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hydrogen sulfide + ROOH = ?
-
H2S + NADH + H+ = H2 + NAD+
-
H2S + NADPH + H+ = H2 + NADP+
-
hydrogen sulfide + 3 NADP+ + 3 H2O = sulfite + 3 NADPH + 3 H+
-
hydrogen sulfide + NADP+ + H2O = sulfite + NADPH + H+
-
hydrogen sulfide + 2 ferricytochrome c = sulfur + 2 ferrocytochrome c + 2 H+
-
hydrogen sulfide + ferricytochrome c 555 = sulfur + ferrocytochrome c 555 + H+
-
hydrogen sulfide + oxidized flavocytochrome c = sulfur + reduced flavocytochrome c + H+
-
sulfide + oxidized benzyl viologen = sulfur + reduced benzyl viologen + H+
-
sulfide + oxidized cytochrome c = sulfur + reduced cytochrome c + H+
-
sulfide + oxidized flavocytochrome c = sulfur + reduced flavocytochrome c + H+
-
sulfide + oxidized heart cytochrome c = sulfur + reduced heart cytochrome c + H+
-
sulfide + oxidized horse cytochrome c = sulfur + reduced horse cytochrome c + H+
-
sulfide + oxidized Nitrosomonas europaea cytochrome c552 = sulfur + reduced Nitrosomonas europaea cytochrome c552 + H+
-
sulfide + oxidized Rhodospirillum rubrum cytochrome c2 = sulfur + reduced Rhodospirillum rubrum cytochrome c2
-
sulfide + O2 = sulfur + H2O2
-
Abz-SAL-3-oxo-L-Ala-SPTRA-NH2 + O2 + hydrogen sulfide + oxidized dithiothreitol = ?
-
Ac-AL-3-oxo-L-Ala-TPSRGSLFTGR-NH2 + hydrogen sulfide + oxidized dithiothreitol + H2O = ?
-
2 sulfide + ubiquinone-1 = hydrogen disulfide + ubiquinol-1
-
HS- + quinone = polysulfide + quinol
-
sulfide + 2,3-dimethyl-1,4-naphthoquinone = sulfur + 2,3-dimethyl-1,4-naphthoquinol
-
sulfide + 2-methyl-3-methylthio-1,4-naphthoquinone = sulfur + 2-methyl-3-methylthio-1,4-naphthoquinol
-
sulfide + caldariellaquinone = sulfur + caldariellaquinol
-
sulfide + coenzyme Q = sulfane sulfur + reduced coenzyme Q
-
sulfide + coenzyme Q = sulfur + reduced coenzyme Q
-
sulfide + coenzyme Q1 = sulfur + reduced coenzyme Q1
-
sulfide + coenzyme Q10 = sulfur + reduced coenzyme Q10
-
sulfide + cyanide + coenzyme Q = thiocyanate + reduced coenzyme Q
-
sulfide + cyanide + ubiquinone-1 = thiocyanate + ubiquinol-1
-
sulfide + cysteine + coenzyme Q1 = cysteine persulfide + reduced coenzyme Q1
-
sulfide + decylubiquinone + cyanide = sulfur + decylubiquinol + thiocyanate
-
sulfide + decylubiquinone + Escherichia coli thioredoxin = sulfur + decylubiquinol + ?
-
sulfide + decylubiquinone + sulfite = sulfur + decylubiquinol + ?
-
sulfide + decylubiquinone = polysulfide + decylubiquinol
-
sulfide + decylubiquinone = sulfur + decylubiquinol
714148, 713985, 714310, 742453, 714172, 727080, 742790, 742387, 715434, 715911, 741767, 742250, 716746, 742883, 742540
-
sulfide + duroquinone 23 = sulfur + duroquinol 23
-
sulfide + duroquinone = sulfur + duroquinol
-
sulfide + glutathione = sulfur + reduced glutathione
-
sulfide + homocysteine + coenzyme Q1 = homocysteine persulfide + reduced coenzyme Q1
-
sulfide + menadione = polysulfide + menadiol
-
sulfide + menadione = sulfur + menadiol
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sulfide + plastoquinone-1 = sulfur + plastoquinol-1
-
sulfide + plastoquinone-2 = sulfur + plastoquinol-2
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sulfide + quinone = elemental sulfur + quinol
-
sulfide + quinone = sulfur + quinol
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sulfide + reduced glutathione + coenzyme Q1 = glutathione persulfide + reduced coenzyme Q1
-
sulfide + sulfide + coenzyme Q = hydrogen disulfide + reduced coenzyme Q
-
sulfide + sulfite + coenzyme Q = thiosulfate + reduced coenzyme Q
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sulfide + sulfite + ubiquinone-1 = thiosulfate + ubiquinol-1
-
sulfide + ubiquinone = ? + ubiquinol
-
sulfide + ubiquinone-1 = sulfur + ubiquinol-1
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sulfide + ubiquinone-2 = sulfur + ubiquinol-2
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sulfide + ubiquinone-4 = sulfur + ubiquinol-4
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sulfide + ubiquinone-9 = sulfur + ubiquinol-9
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sulfite + hydrogen sulfide + menaquinone = thiosulfate + menaquinol
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hydrogen sulfide + CoA + coenzyme Q1 = CoA-SSH + H+ + reduced coenzyme Q1
-
hydrogen sulfide + coenzyme Q1 = hydrogen disulfide + reduced coenzyme Q1
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hydrogen sulfide + coenzyme Q2 = ?
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hydrogen sulfide + cysteine + coenzyme Q1 = ?
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hydrogen sulfide + glutathione + a quinone = S-sulfanylglutathione + a quinol
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hydrogen sulfide + glutathione + coenzyme Q = S-sulfanylglutathione + reduced coenzyme Q
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hydrogen sulfide + glutathione + coenzyme Q1 = ?
-
hydrogen sulfide + glutathione + coenzyme Q1 = glutathione persulfide + H+ + reduced coenzyme Q1
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hydrogen sulfide + glutathione + coenzyme Q1 = S-sulfanylglutathione + reduced coenzyme Q1
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hydrogen sulfide + glutathione + coenzyme Q10 = S-sulfanylglutathione + reduced coenzyme Q10
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hydrogen sulfide + glutathione + decylubiquinone = S-sulfanylglutathione + decylubiquinol
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hydrogen sulfide + glutathione + quinone = S-sulfanylglutathione + quinol
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hydrogen sulfide + glutathione + ubiquinone = S-sulfanylglutathione + ubiquinol
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hydrogen sulfide + homocysteine + coenzyme Q1 = ?
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hydrogen sulfide + sulfide + coenzyme Q = ?
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hydrogen sulfide + sulfide + coenzyme Q1 = ?
-
hydrogen sulfide + sulfite + coenzyme Q = ?
-
hydrogen sulfide + sulfite + coenzyme Q1 = thiosulfate + reduced coenzyme Q1
-
hydrogen sulfide + sulfide + coenzyme Q = ?
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hydrogen sulfide + sulfide + coenzyme Q1 = ?
-
sulfide + coenzyme Q2 = ?
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sulfide + ubiquinone = ?
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hydrogen sulfide + 6 oxidized ferredoxin I [iron-sulfur] cluster + 3 H2O = sulfite + 6 reduced ferredoxin I [iron-sulfur] cluster + 6 H+
-
hydrogen sulfide + 6 oxidized ferredoxin [iron-sulfur] cluster + 3 H2O = sulfite + 6 reduced ferredoxin [iron-sulfur] cluster + 6 H+
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hydrogen sulfide + 6 oxidized methyl viologen [iron-sulfur] cluster + 3 H2O = sulfite + 6 reduced methyl viologen [iron-sulfur] cluster + 6 H+
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hydrogen sulfide + oxidized ferredoxin + H2O = sulfite + reduced ferredoxin + H+
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hydrogen sulfide + oxidized methyl viologen + H2O = sulfite + reduced methyl viologen + H+
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peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + 2 H2S = peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + HS-SH
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hydrogen sulfide + a [DsrC protein]-disulfide + acceptor + H2O = sulfite + a [DsrC protein]-dithiol + reduced acceptor + H+
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bisulfide + S-adenosyl-L-methionine = methanethiol + S-adenosyl-L-homocysteine
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H2S + S-adenosyl-L-methionine = methanethiol + S-adenosyl-L-homocysteine
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S-adenosyl-L-methionine + HS- = ?
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S-adenosyl-L-methionine + HS- = S-adenosyl-L-homocysteine + CH3SH
-
SH- + S-adenosyl-L-methionine = CH3SH + S-adenosyl-L-homocysteine
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acetyl-CoA + hydrogen sulfide = CoA + thioacetate
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NAD+ + glycine + sulfide = nicotinamide + ADP-5-ethyl-4-methylthiazole-2-carboxylate + 3 H2O
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O-acetyl-L-serine + sulfide = 2-amino-3-sulfanylpropanoic acid + acetate
-
O-acetyl-L-serine + sulfide = L-cysteine + acetate
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monofluoralanine + H2S = ?
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O-acetyl-L-Ser + H2S = L-Cys + acetate
637347, 637381, 637390, 637391, 637326, 637383, 637382, 676961, 33982, 486775, 637350, 637378, 637354, 637388, 637379, 637385, 674625, 637387, 674844, 676401, 637342, 637353, 637384, 637386, 637352, 759559, 721382, 759954, 758861, 637328, 671160, 674254, 676569, 672024, 671031
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O-acetyl-L-serine + H2S = L-cysteine + acetic acid
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O-acetylhomoserine + H2S = homocysteine + ?
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O-phosphoserine + H2S = L-Cys + phosphate
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O-acetyl-L-Ser + hydrogen sulfide = L-Cys + acetate
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O-acetyl-L-serine + hydrogen sulfide = L-cysteine + acetate
737768, 737868, 738985, 738249, 738846, 739486, 661211, 739348, 738828, 739490, 737462, 737472, 739364, 739756, 738292, 737756, 756864, 721306
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O3-acetyl-L-serine + hydrogen sulfide = L-cysteine + acetate
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O3-acetyl-L-serine + hydrogensulfide = L-cysteine + acetate
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chloroalanine + sulfide = cysteine + chloride
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L-homoserine + sulfide = ?
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O-acetyl-L-Ser + sulfide = L-Cys + acetate
637351, 637327, 486775, 637385, 637329, 637356, 637363, 637365, 637331, 34691, 637345, 637347, 637326, 637328, 637330, 637384, 637386, 637337, 637364, 637339
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O-acetyl-L-serine + sulfide = L-Cys + acetate
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O-diazoacetyl-L-serine + sulfide = ?
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O-succinyl-L-homoserine + sulfide = ?
-
O3-acetyl-L-serine + sulfide = L-cysteine + acetate
-
O-succinyl-L-homoserine + H2S = L-homocysteine + succinate
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2 O-acetyl-L-homoserine + H2S = 2 L-homocysteine + 2 acetate
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L-homoserine + H2S = homocysteine + ?
-
L-homoserine + H2S = L-homocysteine + H2O
-
L-serine + H2S = L-cysteine + H2O
-
o-acetyl-L-homoserine + H2S = L-homocysteine + acetate
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O-acetyl-L-homoserine + H2S = L-homocysteine + acetic acid
637329, 637331, 637825, 637835, 671277, 637836, 637823, 637824, 34702, 637834, 637832, 637830, 637841
-
O-acetyl-L-serine + H2S = L-cysteine + acetic acid
-
O-acetyl-L-serine + H2S = S-methylcysteine + ?
-
O-phospho-L-serine + H2S = ?
-
O-phosphoryl-L-serine + H2S = L-cysteine + H2O
-
O-succinyl-L-homoserine + H2S = homocysteine + ?
-
O-succinyl-L-homoserine + H2S = L-homocysteine + succinate
-
O-acetyl-L-homoserine + hydrogen sulfide = L-homocysteine + acetate
-
3-chloro-L-alanine + hydrogen sulfide = ?
-
L-azaserine + hydrogen sulfide = ?
-
O-acetyl-L-serine + hydrogen sulfide = L-cysteine + acetate
-
O-phospho-L-serine + hydrogen sulfide = L-cysteine + phosphate
-
O3-phospho-L-serine + hydrogen sulfide = L-cysteine + phosphate
-
3-chloro-L-alanine + sulfide = ?
-
L-azaserine + sulfide = ?
-
O-acetyl-L-serine + sulfide = L-cysteine + acetic acid
-
O-phospho-L-serine + sulfide = L-cysteine + phosphate
-
O-phospho-L-seryl-tRNACys + sulfide = L-cysteinyl-tRNACys + phosphate
-
O-phospho-L-seryl-tRNASec + sulfide = L-cysteinyl-tRNASec + phosphate
-
H2S + cyanide = thiocyanate
-
hydrogen sulfide + L-aspartate 4-semialdehyde + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ = L-homocysteine + H2O + 2 oxidized ferredoxin [iron-sulfur] cluster
-
sulfide + tRNA-uridine = tRNA-4-thiouridine
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sulfide + [tRNACys]-uridine = [tRNACys]-4-thiouridine
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sulfide + adenylated-tRNA-uridine(position8) = tRNA-4-thiouridine(position8) + ?
-
3-phospho-L-serine + sulfide = ?
-
L-Seryl-tRNASec + sulfide = ?
-
horse heart cytochrome c + sulfide = ?
-
L-serine + H2S = L-cysteine
-
O-acetyl-L-serine + H2S = L-cysteine + acetic acid
-
L-Serine + HS- = Cysteine + OH-
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O-Acetyl-L-serine + H2S = Cysteine + acetate
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O-acetyl-D-serine + sulfide = D-cysteine + ?
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O-acetylserine + H2S = cysteine + acetic acid
-
chloroalanine + sulfide = L-cysteine + Cl-
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O-acetyl-L-serine + sulfide = L-cysteine + acetate
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3-chloro-D-alanine + H2S = D-cysteine + HCl
-
ATP + sulfide + a [methyl-coenzyme M reductase alpha-subunit McrA]-glycine465 = ADP + phosphate + a [methyl-coenzyme M reductase alpha-subunit McrA]-thioglycine465
-
ATP + sulfide + GGRLGFYGYDLQD = ADP + phosphate + GGRLGFY(thioglycine)YDLQD
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ATP + sulfide + RLGFFGFDLQD = ADP + phosphate + RLGFF(thioglycine)FDLQD
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ATP + sulfide + [methyl-coenzyme M reductase alpha-subunit McrA]-glycine = ADP + phosphate + [methyl-coenzyme M reductase alpha-subunit McrA]-thioglycine
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ATP + sulfide + [methyl-coenzyme M reductase alpha-subunit McrA]-glycine465 = ADP + phosphate + [methyl-coenzyme M reductase alpha-subunit McrA]-thioglycine465
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disulfide + electron donor = H2S
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H2 + benzyl viologen = H2S + reduced benzyl viologen
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H2 + methyl viologen = H2S + reduced methyl viologen
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H2 + NADP+ = H2S + NADPH + H+
-
H2 + polysulfide(n) = H2S + polysulfide(n-1)
-
organic trisulfides + electron donor = H2S + oxidized electron donor
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polysulfide + electron donor = H2S + oxidized electron donor
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sulfur + electron donor = H2S + oxidized electron donor
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tetrasulfide + electron donor = H2S + oxidized electron donor
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5 sulfur + 2 O2 + 2 H2O + 4 H+ = sulfite + thiosulfate + 2 sulfide
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4 sulfur + 4 H2O + O2 = 2 hydrogen sulfide + 2 bisulfite + 2 H+
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4 sulfur + 4 H2O + O2 = 2 hydrogen sulfide + 2 HSO3- + 2 H+
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4 sulfur + 4 H2O + O2 = 2 hydrogen sulfide + 2 sulfite
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S + O2 + H2O = HSO3- + H2S + H+
-
S + O2 = SO32- + S2O32- + H2S
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S + OH- + O2 = HSO3- + S2O32- + HS- + H+
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reduced ferredoxin + H+ + SCN- + ATP = oxidized ferredoxin + H2S + HCN + ADP + phosphate
reduced ferredoxin + H+ + SCN- + ATP = oxidized ferredoxin + H2S + HCN + ADP + phosphate
reduced ferredoxin + H+ + SCN- + ATP = oxidized ferredoxin + H2S + HCN + ADP + phosphate
reduced ferredoxin + H+ + SCN- + ATP = oxidized ferredoxin + H2S + HCN + ADP + phosphate
reduced ferredoxin + H+ + SCN- + ATP = oxidized ferredoxin + H2S + HCN + ADP + phosphate
reduced ferredoxin + H+ + SCN- + ATP = oxidized ferredoxin + H2S + HCN + ADP + phosphate
cypemycin(1-18)-L-Cys-L-Leu-L-Val-L-Cys + acceptor = C3.19,S21-cyclocypemycin(1-18)-L-Ala-L-Leu-N-thioethenyl-L-valinamide + CO2 + H2S + reduced acceptor
-
sulfite + 6 ferrocytochrome c + 6 H+ = H2S + 3 H2O + 6 ferricytochrome c
-
sulfite + reduced methyl viologen + H+ = H2S + oxidized methyl viologen + H2O
-
sulfite + reduced methyl viologen = H2S + oxidized methyl viologen + H2O
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sulfite + ? = sulfide + ?
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polysulfide(n) + NADPH + H+ = hydrogen sulfide + polysulfide(n-1) + NADP+
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sulfur + NAD(P)H + H+ = hydrogen sulfide + NAD(P)+
-
sulfur + NADH + H+ = hydrogen sulfide + NAD+
-
sulfur + NADPH + H+ = hydrogen sulfide + NADP+
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(sulfide)n+1 + NADPH + H+ = hydrogen sulfide + (sulfide)n + NADP+
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sulfite + 3 NADPH + 3 H+ = hydrogen sulfide + 3 NADP+ + 3 H2O
-
sulfite + NADPH = hydrogen sulfide + NADP+ + H2O
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sulfite + NADPH + H+ = sulfide + NADP+ + H2O
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sulfite + NADPH = sulfide + NADP+ + H2O
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sulfite + reduced F420 = sulfide + oxidized F420
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thiosulfate + 2 ferrocytochrome c3 = sulfite + hydrogen sulfide + 2 ferricytochrome c3
thiosulfate + reduced methyl viologen = sulfite + hydrogen sulfide + oxidized methyl viologen
sulfur + reduced benzyl viologen + H+ = sulfide + oxidized benzyl viologen
-
thiosulfate + 2 ferrocytochrome c3 = sulfite + hydrogen sulfide + 2 ferricytochrome c3
-
thiosulfate + reduced benzyl viologen = sulfite + hydrogen sulfide + oxidized benzyl viologen
-
thiosulfate + reduced methyl viologen = sulfite + hydrogen sulfide + oxidized methyl viologen
-
ethyl mercaptan + O2 + H2O = acetaldehyde + H2S + H2O2
-
methanethiol + O2 + H2O = formaldehyde + H2S + H2O2
-
methanethiol + O2 + H2O = formaldehyde + hydrogen sulfide + H2O2
-
a [sulfatase]-L-cysteine + O(2) + a thiol = a [sulfatase]-3-oxo-L-alanine + hydrogen sulfide + a disulfide + H2O
-
a [sulfatase]-L-cysteine + O2 + 2 a thiol = a [sulfatase]-3-oxo-L-alanine + hydrogen sulfide + a disulfide + H2O
-
a [sulfatase]-L-cysteine + O2 + a thiol = a [sulfatase]-3-oxo-L-alanine + hydrogen sulfide + a disulfide + H2O
-
Abz-ATTPLCGPSRASILSGR + O2 + reduced dithiothreitol = ? + hydrogen sulfide + oxidized dithiothreitol + H2O
-
Abz-SALCSPTRA-NH2 + O2 + reduced dithiothreitol = Abz-SAL-3-oxo-L-Ala-SPTRA-NH2 + H2O + hydrogen sulfide + oxidized dithiothreitol
-
Ac-EQSCTAGRAAFITGQGLCTPSRAG-NH2 + O2 + reduced dithiothreitol = ? + hydrogen sulfide + oxidized dithiothreitol + H2O
-
Ac-LCSPSRGSLFTGR-NH2 + O2 + reduced dithiothreitol = Ac-L-3-oxo-L-Ala-SPSRGSLFTGR-NH2 + H2O + hydrogen sulfide + oxidized dithiothreitol
-
AC-MTDFYVPVSLCTPSRAALLTGRS-amide + O2 + reduced dithiothreitol = AC-MTDFYVPVSL-3-oxo-Ala-TPSRAALLTGRS-amide + H2O + hydrogen sulfide + oxidized dithiothreitol
-
[arylsulfatase A]-L-cysteine69 + O2 + reduced acceptor = [arylsulfatase A]-Calpha-formylglycine69 + hydrogen sulfide + acceptor
-
LCSPSRGSLFTGR + O2 + dithiothreitol = leucyl-formylglycyl-SPSRGSLFTGR + sulfide + oxidized dithiothreitol + H2O
-
thiosulfate + menaquinol = sulfite + hydrogen sulfide + menaquinone
-
sulfur + reduced methyl viologen + H2O = H2S + oxidized methyl viologen
-
sulfite + reduced ferredoxin + H+ = hydrogen sulfide + oxidized ferredoxin + H2O
-
sulfite + reduced ferredoxin = hydrogen sulfide + oxidized ferredoxin + H2O
-
sulfite + reduced methyl viologen + H+ = hydrogen sulfide + oxidized methyl viologen + H2O
-
sulfite + 3 FMNH2 = sulfide + 3 FMN + 3 H2O
-
sulfite + methyl viologen = sulfide + ?
-
sulfite + reduced coenzyme F420 = sulfide + oxidized coenzyme F420
-
sulfite + reduced ferredoxin + 6 H+ = sulfide + oxidized ferredoxin + 3 H2O
-
sulfite + reduced coenzyme F420 = hydrogen sulfide + oxidized coenzyme F420
sulfite + reduced methyl viologen = hydrogen sulfide + oxidized methyl viologen
Ac-AVPSCIPSRASILTGM-NH2 + S-adenosyl-L-methionine + dithionite = Ac-AVPS-3-oxo-L-Ala-IPSRASILTGM-NH2 + L-methionine + 5'-deoxyadenosine + sulfur dioxide + hydrogen sulfide
-
Ac-FENAYTAVPSCIASRASILTGMS-NH2 + S-adenosyl-L-methionine + reduced acceptor = Ac-FENAYTAVPS-3-oxo-L-Ala-IASRASILTGMS-NH2 + L-methionine + 5'-deoxyadenosine + acceptor + hydrogen sulfide
-
Ac-FENAYTAVPSCIASRASILTMSQ-NH2 + S-adenosyl-L-methionine + dithionite = Ac-FENAYTAVPS-3-oxo-L-Ala-IASRASILTMSQ-NH2 + L-methionine + 5'-deoxyadenosine + sulfur dioxide + hydrogen sulfide
-
Ac-YTAVPSCIPSRASILTGM + S-adenosyl-L-methionine + dithionite = Ac-YTAVPS-3-oxo-L-Ala-IPSRASILTGM + L-methionine + 5'-deoxyadenosine + sulfur dioxide + hydrogen sulfide
-
Ac-YYTSPMCAPARSMLLTGN + S-adenosyl-L-methionine = Ac-YYTSPM-3-oxo-L-Ala-APARSMLLTGN + L-methionine + 5'-deoxyadenosine + sulfur dioxide + hydrogen sulfide
-
Tyr-Tyr-Thr-Ser-Pro-Met-Cys-Ala-Pro-Ala-Arg-Ser-Met-Leu-Leu-Thr-Gly-Asn + S-adenosyl-L-methionine = Tyr-Tyr-Thr-Ser-Pro-Met-3-oxo-L-Ala-Ala-Pro-Ala-Arg-Ser-Met-Leu-Leu-Thr-Gly-Asn + L-methionine + 5'-deoxyadenosine + sulfur dioxide + hydrogen sulfide
-
sulfite + a [DsrC protein]-dithiol + 2 reduced ferredoxin + 2 H+ = hydrogen sulfide + a [DsrC protein]-disulfide + 2 oxidized ferredoxin + 3 H2O
-
sulfite + 6 ferrocytochrome c + 6 H+ = sulfide + 6 ferricytochrome c + 3 H2O
-
methanethiol + a [Co(I) methylated-thiol-specific corrinoid protein] = a [methyl-Co(III) methylated-thiol-specific corrinoid protein] + hydrogen sulfide
-
methanethiol + coenzyme M = methyl-CoM + hydrogen sulfide
-
2 L-cysteine = (2R,2'R)-3,3'-sulfanediylbis(2-aminopropanoic acid) + H2S
-
cysteine + CN- = cyanoalanine + H2S
-
L-Cys + acetate = O-acetyl-L-Ser + H2S
-
L-Cys + dithiothreitol = beta-cyanoalanine + H2S
-
L-cysteine + cyanide = cyanoalanine + H2S
-
L-cysteine + dithiothreitol = S-(2,3-hydroxy-4-thiobutyl)-L-cysteine + H2S
-
L-cysteine + H2O = L-serine + H2S
-
L-cysteine + L-cysteine = L-lanthionine + H2S
-
L-cysteine + L-homocysteine = L-cystathionine + H2S
-
cyanide + cysteine = beta-cyanoalanine + sulfide
-
L-homocysteine + KCN = gamma-cyano-alpha-aminobutyric acid + H2S
-
L-cysteine + dithiothreitol = S-(2,3-hydroxy-4-thiobutyl)-L-cysteine + sulfide
-
cysteine + cyanide = cyanoalanine + H2S
-
thiosulfate + 2 glutathione = sulfite + glutathione disulfide + sulfide
-
3-mercaptopyruvate + cyanide = H2S + ?
-
3-mercaptopyruvate + thiosulfate = pyruvate + H2S
-
[3-mercaptopyruvate sulfurtransferase]-S-sulfanyl-L-cysteine + reduced thioredoxin = hydrogen sulfide + [3-mercaptopyruvate sulfurtransferase]-L-cysteine + oxidized thioredoxin
-
thiosulfate + glutathione = sulfite + glutathione disulfide + sulfide
-
thiosulfate + NAD(P)H = H2S + NAD(P)+ + sulfite
-
thiosulfate + NADH = H2S + NAD+ + sulfite
-
thiosulfate + 2 dithioerythritol = sulfite + dithioerythritol disulfide + sulfide
-
thiosulfate + 2 dithiothreitol = sulfite + dithiothreitol disulfide + sulfide
-
thiosulfate + dithiothreitol = sulfite + oxidized dithiothreitol + sulfide
-
thiosulfate + menaquinol = sulfite + oxidized menaquinol + sulfide
-
thiosulfate + methylviologen = sulfide + ?
-
L-cysteine = L-alanine + sulfide
-
L-cysteine = L-alanine + H2S
-
L-cysteine + acceptor = L-alanine + sulfide + ?
-
L-cysteine = L-alanine + sulfide
-
[protein]-N6-(octanoyl)-L-lysine + an [Fe-S] cluster scaffold protein carrying a [4Fe-4S]2+ cluster + 2 S-adenosyl-L-methionine + 2 oxidized [2Fe-2S] ferredoxin + 6 H+ = [protein]-N6-[(R)-dihydrolipoyl]-L-lysine + an [Fe-S] cluster scaffold protein + 2 sulfide + 4 Fe3+ + 2 L-methionine + 2 5'-deoxyadenosine + 2 reduced [2Fe-2S] ferredoxin
-
L-cysteine = L-alanine + H2S
-
L-cysteine methyl ester = L-alanine methyl ester + H2S
-
carbon disulfide + 2 H2O = CO2 + 2 hydrogen sulfide
-
carbonyl sulfide + H2O = CO2 + H2S
-
carbonyl sulfide + H2O = CO2 + hydrogen sulfide
-
carbonyl sulfide + H2O = hydrogen sulfide + CO2
-
benzoyl-thiocarbamic acid + H2O = N-benzoyl-Gly + SH2
-
D-cysteine + H2O = sulfide + NH3 + pyruvate
-
CS2 + 2 H2O = CO2 + 2 H2S
CS2 + 2 H2O = CO2 + 2 H2S
2 L-cysteine = (2R,2'R)-3,3'-sulfanediylbis(2-aminopropanoic acid) + H2S
-
L-Cysteine + 1-mercapto-2-propanol = HOOC-CH(NH2)-CH2-S-CH2-CH(OH)-CH3 + H2S
-
L-Cysteine + 2-mercaptoethanol = HOOC-CH(NH2)-CH2-S-CH2-CH2OH + H2S
-
L-cysteine + 2-mercaptoethanol = S-hydroxyethyl-L-cysteine + H2S
-
L-Cysteine + DL-homocysteine = Cystathionine + H2S
-
L-cysteine + H2O = L-serine + H2S
-
L-cysteine + L-homocysteine = L-cystathionine + H2S
-
L-cysteine = H2S + L-serine
-
L-cystine + 2 H2O = 2 NH3 + 2 pyruvate + 2 hydrogen sulfide
-
(DL)-homocysteine = H2S + ?
-
L-Cys = H2S + NH3 + pyruvate
-
L-cysteine + H2O = H2S + pyruvate + NH3
-
L-cysteine + L-cysteine = H2S + L-lanthionine
-
L-cysteine + L-cysteine = L-lanthionine + H2S
-
L-cysteine = H2S + NH3 + pyruvate
-
L-homocysteine + H2O = H2S + ?
-
L-homocysteine + H2O = NH3 + 2-oxobutanoate + H2S
-
L-homocysteine + L-cysteine = L-cystathionine + H2S
-
L-homocysteine + L-homocysteine = L-homolanthionine + H2S
-
L-cysteine + H2O = sulfide + NH3 + pyruvate
-
L-Cys + sulfite = L-cysteate + H2S
-
DL-homocysteine + 2-mercaptoethanol = H2S + S-(beta-hydroxyethyl)-L-homocysteine
DL-homocysteine + 2-mercaptoethanol = H2S + S-(beta-hydroxyethyl)-L-homocysteine
DL-homocysteine + H2O = 2-oxobutanoate + NH3 + H2S
DL-homocysteine + H2O = 2-oxobutanoate + NH3 + H2S
L-cysteine + 2-mercaptoethanol = H2S + S-(beta-hydroxyethyl)-L-cysteine
L-cysteine + 2-mercaptoethanol = H2S + S-(beta-hydroxyethyl)-L-cysteine
L-cysteine = 2-oxopropanoate + NH3 + H2S
L-cysteine = 2-oxopropanoate + NH3 + H2S
DL-homocysteine + H2O = 2-oxobutanoate + NH3 + hydrogen sulfide
DL-homocysteine + H2O = 2-oxobutanoate + NH3 + hydrogen sulfide
DL-homocysteine + H2O = hydrogen sulfide + NH3 + 2-oxobutanoate
DL-homocysteine + H2O = hydrogen sulfide + NH3 + 2-oxobutanoate
L-homocysteine + H2O = hydrogen sulfide + NH3 + 2-oxobutanoate
L-homocysteine + H2O = hydrogen sulfide + NH3 + 2-oxobutanoate
L-homocysteine = 2-oxobutanoate + NH3 + hydrogen sulfide
L-homocysteine = 2-oxobutanoate + NH3 + hydrogen sulfide
L-cysteine + H2O = sulfide + NH3 + pyruvate
L-cysteine + H2O = sulfide + NH3 + pyruvate
L-homocysteine + H2O = sulfide + NH3 + 2-oxobutanoate
L-homocysteine + H2O = sulfide + NH3 + 2-oxobutanoate
DL-homocysteine + H2O = hydrogen sulfide + 2-oxobutyrate + ?
-
L-cysteine + H2O = hydrogen sulfide + pyruvate + ?
-
L-cysteine + H2O = pyruvate + NH3 + hydrogen sulfide
-
L-serine + H2O = hydrogen sulfide + pyruvate + NH3
-
L-cysteine + H2O = sulfide + NH3 + pyruvate
-
D-cysteine + H2O = sulfide + NH3 + pyruvate
-
L-cysteine + H2O = sulfide + NH3 + pyruvate
-
D-cysteine + H2O = sulfide + NH3 + pyruvate
-
L-homocysteine + H2O = H2S + NH3 + 2-oxobutanoate
L-homocysteine + H2O = H2S + NH3 + 2-oxobutanoate
L-homocysteine + H2O = hydrogen sulfide + NH3 + 2-oxobutanoate
L-homocysteine + H2O = hydrogen sulfide + NH3 + 2-oxobutanoate
beta-chloro-L-alanine + H2O = sulfide + ?
-
L-cysteine + H2O = sulfide + NH3 + pyruvate
-
L-cysteine methyl ester + H2O = sulfide + ?
-
S-ethyl-L-cysteine + H2O = sulfide + ?
-
S-methyl-L-cysteine + H2O = sulfide + ?
-
L-cysteine + HCN = H2S + L-3-cyanoalanine
-
L-cysteine + hydrogen cyanide = hydrogen sulfide + L-3-cyanoalanine
-
L-cysteine + hydrogen cyanide = L-3-cyanoalanine + hydrogen sulfide
-
L-cysteine + CN- = sulfide + L-3-cyanoalanine
-
L-cysteine + HCN = sulfide + L-3-cyanoalanine
-
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0.1
-
mutant enzyme C160A, at pH 7.0 and 23°C
0.1
-
mutant enzyme C356S, at pH 7.0 and 23°C
0.3
-
mutant enzyme C198A, at pH 7.0 and 23°C
0.5
-
mutant enzyme C160S, at pH 7.0 and 23°C
0.6
-
pH 7.5, 60°C, membrane-bound wild-type enzyme
0.62
-
pH 7.5, 60°C, membrane-bound mutant enzyme M380N
0.82
-
pH 7.5, 60°C, membrane-bound mutant enzyme Y383Q/F384K
1
-
mutant enzyme C128A, at pH 7.0 and 23°C
1.2
-
pH 7.5, 60°C, cytoplasmic mutant enzyme Y383Q/F384K
1.4
-
mutant enzyme H132A, at pH 7.0 and 23°C
1.6
-
mutant enzyme C128S, at pH 7.0 and 23°C
6.5
-
wild type enzyme, at pH 7.0 and 23°C
18.5
-
with coenzyme Q as cosubstrate, at pH 8.0 and 25°C
54
-
recombinant enzyme, at pH 7.4 and 47°C
62
-
solubilized enzyme, at pH 6.8 and 25°C
65
-
cosubstrates sulfide, ubiquinone-1, pH 7.0, 25°C
65
-
with coenzyme Q as cosubstrate, at pH 8.0 and 25°C
84
-
enzyme in nanodiscs, at pH 6.8 and 25°C
343
-
cosubstrates cyanide, ubiquinone-1, pH 8.5, 25°C
343
-
with coenzyme Q and cyanide as cosubstrates, at pH 8.0 and 25°C
379
-
cosubstrates sulfite, ubiquinone-1, pH 7.5, 25°C
379
-
with coenzyme Q and sulfite as cosubstrates, at pH 8.0 and 25°C
62
-
solubilized enzyme, at pH 6.8 and 25°C
74
-
with homocysteine as acceptor, at pH 7.4 and 37°C
84
-
enzyme in nanodiscs, at pH 6.8 and 25°C
92
-
with cysteine as acceptor, at pH 7.4 and 37°C
94
-
with glutathione as acceptor, at pH 7.4 and 37°C
113
-
with sulfite as acceptor, at pH 7.4 and 37°C
373
-
at pH 7.4 and 37°C
0.22
-
mutant Q147S, pH 7.0, 25°C
0.42
-
mutant T74A, pH 7.0, 25°C
0.73
-
mutant N77D, pH 7.0, 25°C
1.44
-
mutant T185A, pH 7.0, 25°C
1.45
-
mutant S75N, pH 7.0, 25°C
5.57
-
mutant T185S, pH 7.0, 25°C
6.3
-
at pH 7.4 and 25°C
10
-
mutant Y97F, pH 8.0, 30°C
12
-
wild-type, pH 8.0, 30°C
12.5
-
mutant Q147A, pH 7.0, 25°C
15
-
mutant S121A, pH 8.0, 30°C
20.2
-
mutant S75A, pH 7.0, 25°C
22
-
mutant Y97M, pH 8.0, 30°C
26
-
mutant V74T, pH 8.0, 30°C
29.5
-
mutant S269A, pH 7.0, 25°C
44
-
mutant S121M, pH 8.0, 30°C
82.7
-
mutant S75T, pH 7.0, 25°C
155
-
mutant N77A, pH 7.0, 25°C
202
-
sulfhydrylation of O-acetyl-L-serine
370
-
mutant T78S, pH 7.0, 25°C
537
-
mutant T78A, pH 7.0, 25°C
929
-
mutant S269T, pH 7.0, 25°C
1600
-
mutant T182A, pH 7.0, 25°C
1690
-
mutant T182S, pH 7.0, 25°C
1700
-
mutant T74S, pH 7.0, 25°C
1780
-
mutant H157Q, pH 7.0, 25°C
1990
-
mutant H157N, pH 7.0, 25°C
2170
-
wild-type, pH 7.0, 25°C
33
-
pH 7.5, 80°C, wild-type enzyme, with O-acetyl-L-serine
130
-
pH 7.5, 80°C, mutant F225A, with O-phospho-L-serine
730
-
pH 7.5, 80°C, wild-type enzyme, with O-phospho-L-serine
0.35
-
cosubstrate L-serine, pH 7.4, 37°C
0.78
-
cosubstrate L-serine, presence of S-adenosyl-L-methionine, pH 7.4, 37°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.0017
-
pH and temperature not specified in the publication
0.0023
-
at pH 6.0 and 30°C
0.0125
-
in 10 mM Tris-HCl buffer, pH 8.5, at 20°C
0.002
-
in 10 mM bis-Tris-HCl, pH 6.5, temperature not specified in the publication
0.0028
-
in 50 mM 2-[bis(2-hydroxyethyl)amino]-2-(hydroxymethyl)propane-1,3-diol (pH 6.5), temperature not specified in the publication
0.00297
-
wild type enzyme, at pH 7.0 and 23°C
0.005
-
mutant enzyme H132A, at pH 7.0 and 23°C
0.005
-
wild type enzyme, in 250 mM Tris-HCl (pH 8.0), temperature not specified in the publication
0.00553
-
mutant enzyme C128S, at pH 7.0 and 23°C
0.0056
-
mutant enzyme C128A, at pH 7.0 and 23°C
0.00594
-
in 50 mM Tris-HCl, pH 7.4, 40°C
0.00594
-
pH 7.4, temperature not specified in the publication
0.008
-
in 10 mM HEPES, pH 7.4, 10 mM MgCl, 10 mM KCl, at 22°C
0.0109
-
cosubstrates cyanide, ubiquinone-1, pH 8.5, 25°C
0.0109
-
with coenzyme Q and cyanide as cosubstrates, at pH 8.0 and 25°C
0.011
-
in 50 mM Bis-Tris (pH 7.0), at 20°C
0.011
-
mutant enzyme H131A, in 250 mM Tris-HCl (pH 8.0), temperature not specified in the publication
0.013
-
cosubstrates sulfite, ubiquinone-1, pH 7.5, 25°C
0.013
-
with coenzyme Q and sulfite as cosubstrates, at pH 8.0 and 25°C
0.015
-
mutant enzyme H196A, in 250 mM Tris-HCl (pH 8.0), temperature not specified in the publication
0.02
-
in 10 mM potassium HEPES (pH 7.4), 10 mM MgCl2, 10 mM KCl, temperature not specified in the publication
0.026
-
in 50 mM Bis-Tris (pH 6.5), temperature not specified in the publication
0.042
-
apparent value, at pH 7.0, temperature not specified in the publication
0.046
-
pH 7.5, 60°C, membrane-bound mutant enzyme Y383Q/F384K
0.073
-
pH 7.5, 60°C, membrane-bound mutant enzyme M380N
0.077
-
pH 7.5, 60°C, cytoplasmic mutant enzyme Y383Q/F384K
0.077
-
pH 7.5, 60°C, membrane-bound wild-type enzyme
0.077
-
pH 7.5, 60°C, wild-type enzyme
0.23
-
20 mM Tris-HCl, pH 8.0, at 22°C
0.23
-
enzyme in nanodiscs, at pH 6.8 and 25°C
0.315
-
cosubstrates sulfide, ubiquinone-1, pH 7.0, 25°C
0.315
-
with coenzyme Q as cosubstrate, at pH 8.0 and 25°C
0.35
-
solubilized enzyme, at pH 6.8 and 25°C
0.4
-
Km above 0.4 mM, mutant enzyme V300D, in 250 mM Tris-HCl (pH 8.0), temperature not specified in the publication
1.95
-
recombinant enzyme, at pH 7.4 and 47°C
0.00287
-
at pH 7.4 and 25°C
0.005
-
with cysteine as acceptor, at pH 7.4 and 37°C
0.007
-
with homocysteine as acceptor, at pH 7.4 and 37°C
0.00994
-
at pH 7.4 and 25°C
0.01
-
with glutathione as acceptor, at pH 7.4 and 37°C
0.043
-
with ubiquinone as cosubstrate, at pH 8.5 and 37°C
0.13
-
with sulfite as acceptor, at pH 7.4 and 37°C
0.23
-
enzyme in nanodiscs, at pH 6.8 and 25°C
0.32
-
at pH 7.4 and 37°C
0.35
-
solubilized enzyme, at pH 6.8 and 25°C
12.24
-
in 20 mM MES (pH 7.0), at 30°C
12.24
-
pH 7.0, 30°C, purified recombinant enzyme
0.6
-
pH and temperature not specified in the publication
0.006
-
pH 7.5, 25°C, free enzyme
0.013
-
pH 7.5, 25°C, enzyme bound to serine acetyltransferase
0.029
-
37°C, pH 7.8, cosubstrate: O-phosphoserine
0.033
-
pH 8.0, 30°C, isoenzyme 1
0.038
-
pH 7.8, 35°C, isoenzyme 2
0.073
-
mutant Y97F, pH 8.0, 30°C
0.084
-
mutant Y97M, pH 8.0, 30°C
0.095
-
mutant S121A, pH 8.0, 30°C
0.12
-
wild-type, pH 8.0, 30°C
0.14
-
mutant V74T, pH 8.0, 30°C
0.16
-
at pH 7.4 and 25°C
0.18
-
mutant N77D, pH 7.0, 25°C
0.2
-
mutant S121M, pH 8.0, 30°C
0.21
-
mutant S75T, pH 7.0, 25°C
0.22
-
mutant T182S, pH 7.0, 25°C
0.22
-
mutant T185A, pH 7.0, 25°C
0.22
-
wild-type, pH 7.0, 25°C
0.23
-
mutant N77A, pH 7.0, 25°C
0.25
-
pH 7.5, 25°C, chloroplast enzyme
0.27
-
mutant Q147S, pH 7.0, 25°C
0.3
-
mutant H157Q, pH 7.0, 25°C
0.3
-
mutant T78S, pH 7.0, 25°C
0.36
-
mutant T185S, pH 7.0, 25°C
0.37
-
pH 7.0, 25°C, recombinant free enzyme
0.39
-
mutant T182A, pH 7.0, 25°C
0.4
-
pH 7.4, 37°C, enzyme 1
0.4
-
mutant H157N, pH 7.0, 25°C
0.44
-
mutant T78A, pH 7.0, 25°C
0.54
-
mutant S269A, pH 7.0, 25°C
0.55
-
pH 7.5, 25°C, recombinant complex-bound enzyme
0.55
-
pH 8.0, 25°C, isoenzyme 1
0.66
-
pH 8.0, 25°, isoenzyme 1'
0.8
-
37°C, pH 7.8, cosubstrate: O-acetyl-L-Ser
0.8
-
pH 7.5, 37°C, isoenzyme 1 and 2
0.998
-
pH 7.5, enzyme form PCS-2
1.25
-
pH 8.0, 25°C, isoenzyme 2
1.46
-
pH 7.5, 22°C, recombinant enzyme, Lineweaver-Burke model
1.57
-
pH 7.5, enzyme form PCS-1
1.6
-
pH 7.4, 37°C, isoenzyme 2
1.6
-
mutant S269T, pH 7.0, 25°C
1.7
-
mutant Q147A, pH 7.0, 25°C
1.85
-
pH 7.5, 22°C, recombinant enzymem, Michaelis-Menten model
2.5
-
pH 8.0, 25°C, isoenzyme 3
3
-
isoform B, pH 7.5, 25°C, Michaelis-Menten kinetics
3.2
-
isoform B, pH 7.5, 25°C, Hill equation, Hill coefficient 0.75
3.2
-
mutant T74S, pH 7.0, 25°C
3.9
-
mutant T74A, pH 7.0, 25°C
4.6
-
isoform C, pH 7.5, 25°C, Hill equation, Hill coefficient 1.05
4.6
-
mutant S75A, pH 7.0, 25°C
4.7
-
isoform C, pH 7.5, 25°C, Michaelis-Menten kinetics
5.2
-
pH 7.5, 50°C, isoenzyme 1 and 2
5.6
-
isoform A, pH 7.5, 25°C, Michaelis-Menten kinetics
5.7
-
mutant S75N, pH 7.0, 25°C
6.4
-
isoform A, pH 7.5, 25°C, Hill equation, Hill coefficient 0.81
3
-
pH 7.3, 30°C, gamma-replacement reaction
0.25
-
pH 7.6, 60°C, with O-acetyl-L-serine
0.25
-
60°C, O-acetyl-L-serine sulfhydrylation reaction
0.39
-
pH 7.5, 80°C, wild-type enzyme, with O-acetyl-L-serine
1.6
-
pH 7.5, 80°C, mutant F225A, with O-phospho-L-serine
3.8
-
pH 7.5, 80°C, wild-type enzyme, with O-phospho-L-serine
5
-
pH 7.6, 60°C, with O-phospho-L-serine
5
-
60°C, O-phospho-L-serine sulfhydrylation reaction
12.5
-
pH 7.6, 85°C, with O-phospho-L-serine
12.5
-
85°C, O-phospho-L-serine sulfhydrylation reaction
4.7
-
cosubstrate L-serine, presence of S-adenosyl-L-methionine, pH 7.4, 37°C
5.02
-
cosubstrate L-serine, pH 7.4, 37°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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The beta-replacement-specific pyridoxal-P-dependent lyases
1984
Braunstein, A.E.; Goryachenkova, E.V.
Adv. Enzymol. Relat. Areas Mol. Biol.
56
1-89
Characterization of human cystathionine beta-synthase. Evidence for the identity of human L-serine dehydratase and cystathionine beta-synthase
1974
Porter, P.N.; Grishaver, M.S.; Jones, O.W.
Biochim. Biophys. Acta
364
128-139
An Aspergillus nidulans mutant lacking cystathionine beta-synthase: identity of L-serine sulfhydrolase with cystathionine beta-synthase and its distinctness from O-acetyl-L-serine sulfhydrolase
1973
Pieniazek, N.J.; Stepien, P.P.; Paszewski, A.
Biochim. Biophys. Acta
297
37-47
Specificity and some other properties of liver serine sulphhydrolase: evidence for its identity with cystathionine beta-synthase
1971
Braunstein, A.E.; Goryachenkova, E.V.; Tolosa, E.A.; Willhardt, I.H.; Yefremova, L.L.
Biochim. Biophys. Acta
242
247-260
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Biosynthese des Cysteins. I. Nachweis und Isolierung der Serinsulfhydrase aus BĂ€ckerhefe
1962
Schlossmann, K.; Brueggemann, J.; Lynen, F.
Biochem. Z.
336
258-273
The identification of a variant form of cystathionine beta-synthase
1992
Walker, J.; Barrett, J.; Thong, K.W.
Exp. Parasitol.
75
415-424
A novel cystathionine beta-synthase from Panagrellus redivivus (Nematoda)
1996
Papadopoulos, A.I.; Walker, J.; Barrett, J.
Int. J. Biochem. Cell Biol.
28
543-549
Photoactivation of urocanase in Pseudomonas putida
1978
Hug, D.H.; O'Donnell, P.S.; Hunter, J.K.
J. Biol. Chem.
253
7622-7629
Evidence for identity of beta-pyrazolealanine synthase with cysteine synthase in watermelon: Formation of beta-pyrazolealanine by cloned cysteine synthase in vitro and in vivo
1993
Noji, M.; Murakoshi, I.; Saito, K.
Biochem. Biophys. Res. Commun.
197
1111-1117
Bacterial selenocysteine synthase
1998
Tormay, P.; Wilting, R.; Lottspeich, F.; Mehta, P.K.; Christen, P.; Böck, A.
Eur. J. Biochem.
254
655-661
Studies on the synthesis of the Fe-S cluster of dihydroxy-acid dehydratase in escherichia coli crude extract. Isolation of O-acetylserine sulfhydrylases A and B and beta-cystathionase based on their ability to mobilize sulfur from cysteine and to participate in Fe-S cluster synthesis
1996
Flint, D.H.; Tuminello, J.F.; Miller, T.J.
J. Biol. Chem.
271
16053-16067
Purification and characterization of cystathionine gamma-lyase from Lactobacillus fermentum DT41
1998
Smacchi, E.; Gobbetti, M.
FEMS Microbiol. Lett.
166
197-202
Cystalysin, a 46-kDa L-cysteine desulfhydrase from Treponema denticola: biochemical and biophysical characterization
1999
Chu, L.; Ebersole, J.L.; Kurzban, G.P.; Holt, S.C.
Clin. Infect. Dis.
28
442-450
The pyridoxal-phosphate-dependent enzymes exclusively catalyzing reactions of beta-replacement
1976
Braunstein, A.E.; Goryachenkova, E.V.
Biochimie
58
5-17
Reactions catalysed by cysteine lyase from the yolk sac of chicken embryo
1969
Tolosa, E.A.; Chepurnova, N.K.; Khomutov, R.M.; Severin, E.S.
Biochim. Biophys. Acta
171
369-371
Trichomonas species: homocysteine desulphurase and serine sulphydrase activities
1987
Thong, K.W.; Coombs, G.H.
Exp. Parasitol.
63
143-151
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Homocysteine desulphurase activity in trichomonads
1985
Thong, K.W.; Coombs, G.H.
IRCS Med. Sci. Libr. Compend.
13
493-494
Function of pyridoxal phosphate in desulfhydrase system of Proteus morganii
1951
Kallio, R.E.
J. Biol. Chem.
192
371-377
Sulphur metabolism in Paracoccus denitrificans. Purification, properties and regulation of serine transacetylase, O-acetylserine sulphydrylase and beta-cystathionase
1977
Burnell, J.N.; Whatley, F.R.
Biochim. Biophys. Acta
481
246-265
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Biosynthesis of homocysteine in a facultative methylotroph, Pseudomonas FM518
1983
Morinaga, Y.; Tani, Y.; Yamada, H.
Agric. Biol. Chem.
47
2855-2860
-
Purification and properties of beta-cyano-L-alanine synthase from Vicia angustifolia
1989
Ikegami, F.; Takayama, K.; Kurihara, T.; Horiuchi, S.; Tajima, C.; Shirai, R.; Murakoshi, I.
Phytochemistry
28
2285-2291
-
Purification and properties of beta-cyano-L-alanine synthase from Spinacia oleracea
1988
Ikegami, F.; Takayama, K.; Tajima, Ch.; Murakoshi, I.
Phytochemistry
27
2011-2016
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beta-Cyanoalanine synthase (blue lupine)
1971
Hendickson, H.R.; Conn, E.E.
Methods Enzymol.
17B
233-239
Link between L-3-cyanoalanine synthase activity and differential cyanide sensitivity of insects
1991
Meyers., D.M.; Ahmad, S.
Biochim. Biophys. Acta
1075
195-197
Cytosolic beta-cyanoalanine synthase activity attributed to cysteine synthases in cocklebur seeds. Purification and characterization of cytosolic cysteine synthases
1998
Maruyama, A.; Ishizawa, K.; Takagi, T.; Esashi, Y.
Plant Cell Physiol.
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