar concentrations, Kd values and binding structures, molecular modeling and docking study, overview; computational and spectroscopic approaches to rationally design, synthesize, and test a series of substituted 2-phenylcyclopropane carboxylic acids that bind to the two Salmonella typhymurium OASS isoforms at nanomolar concentrations, Kd values and binding structures, molecular modeling and docking study, overview 2 2.5.1.47 additional information enzyme inhibitor development, in silico molecular docking simulations, using the three-dimensional crystal structure of O-acetyl-L-serine sulfhydrylase enzyme complexed with cysteine and pyridoxal 5'-phosphate ligands, PDB ID 3BM5, on nine pyrazolo[3,4-d]pyrimidine molecules without linkers and nine pyrazolo[3,4-d]pyrimidine molecules with a trimethylene linker along with the reference drug metronidazole, binding structures, ligand docking and interaction analysis, detiled overview 2 2.5.1.47 additional information direct targeting of Arabidopsis thaliana cysteine synthase complexes with synthetic polypeptides to selectively deregulate cysteine synthesis, several polypeptides based on OAS-TL C amino-acid sequence found at SAT-OASTL interaction sites are designed as probable competitors for SAT binding. After verification of the binding in a yeast two-hybrid assay, the most strongly interacting polypeptide is introduced to different cellular compartments of Arabidopsis thaliana cell via genetic transformation 2 2.5.1.47 additional information identification of potential inhibitors of the two isozymes A and B via a ligand- and structure-based in silico screening of a subset of the ZINC library using FLAP. The binding affinities of the most promising candidates are measured in vitro on purified O-acetylserine sulfhydrylase-A and O-acetylserine sulfhydrylase-B by a direct method that exploits the change in the cofactor fluorescence, ligand binding analysis, overview; identification of potential inhibitors of the two isozymes A and B via a ligand- and structure-based in silico screening of a subset of the ZINC library using FLAP. The binding affinities of the most promising candidates are measured in vitro on purified O-acetylserine sulfhydrylase-A and O-acetylserine sulfhydrylase-B by a direct method that exploits the change in the cofactor fluorescence, ligand binding analysis, overview 2 2.5.1.47 N-(furan-2-ylcarbonyl)leucine - 212979 2.5.1.47 N-(furan-2-ylcarbonyl)phenylalanine - 212981 2.5.1.47 N-(thiophen-2-ylsulfonyl)valine - 212975 2.5.1.47 N-[(2,2-dimethyl-4,6-dioxo-1,3-dioxan-5-ylidene)methyl]glutamic acid - 212989 2.5.1.47 N-[(2,2-dimethyl-4,6-dioxo-1,3-dioxan-5-ylidene)methyl]leucine - 212984 2.5.1.47 N-[(3-carboxybicyclo[2.2.1]hept-5-en-2-yl)carbonyl]glycylglycine - 212973 2.5.1.47 N-{4-[(4-amino-3-phenyl-1H-pyrazolo[3,4-d]pyrimidin-1-yl)sulfonyl]phenyl}acetamide - 212958 2.5.1.47 NaN3 - 238 2.5.1.47 nanaomycin A - 18674 2.5.1.47 naphthacemycin A - 213004 2.5.1.47 NEM non-competitive 89 2.5.1.47 NH2OH 97% loss of activity at 10 mM 1109 2.5.1.47 Ni2+ complete inhibition at 1 mM 38 2.5.1.47 Ni2+ - 38 2.5.1.47 O-acetylserine above 72 mM 2752 2.5.1.47 O-acetylserine at 150 mM 2752 2.5.1.47 O-acetylserine - 2752 2.5.1.47 O-acetylserine substrate inhibition 2752 2.5.1.47 ornidazole - 14341 2.5.1.47 p-chloromercuribenzoate non-competitive 43 2.5.1.47 p-chloromercuribenzoate 40% inhibition at 1 mM 43 2.5.1.47 p-chloromercuribenzoate 14% and 4% inhibition at 1 mM, isoenzymes 1 and 2, respectively 43 2.5.1.47 p-chloromercuribenzoate 1 mM, 59% inhibition 43 2.5.1.47 p-chloromercuriphenylsulfonic acid 46% inhibition at 1 mM 1416 2.5.1.47 p-hydroxymercuribenzoate - 98 2.5.1.47 patulin - 213005 2.5.1.47 PCMB 1 mM, 97% loss of activity 78 2.5.1.47 pencolide shows cysteine deprivation-dependent antiamebic activity,with 7.6 times lower IC50 in the absence of cysteine than that in the presence of cysteine; shows cysteine deprivation-dependent antiamebic activity,with 7.6 times lower IC50 in the absence of cysteine than that in the presence of cysteine 252605 2.5.1.47 peroxynitrite nitrating conditions after exposure to peroxynitrite strongly inhibit enzyme activity. Among the isoforms, cytosolic OASA1 is markedly sensitive to nitration. Nitration assays on purified recombinant OASA1 protein lead to 90% reduction of the activity due to inhibition of the enzyme. Inhibition of OASA1 activity upon nitration correlates with the identification of a modified OASA1 protein containing a 3-nitroTyr302 residue. Inhibition caused by Tyr302 nitration on OASA1 activity seems to be due to a drastically reduced O-acetylserine substrate binding to the nitrated protein, and also to reduced stabilization of the pyridoxal-5-phosphate cofactor through hydrogen bonds 1220 2.5.1.47 phenylhydrazine 73% inhibition by 1 mM, 97.4% inhibition by 10 mM 398 2.5.1.47 pyridoxal - 608 2.5.1.47 pyridoxal hydrochloride 54% inhibition at 1 mM 45867 2.5.1.47 S-methylcysteine slight inhibition 9355 2.5.1.47 S-sulfocysteine 52% inhibition at 4.5 mM 9262 2.5.1.47 S-sulfocysteine 24% inhibition at 4.5 mM, isoenzyme 1 9262 2.5.1.47 S-sulfocysteine 26% loss of activity at 5 mM 9262 2.5.1.47 S2- - 1009 2.5.1.47 Semicarbazide 60% loss of activity at 1 mM 382 2.5.1.47 Semicarbazide 13% inhibition by 1 mM, 38.6% inhibition by 10 mM 382 2.5.1.47 serine competitive to O-acetylserine 930 2.5.1.47 serine acetyltransferase serine acetyltransferase (EC 2.3.1.30) can inhibit O-acetylserine sulfhydrylase catalytic activity with a double mechanism, the competition with O-acetylserine for binding to the enzyme active site and the stabilization of a closed conformation that is less accessible to the natural substrate 135463 2.5.1.47 SO32- competitive to sulfide 902 2.5.1.47 SO42- - 245 2.5.1.47 sodium arsenite plants grown in the presence of 0.0267 mM sodium arsenite show 109% increase in activity in leaves, and 238% increase in activity in root, respectively 2419 2.5.1.47 sodium arsenite plants grown in the presence of 0.0267 mM sodium arsenite show 108% increase in activity in leaves, and 250% increase in activity in root, respectively; plants grown in the presence of 0.0267 mM sodium arsenite show 120% increase in activity in leaves 2419 2.5.1.47 Sodium borohydride 59% inhibition at 1 mM 2356 2.5.1.47 Sulfide above 107 mM 318 2.5.1.47 Sulfide - 318 2.5.1.47 Sulfide above 200 mM 318 2.5.1.47 Sulfide substrate inhibition 318 2.5.1.47 tetracycline - 2872 2.5.1.47 Thiourea 34% inhibition at 1 mM 844 2.5.1.47 tinidazole - 212955 2.5.1.47 trans-1-(4-chlorobenzyl)-2-phenylcyclopropanecarboxylic acid - 213016 2.5.1.47 trans-1-(4-methylbenzyl)-2-phenylcyclopropanecarboxylic acid - 213013 2.5.1.47 trans-1-benzyl-2-phenylcyclopropanecarboxylic acid - 213010 2.5.1.47 trans-1-ethyl-2-phenylcyclopropanecarboxylic acid - 213007 2.5.1.47 trans-1-phenethyl-2-phenylcyclopropanecarboxylic acid - 213019 2.5.1.47 trans-2-phenylcyclopropanecarboxylic acid - 213006 2.5.1.47 trichloroacetic acid inactivation at 16.6% v/v; inactivation at 16.6% v/v 48176 2.5.1.47 trifluoroalanine irreversible but weak inhibitor; irreversible but weak inhibitor 135410 2.5.1.47 xanthofulvin from Penicillium sp. if08054; from Penicillium sp. if08054 , inhibits isozymes CS1 and CS3 212997 2.5.1.47 Zn2+ 95% inhibition at 1 mM 14 2.5.1.47 Zn2+ 1 mM, 94% inhibition 14 2.5.1.47 ZnCl2 1 mM, 88% loss of activity 271 2.5.1.47 [2-[3-acetyl-1-(2,2-dihydroxyethyl)-4-hydroxy-5-oxo-2,5-dihydro-1H-pyrrol-2-yl]phenyl](hydroxy)oxoammonium - 212992 2.5.1.47 [3-[(2-carboxy-3-methyl-8-oxo-5-thia-1-azabicyclo[4.2.0]oct-2-en-7-yl)carbamoyl]-1-methyl-1H-pyrazol-4-yl](hydroxy)oxoammonium - 212980 2.5.1.47 [3-[(2-carboxypiperidin-1-yl)sulfonyl]phenyl](hydroxy)oxoammonium - 212977