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Ligand L-cysteine
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Basic Ligand Information
BRENDA
moreKEGG
Show all BRENDA pathways known for L-cysteine
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open all tablesRoles as Enzyme Ligand
In Vivo Substrate in Enzyme-catalyzed Reactions (50 results)
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EC NUMBER 
PROVEN IN VIVO REACTION
REACTION DIAGRAM
LITERATURE
ENZYME 3D STRUCTURE
L-cysteine + O2 = 3-sulfino-L-alanine
-
L-cysteine + O2 = 3-sulfinoalanine
725864, 724297, 724391, 725720, 724336, 743757, 741585, 742295, 741904, 742253, 742264, 742755, 743088, 741704
-
hercynine + L-cysteine + O2 = S-(hercyn-2-yl)-L-cysteine S-oxide + H2O
-
L-histidine + L-cysteine + O2 = S-(L-histidin-5-yl)-L-cysteine S-oxide + H2O
-
hercynine + L-cysteine + O2 = S-(hercyn-2-yl)-L-cysteine S-oxide + H2O
-
O-succinyl-L-homoserine + L-cysteine = L-cystathionine + succinate
34706, 660307, 637426, 637454, 637455, 637452, 637453, 637456, 637424, 637428, 637458, 660344, 657952
-
L-cysteine + 'activated' tRNA = L-serine + tRNA containing a thionucleotide
-
L-cysteine + acceptor = L-alanine + S-sulfanyl-acceptor
-
L-cysteine + [enzyme]-cysteine = L-alanine + [enzyme]-S-sulfanylcysteine
645619, 645615, 645616, 645627, 645628, 645630, 645632, 645633, 645634, 645635, 645638, 725215, 645624, 645631, 645636, 645621, 645640, 645620
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molybdenum cofactor + L-cysteine + H+ = thio-molybdenum cofactor + L-alanine + H2O
-
molybdenum cofactor + L-cysteine + reduced acceptor + 2 H+ = thio-molybdenum cofactor + L-alanine + H2O + oxidized acceptor
-
MoO2(OH)Dtpp-mP + L-cysteine + 2 H+ = MoOS(OH)Dtpp-mP + L-alanine + H2O
-
L-cysteine + HCN = sulfide + L-3-cyanoalanine
-
L-cysteine + hydrogen cyanide = hydrogen sulfide + L-3-cyanoalanine
-
ATP + L-cysteine + tRNACys = AMP + diphosphate + L-cysteinyl-tRNACys
653867, 745862, 649098, 652821, 652909, 675435, 650423, 746197, 746259, 672180, 650990, 675395, 745531, 746416, 653662
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ATP + L-cysteine + holo-[L-cysteinyl-carrier protein] = AMP + diphosphate + L-cysteinyl-[L-cysteinyl-carrier protein]
-
1-O-(2-amino-2-deoxy-alpha-D-glucopyranosyl)-1D-myo-inositol + L-cysteine + ATP = 1-O-[2-(L-cysteinamido)-2-deoxy-alpha-D-glucopyranosyl]-1D-myo-inositol + AMP + diphosphate
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ATP + L-Glu + L-Cys = ADP + phosphate + gamma-L-Glu-L-Cys
653272, 651813, 649655, 649189, 653993, 650713, 653987, 652979, 649413, 653714, 650595, 653171, 652341, 650330, 651896, 650135, 652304, 652192, 649263, 651996, 651393, 649525, 651392, 652480, 652649
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ATP + L-glutamate + L-cysteine = ADP + phosphate + gamma-L-glutamyl-L-cysteine
694060, 727274, 726910, 690385, 690630, 692442, 694485, 745900, 745490, 745745, 744070, 745492, 726912, 745805, 744469, 744853, 745888, 744122, 744438, 745734, 691909, 692055, 663122, 663074, 660680, 663215, 662512, 663435, 661811, 675918, 671927, 674643, 672053, 676524, 672367, 676435, 672904, 671223, 691912, 690440, 694609, 692437, 692058, 692444, 694674, 690387
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3 ATP + L-2-aminohexanedioate + L-cysteine + L-valine + H2O = 3 AMP + 3 diphosphate + N-[L-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine
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CTP + (R)-4'-phosphopantothenate + L-cysteine = CMP + diphosphate + N-[(R)-4'-phosphopantothenoyl]-L-cysteine
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ATP + (R)-4'-phosphopantothenate + L-cysteine = AMP + diphosphate + N-[(R)-4'-phosphopantothenoyl]-L-cysteine
-
CTP + (R)-4'-phosphopantothenate + L-cysteine = CMP + diphosphate + N-[(R)-4'-phosphopantothenoyl]-L-cysteine
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In Vivo Product in Enzyme-catalyzed Reactions (28 results)
EC NUMBER
PROVEN IN VIVO REACTION
REACTION DIAGRAM
LITERATURE
ENZYME 3D STRUCTURE
O-acetyl-L-serine + sulfide = L-cysteine + acetate
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Substrate in Enzyme-catalyzed Reactions (296 results)
EC NUMBER
REACTION
REACTION DIAGRAM
LITERATURE
ENZYME 3D STRUCTURE
L-cysteine + O2 = 3-sulfino-L-alanine
711255, 657832, 659966, 439541, 439544, 439545, 439547, 439548, 439549, 439550, 439551, 439552, 439553, 439554, 439555, 657515, 657523, 659515, 659767, 674569, 676962, 693792, 695529, 710849, 698981, 674292, 695531, 713084, 674873, 697475, 765261, 676850, 765168, 439542, 439546, 439543
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L-cysteine + O2 = 3-sulfinoalanine
725864, 724297, 724391, 725720, 724336, 758785, 743757, 741585, 742295, 741904, 742253, 742264, 742755, 743088, 741704, 758787, 759471
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p-hydroxyphenylacetaldoxime + [reduced NADPH-hemoprotein reductase] + cysteine + O2 = S-(benzohydroximoyl)-L-cysteine + [oxidized NADPH-hemoprotein reductase] + 2 H2O
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2-fluoro-L-histidine + L-cysteine + O2 = S-(2-fluoro-L-histidin-5-yl)-L-cysteine S-oxide + H2O
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D-histidine + L-cysteine + O2 = S-(D-histidin-5-yl)-L-cysteine S-oxide + S-(D-histidin-2-yl)-L-cysteine S-oxide + H2O
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hercynine + L-cysteine + O2 = S-(hercyn-2-yl)-L-cysteine S-oxide + H2O
-
L-histidinamide + L-cysteine + O2 = S-(L-histidinamide-5-yl)-L-cysteine S-oxide + H2O
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L-histidine + L-cysteine + O2 = S-(L-histidin-5-yl)-L-cysteine S-oxide + H2O
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hercynine + L-cysteine + O2 = S-(hercyn-2-yl)-L-cysteine S-oxide + H2O
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L-cysteine + H2O + O2 = 2-oxo-3-mercaptopropanoic acid + NH3 + H2O2
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L-cysteine + H2O + 2 cytochrome b = 2-oxo-3-thiopropanoate + NH3 + 2 reduced cytochrome b
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L-Cys + O2 = ? + H2O
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L-cysteine + 2-(glutathione-S-yl)-trichloro-p-hydroquinone = glutathionyl cysteinyl disulfide + trichloro-p-hydroquinone
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S-adenosyl-L-methionine + L-cysteine = S-adenosyl-L-homocysteine + S-methyl-L-cysteine
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S-adenosyl-L-methionine + L-cysteine = S-adenosyl-L-homocysteine + S-methyl-L-cysteine
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S-adenosyl-L-methionine + L-cysteine = S-methyl-L-cysteine + S-adenosyl-L-homocysteine
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5-L-glutamyl-4-nitroanilide + L-cysteine = 4-nitroaniline + 5-L-glutamyl-L-cysteine
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thiamine + L-cysteine = 4-methyl-5-(2-hydroxyethyl)-thiazole + 2-[[(4-amino-2-ethylpyrimidin-5-yl)methyl]amino]-3-mercaptopropanoic acid
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L-cysteine + dithiothreitol = S-(2,3-hydroxy-4-thiobutyl)-L-cysteine + H2S
-
O-acetyl-L-homoserine + L-cysteine = L-cystathionine + acetate
-
O-phospho-L-homoserine + L-cysteine = L-cystathionine + phosphate
-
O-succinyl-L-homoserine + L-cysteine = L-cystathionine + succinate
34706, 637424, 637425, 637427, 637428, 637429, 637430, 637431, 637432, 637433, 637437, 637443, 637444, 637423, 672232, 673497, 723726, 637446, 637426, 637449, 637452, 637457, 660307, 666989, 676404, 676507, 637439, 637440, 637453, 676544, 637434, 660344, 637454, 637455, 637456, 637458, 657952
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L-cysteine + phenylpyruvate = 3-mercapto-2-oxopropanoate + L-phenylalanine
-
L-cysteine + 2-oxobutanoate = 2-aminobutanoate + 3-mercapto-2-oxopropanoate
-
L-cysteine + 'activated' tRNA = L-serine + tRNA containing a thionucleotide
-
L-cysteine + Bacillus subtilis 'activated' tRNA = L-serine + tRNA containing a thionucleotide
-
L-cysteine + Bos taurus 'activated' tRNA = L-serine + tRNA containing a thionucleotide
-
L-cysteine + E. coli 'activated' tRNA = L-serine + tRNA containing a thionucleotide
-
L-cysteine + rabbit liver 'activated' tRNA = L-serine + tRNA containing a thionucleotide
-
L-cysteine + Rattus norvegicus brain 'activated' tRNA = L-serine + tRNA containing a thionucleotide
-
L-cysteine + Rattus norvegicus liver 'activated' tRNA = L-serine + tRNA containing a thionucleotide
-
L-cysteine + Saccharomyces cerevisiae 'activated' tRNA = L-serine + tRNA containing a thionucleotide
-
L-cysteine + acceptor = L-alanine + S-sulfanyl-acceptor
737594, 738601, 738144, 737643, 739016, 739655, 739090, 760243, 737375, 739453, 738590, 761583, 760286
-
L-cysteine + N,N-dimethyl-4-phenylenediamine = L-alanine + N,N-dimethyl-4-phenylenediamine sulfate
-
L-cysteine + [enzyme]-cysteine = L-alanine + [enzyme]-S-sulfanylcysteine
645619, 724057, 645615, 645616, 645627, 645628, 645630, 645632, 645633, 645634, 645635, 645638, 725215, 726333, 645624, 645631, 645636, 645621, 702269, 645640, 726016, 645620, 703682, 726296, 706851, 704679
-
molybdenum cofactor + L-cysteine + H+ = thio-molybdenum cofactor + L-alanine + H2O
-
molybdenum cofactor + L-cysteine + reduced acceptor + 2 H+ = thio-molybdenum cofactor + L-alanine + H2O + oxidized acceptor
-
MoO2(OH)Dtpp-mP + L-cysteine + 2 H+ = MoOS(OH)Dtpp-mP + L-alanine + H2O
-
3'-phosphoadenylylsulfate + cysteine = adenosine 3',5'-bisphosphate + 2-amino-3-sulfosulfanyl-propionic acid
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L-Cysteine + 2-mercaptoethanol = HOOC-CH(NH2)-CH2-S-CH2-CH2OH + H2S
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L-cysteine + L-homocysteine = L-cystathionine + H2S
-
L-cysteine + H2O = sulfide + NH3 + pyruvate
707582, 708059, 708300, 708397, 708627, 709608, 710627, 693241, 695079, 707333, 709005, 709040, 709390, 709539, 710063, 710421, 690781, 691828, 691972, 692207, 693818, 693936, 694398, 708133, 708411, 709212, 709676, 709778, 692223, 694364, 708240, 650640, 709711, 691353, 710321, 691890, 690376, 690377, 649609, 652626, 664075, 665558, 690967, 653162, 665587, 671325, 708517, 693730, 651351
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L-cysteine + H2O = sulfide + NH3 + pyruvate
-
L-cysteine + H2O = sulfide + NH3 + pyruvate
-
L-cysteine + HCN = H2S + L-3-cyanoalanine
34722, 34716, 34723, 34724, 34727, 34728, 34729, 34725, 34719, 34718, 34720, 34730, 34735, 34726, 704926, 34721, 706135, 34733, 34734, 34736, 34717, 34731, 34732, 682356
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L-cysteine + HCN = sulfide + L-3-cyanoalanine
-
L-cysteine + hydrogen cyanide = hydrogen sulfide + L-3-cyanoalanine
-
ATP + L-cysteine + tRNA = AMP + diphosphate + L-cysteinyl-tRNA
-
ATP + L-cysteine + tRNAPro = AMP + diphosphate + L-cysteinyl-tRNAPro
-
ATP + L-cysteine + tRNA3CysC20U/U21C/A44U/C46A/A47G = AMP + diphosphate + L-cysteinyl-tRNA3CysC20U/U21C/A44U/C46A/A47G
-
ATP + L-cysteine + tRNA3CysC20U/U21C/A44U/C46A/A47G/G57A = AMP + diphosphate + L-cysteinyl-tRNA3CysC20U/U21C/A44U/C46A/A47G/G57A
-
ATP + L-cysteine + tRNACys = AMP + diphosphate + L-cysteinyl-tRNACys
187, 190, 191, 58, 653867, 745862, 179, 181, 185, 188, 195, 649098, 652821, 652909, 661203, 662024, 689145, 180, 184, 194, 675435, 192, 193, 92, 650423, 746197, 186, 746259, 672180, 653662, 650990, 662934, 675395, 727889, 745531, 746416, 182, 662647
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ATP + L-cysteine + tRNACys mutant = AMP + diphosphate + L-cysteinyl-tRNACys mutant
-
ATP + L-cysteine + tRNACysG15C/C48G = AMP + diphosphate + L-cysteinyl-tRNACysG15C/C48G
-
ATP + L-cysteine + tRNAGln duoble-mutant = AMP + diphosphate + L-cysteinyl-tRNAGln double-mutant
-
ATP + L-cysteine + tRNAGln mutant = AMP + diphosphate + L-cysteinyl-tRNAGln mutant
-
ATP + L-cysteine + holo-[L-cysteinyl-carrier protein] = AMP + diphosphate + L-cysteinyl-[L-cysteinyl-carrier protein]
-
1-O-(2-amino-2-deoxy-alpha-D-glucopyranosyl)-1D-myo-inositol + L-cysteine + ATP = 1-O-[2-(L-cysteinamido)-2-deoxy-alpha-D-glucopyranosyl]-1D-myo-inositol + AMP + diphosphate
-
ATP + L-Glu + L-Cys = ADP + phosphate + gamma-L-Glu-L-Cys
652480, 1145, 652979, 651393, 1118, 1120, 1126, 1127, 1141, 649189, 650595, 651813, 650634, 1143, 649413, 649660, 650713, 651391, 651996, 653993, 704665, 714265, 653714, 1119, 1121, 1122, 1123, 1124, 1125, 1129, 1130, 1132, 1133, 1134, 1135, 1136, 1138, 1139, 1144, 1147, 1150, 649315, 649525, 650330, 652304, 653987, 649263, 653272, 1131, 1137, 1149, 1128, 1142, 1148, 651896, 652192, 650135, 1140, 1146, 706061, 652649, 704660, 652341, 653171, 651392, 649655
-
ATP + N-methyl-L-glutarate + L-Cys = ADP + phosphate + N-methyl-L-glutaryl-L-Cys
-
ATP + threo-beta-hydroxy-L-Glu + L-Cys = ADP + phosphate + threo-beta-hydroxy-L-Glu-L-Cys
-
ATP + DL-alpha-aminoadipate + L-cysteine = ADP + phosphate + DL-aminoadipyl-L-cysteine
-
ATP + L-glutamate + L-cysteine = ADP + phosphate + gamma-L-glutamyl-L-cysteine
694060, 660892, 662412, 692055, 692058, 727274, 726910, 690385, 690387, 690440, 690630, 692442, 692444, 694609, 663435, 692437, 694485, 694674, 662339, 663074, 662457, 745900, 662512, 672367, 691912, 691909, 745490, 745745, 744070, 745492, 663122, 726912, 745805, 744469, 744853, 745888, 744122, 744438, 745734, 660680, 663215, 661811, 675918, 671927, 674643, 672053, 676524, 676435, 672904, 671223, 671216, 673803, 652192
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3 ATP + L-2-aminohexanedioate + L-cysteine + L-valine + H2O = 3 AMP + 3 diphosphate + N-[L-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine
-
6-oxopiperidine 2-carboxylic acid + L-cysteine + L-valine + ATP = N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine + AMP + diphosphate
-
L-2-aminoadipate + L-cysteine + L-allo-isoleucine + ATP = L-delta-(aminoadipyl)-L-cysteinyl-D-allo-isoleucine + AMP + diphosphate
-
L-2-aminoadipate + L-cysteine + L-isoleucine + ATP = L-delta-(aminoadipyl)-L-cysteinyl-D-isoleucine + AMP + diphosphate
-
L-2-aminoadipate + L-cysteine + L-valine + ATP = N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine + AMP + diphosphate
440075, 440085, 440086, 440084, 440082, 440073, 440074, 440076, 440077, 440078, 440079, 440080, 440083, 440081
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L-glutamate + L-cysteine + L-valine + ATP = L-glutamyl-L-cysteinyl-D-valine + AMP + diphosphate
-
S-carboxymethylcysteine + L-cysteine + L-valine + ATP = L-S-carboxymethylcysteinyl-L-cysteinyl-D-valine + AMP + diphosphate
-
ATP + (R)-4'-phosphopantothenate + L-Cys = (R)-4'-phosphopantothenoyl-L-cysteine + ADP + phosphate
-
CTP + (R)-4'-phosphopantothenate + L-Cys = (R)-4'-phosphopantothenoyl-L-cysteine + CDP + phosphate
-
CTP + (R)-4'-phosphopantothenate + L-cysteine = CMP + diphosphate + N-[(R)-4'-phosphopantothenoyl]-L-cysteine
-
ATP + (R)-4'-phosphopantothenate + L-cysteine = AMP + diphosphate + N-[(R)-4'-phosphopantothenoyl]-L-cysteine
-
CTP + (R)-4'-phosphopantothenate + L-cysteine = CMP + diphosphate + N-[(R)-4'-phosphopantothenoyl]-L-cysteine
-
Product in Enzyme-catalyzed Reactions (116 results)
EC NUMBER
REACTION
REACTION DIAGRAM
LITERATURE
ENZYME 3D STRUCTURE
O-acetyl-L-Ser + H2S = L-Cys + acetate
-
O-acetyl-L-serine + H2S = L-cysteine + acetic acid
-
[CysO sulfur-carrier protein]-Gly-NH-CH2-C(O)-S-L-cysteine + H2O = [CysO sulfur-carrier protein]-Gly-NH-CH2-COOH + L-cysteine
-
[CysO sulfur-carrier protein]-His10-L-Ala-NH-CH2-C(O)-S-L-cysteine + H2O = [CysO sulfur-carrier protein]-His-10-L-Ala-NH-CH2-COOH + L-cysteine
-
[CysO sulfur-carrier protein]-His10-L-Cys-NH-CH2-C(O)-S-L-cysteine + H2O = [CysO sulfur-carrier protein]-His-10-L-Cys-NH-CH2-COOH + L-cysteine
-
L-cysteinyl 7-amido-4-carbamoylmethylcoumarin + H2O = L-cysteine + 7-amino-4-carbamoylmethylcoumarin
-
O-acetyl-L-serine + sulfide = L-cysteine + acetate
-
CMP + diphosphate + N-[(R)-4'-phosphopantothenoyl]-L-cysteine = CTP + (R)-4'-phosphopantothenate + L-cysteine
-
Activator in Enzyme-catalyzed Reactions (327 results)
EC NUMBER
COMMENTARY
LITERATURE
ENZYME 3D STRUCTURE
restoring, also other sulfhydryl compounds, NADH-linked to a greater extent than the NADPH-linked activity
-
L-cysteine is associated with the highest boost in the rate of cyanide formation in the LPO/H2O2/acetonitrile system, achieving 156.7% of the rate of cyanide production of the control
-
addition of L-cysteine significantly enhances the rate of chloroacetonitrile oxidation and cyanide release by the myeloperoxidase/H2O2/Cl- system (45.4% increase at 5 mM)
-
protein expression of recombinant wild-type enzyme in HepG2/C3A cells increases by 160% when extracellular cysteine levels are increased from 0 to 1 mM cysteine
-
acts as an initial signal for regulation of the enzyme, upregulates enzyme activity
-
enzyme has a specific requirement for L-cysteine (6.7 mM), required to restore full activity after dialysis or treatment with chelating agents
-
in absence of thiols or ascorbate, no NO generation is detected from xanthine oxidase mediated organic nitrate reduction
-
essential for assay, interaction of enzyme with orotate or dihydroorotate is dependent on cysteine, whereas NADH oxidase activity is not
-
L-cysteine activates strongly, D-cysteine is also an activator, 1.8 mM L-cysteine is required at pH 8 for half-maximal activity, 10 mM for near-maximal activity
-
required for activation of purified enzyme, but not if crude extract is used for assay
-
recombinant enzyme FlaR (rFlaR) FAD-dependent NADP-reductase is activated in the presence of cysteine, cysteine significantly stimulates rFlaR NADP+-reductase activity
-
NADH-oxidation with free lipoic acid is strongly dependent on the addition of NAD+, EDTA, Mg2+ and cysteine, the reverse reaction with reduced lipoic acid and NAD+ does not show any requirement for cofactors
-
1 pair of redox active cysteines at the N-terminal active center and 1 pair of selenenylsulfide at the C-terminus, crucial for the reduction of thioredoxin
-
part of the active site
-
fungus is not able to use L-Cys as sulfur source instead of sulfate. Presence of L-Cys induces production of an excessive amount of both intracellular and extracellular enzyme
-
stimulates the activity via conformational changes that occur upon binding to the amino acid-binding-domain
-
intraperitoneal administration of 7 mg/kg/day for 14 days, increase in enzyme activity by 185% and increase of total antioxidant status. L-cysteine given before a toxic dose of cadmium results in increase of enzyme activity up to 85%, a total antioxidant status similar to the control values, and survival of the treated animals
-
concentrations of 0.05, 0.1, 0.4 and 0.7 mM are needed to reactivate both hexosaminidase activities of forms I, II, III and IV
-
presence decreases extent of inactivation by Hg2+, Ag2+, thimerosal or p-hydroxymercuribenzoate
-
activates
36625, 36647, 36619, 36636, 36638, 36654, 34988, 34989, 36652, 35024, 36629, 36623, 36656, 36658, 36653
-
cathepsin B is activated at 22°C for 5 min in 100 mM sodium acetate, 1 mM DTT, 2 mM EDTA, 4 mM cysteine, pH 5.5
-
for activation of actinidin, 52 mM L-cysteine is added to the sample and the preparation incubated for 1 h at 45°C
-
the enzyme is activated in 20 mM potassium phosphate buffer, pH 6.5 containing 52 mM L-cysteine and 2 mM EDTA (1:1 (v/v)) for 1 h at 45°C
-
the requirement for reducing conditions during the activation process is investigated with 20 mM DTT or 20 mM cysteine, propapain does not convert to papain even after prolonged incubation with DTT, whereas in presence of 20 mM cysteine, the activation occurs between 30 and 40 min at 50°C
-
10 mM, most effective reducing agent for activation of the enzyme, denaturation occurs at higher concentration above 5 mM
-
gingipains are activated by diluting to 10 mM in 0.2 M HEPES, pH 8.0, 5 mM CaCl2 and 10 mM cysteine, and incubation at 37°C for 10 min
-
gingipains are activated by diluting to 10 mM in 0.2 M HEPES, pH 8.0, 5 mM CaCl2 and 10 mM cysteine, and incubation at 37°C for 10 min
-
maximal activity in presence of various reducing compounds, e.g. Cys, 2,3-dimercaptopropanol, thioglycolic acid, glutathione
-
the action of FheCL1 is enhanced by glutathione, the major reducing agent found in red blood cells. In the presence of DTT, GSH and L-cysteine FheCL1 exhibited similar activation curves with maximal enzyme activity observed in the presence of each reducing agent at a concentration of 0.1 to 1.0 mM
-
effect of cysteine on arginase activity, effect of increasing concentrations of cysteine alone or in combination with iron (II) sulfate on the enhancement of arginase activity in human sickle erythrocytes or purified arginase-1 from Bos taurus liver
-
maximal activity only when both 8 mM Cys and 0.1 mM Fe2+ are present. Fe3+ or Mn2+ can replace Fe2+
-
cofactor system composed of Fe2+, cysteine and/or ascorbate functions under aerobic and anaerobic conditions, a second cofactor system with NADH/FMN requires anaerobic conditions
-
enzyme activity increases 2-4fold in presence of both Fe2+ and cysteine. 0.1-1 mM Fe2+ and 0.05-0.5 mM cysteine
-
low concentration of cellular cysteine leads to elevation of cystathionine gamma-lyase
-
enzyme activity depends on the presence of a reducing compound to a final concentration of 0.1mM
-
varying glutamic acid concentrations from 5 to 80 mM do not affect GCL activities markedly, whereas cysteine concentrations from 2.5 to 40 mM influence GCL activities substantially in a tissue-dependent manner, about 20 mM L-Cys is optimal in the different tissue, overview. After subacute exposure, low doses increases GCL activity and GSH content in liver by 48.3% and 54.4%, respectively. High doses reduce GCL activities significantly in liver and kidney to 31.2% and 43.0% of the control, respectively
-
varying glutamic acid concentrations from 5 to 80 mM do not affect GCL activities markedly, whereas cysteine concentrations from 2.5 to 40 mM influence GCL activities substantially in a tissue-dependent manner, about 20 mM L-Cys is optimal in the different tissue, overview. Low doses activate high doses inhibits the enzyme
-
200% increase of Cd2+ transport across plasma membranes at 50 mM. Cd transport across tonoplasts is stimulated up to 120% by 50 mM L-cysteine
-
millimolar concentration of Cys increase the activity about 800fold. Cys is a non-essential activator of the enzyme, interacting with the cytoplasmic side of the enzyme. K1/2 of 4 mM
-
isoform CtrA2 shows highest activity at 20 mM L-cysteine, isoform CtrA3 shows highest activity at 15 mM L-cysteine
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Inhibitor in Enzyme-catalyzed Reactions (485 results)
EC NUMBER
COMMENTARY
LITERATURE
ENZYME 3D STRUCTURE
the addition of cysteine (more than 2 mM) inactivates human L-xylulose reductase and is accompanied by a 10fold decrease in catalytic efficiency, the activity of the cysteine-inactivated enzyme is not recovered by the addition of 10 mM dithiothreitol and 2-mercaptoethanol
-
strong effect on sorbitol oxidation, slight effect on fructose reduction, ZnSO4 reverses inhibition
-
competitive versus L-homoserine, uncompetitive versus cofactors NAD+ and NADP+. 95% inhibition at 10 mM. The feedback inhibition of StHSD by cysteine occurs through the formation of an enzyme-NAD-cysteine complex. Cysteine situates within the homoserine binding site, formation of a covalent bond between cysteine and the nicotinamide ring. Cysteine interacts with six residues (Gly156, Thr157, Tyr183, Glu185, Asp191, and Lys200) in the StHSD active site, binding structure analysis, overview
-
inhibition of tyrosinase-catalyzed enzymatic browning by trapping the dopaquinone intermediate with cysteine or ascorbic acid, overview
-
competitive with 4-methylcatechol, catechol or pyrogallol. IC50: 0.125 mM in reaction with 4-methylcatechol, IC50: 0.637 mM in reaction with pyrogallol, IC50: 0.15 mM in reaction with catechol
-
complete inhibition at 0.973 mM of the root enzyme, and at 1 mM of the pulp enzyme
-
1 mM, complete inhibition of native enzyme, about 30% inhibition of enzyme immobilized in xerogel matrix of trimethoxysilane and proplytetramethoxysilane
-
73% inhibition at 1 mM; 73% inhibition at 1 mM; 78% inhibition at 1 mM; 78% inhibition at 1 mM
-
0.15 mM, complete inhibition of membrane-bound isoform, 2 mM, complete inhibition of soluble isoform
-
weak competitive inhibitor, Cys can bind directly to the ADO iron center with formation of a low-spin (S=1/2) FeIII complex. The ratio of low-spin to high-spin ferric species can be modulated by the addition of glycerol, with the high-spin Cys-FeIII-ADO complex being the predominant form in the absence of a glassing agent
-
concentrations of cysteine of 2 mM and above are inhibitory in assays of purified cysteine dioxygenase
-
inhibition of tyrosinase-catalyzed enzymatic browning by trapping the dopaquinone intermediate with cysteine or ascorbic acid, overview
-
the phenoloxidase activity of HdPO is most sensitive to cysteine, complete inhibition at 10 mM
-
52% and 76% inhibition at 1 mM for the cv. Narince samples from 2006 and 2007, respectively
-
effects of inhibitors on mushroom PPO are determined by using pyrogallol as substrate
-
in descending order of inhibition potency: p-hydroxybenzoic acid > glutathione = ascorbic acid > L-cysteine > EDTA > citric acid
-
significantly inhibits PPO activity, evaluated for effectiveness as an inhibitor of PPO activity, using catechol as the substrate
-
competitive, binds at the serine substrate site, negatively regulates its own synthesis
-
0.03 mM, 0.5 mM, and 1 mM, strong inhibition, 5-500 microM L-cysteine in the presence of 0.5 mM L-serine inhibits the enzyme remarkably, much less but still significantly in the presence of 3 mM L-serine, 90% inhibition by 0.3 mM L-cysteine with 3 mM L-serine (as found in throphozoite culture), acetyl-CoA concentration influences the inhibitory efficiency as well; 0.5 mM inhibits by 75.3%, no inhibition with 0.03 mM, 1 mM not determined, 20% inhibition by 0.3 mM L-cysteine with 3 mM L-serine (as found in throphozoite culture); 1 mM, weak inhibition, no inhibition by 0.3 mM L-cysteine with 3 mM L-serine (as found in throphozoite culture) or at other L-cysteine concentrations from 10-1000 micoM in the presence of 3 mM L-serine
-
a feedback inhibitor, binding structure from crystal structure analysis of the enzyme-bound complex. A cysteine molecule bound at the active site pocket at the interface of two Kpn CysE subunits. Each Kpn CysE trimer in-houses three cysteine molecules at the equivalent sites related by a 3fold axis, that, in turn, are related to remaining 3 active sites by 2 fold symmetry. Cysteine at the interface of two subunits is stabilized by interactions from one subunit involving Asp92, Pro93 and Ala94 (residues of turn connecting alpha5 and alpha6 helices) and Asp157, His158 (residues of L?betaloop) as well as from Gly183, Gly184, Thr185, Arg192, His193 (residues of substrate binding loop) of the adjacent subunit. About 50% inhibition at 0.005 mM with 500 ng enzyme
-
competitive inhibition versus L-serine, noncompetitive inhibition versus acetyl-CoA
-
dead-end inhibitor, competitive against botn substrates in both reaction directions
-
feed-back inhibition of cytosolic isozyme SAT-c, not of mitochondrial and plastidic isozymes SAT-m and SAT-p
-
feedback inhibition, isoform Serat3,1, noncompetitive versus L-serine, competitive versus acetyl-CoA
-
feedback inhibition; feedback inhibition; feedback inhibition, isozyme SAT3 is almost insensitive to cysteine inhibition. A combination of comparative modeling, multiple molecular dynamics simulations and free energy calculation studies shows a difference in binding energies of wild-type isozyme SAT3 and of a S208H-SAT3 mutant for cysteine
-
feedback inhibition; feedback inhibition; feedback inhibition; feedback inhibition, isozyme VvSERAT2-1 is almost insensitive to cysteine inhibition
-
under physiological conditions L-cysteine specifically inhibits chloroplast enzyme activity, which is linked to the sulfate assimilation network. This metabolic feedback control does not apply to the enzyme activity located in cytosol
-
competitive, forms a nonproductive external aldimine with the pyridoxal 5'-phosphate cofactor
-
uncompetitive inhibition of phosphatase activity, mixed-competitive inhibition of inorganic pyrophosphatase activity. Inorganic pyrophosphatase activity is inhibited more than phosphatase activity. Ca2+ and Mg2+ ion concentrations may regulate this inhibition
-
5 mM, and 2.5 mM Fe2+, pH 5.0 or 6.5, strong inhibition of formation of allyl isothiocyanate
-
2 mM Zn2+ protects at 2 mM cysteine, protects partially at 10 mM cysteine, no protection at 20 mM cysteine
-
complete inhibition at 4 mM, reversal to 95% of initial activity by addition of Zn2+
-
cysteine is able to enter the active site of the enzyme, interact with the pyridoxal 5'-phosphate-lysine internal aldimine, form a cysteine-pyridoxal 5'-phosphate aldimine and undergo intramolecular nucleophilic cyclization through its sulfhydryl group, leading to irreversible inactivation. Reaction is similar for aspartate decarboxylase, glutamate decarboxylase and cysteine sulfinic acid decarboxylase
-
activity is decreased to 20% of the original by treatment with cysteine plus mercaptoethanol. Most of the loss is regained on incubation with pyridoxal 5'-phosphate
-
50 mM, complete inaction at basic pH in the presence of O2 is due to a covalent modification of the enzyme
-
competitive in the presence of EDTA; in the presence of Cd2+; irreversible in the presence of O2
-
12 mM, 65% inhibition after 5 min, 1 mM, 29% inhibition after 10 min, linear noncompetitive inhibitor
-
competitive inhibition of prolylation. A 40fold excess over L-proline concentration reduces the prolylation activity by 80%, no inhibition of mutant P100A
-
no inhibition of wild type enzyme, inhibits activity of D56A and D56E mutant enzymes
-
varying glutamic acid concentrations from 5 to 80 mM do not affect GCL activities markedly, whereas cysteine concentrations from 2.5 to 40 mM influence GCL activities substantially in a tissue-dependent manner, about 20 mM L-Cys is optimal in the different tissue, overview. After subacute exposure, low doses increases GCL activity and GSH content in liver by 48.3% and 54.4%, respectively. High doses reduce GCL activities significantly in liver and kidney to 31.2% and 43.0% of the control, respectively
-
varying glutamic acid concentrations from 5 to 80 mM do not affect GCL activities markedly, whereas cysteine concentrations from 2.5 to 40 mM influence GCL activities substantially in a tissue-dependent manner, about 20 mM L-Cys is optimal in the different tissue, overview. Low doses activate high doses inhibits the enzyme
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Metals and Ions (2 results)
EC NUMBER
COMMENTARY
LITERATURE
ENZYME 3D STRUCTURE
Enzyme Kinetic Parameters
kcat Value (Turnover Number) (203 results)
EC NUMBER
TURNOVER NUMBER [1/S]
TURNOVER NUMBER MAXIMUM [1/S]
COMMENTARY
LITERATURE
0.012
-
assay standart conditions are: the enzyme is incubated at 37°C in the presence of 62.5 mM Mes buffer (pH 6.1), 0.3 mM ferrous sulfate, 0.0125 mM bathocuproine disulfonate and 1.2 mM cysteine
0.12
-
20% cross-linked wild-type enzyme, pH 9.1, temperature not specified in the publication
0.25
-
60% cross-linked wild-type enzyme, pH 7.7, temperature not specified in the publication
0.33
-
not cross-linked wild-type enzyme, pH 7.7, temperature not specified in the publication
0.028
-
mutant A420Y, pH not specified in the publication, temperature not specified in the publication
0.047
-
mutant D52L, pH not specified in the publication, temperature not specified in the publication
0.049
-
mutant D52L/A420Y, pH not specified in the publication, temperature not specified in the publication
0.205
-
wild-type, pH not specified in the publication, temperature not specified in the publication
0.136
-
absence of Anabaena sulfur acceptor E, pH 7.4, temperature not specified in the publication