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Ligand thiosulfate

Basic Ligand Information

Molecular Structure

Pathway Source

Pathways

BRENDA

non-pathway related

KEGG

ABC transporters, Microbial metabolism in diverse environments, Sulfur metabolism

MetaCyc

L-cysteine biosynthesis VII (from S-sulfo-L-cysteine), sulfide oxidation IV (mitochondria), tetrathionate oxidation, tetrathionate reduction I (to thiosulfate), thiosulfate disproportionation I (thiol-dependent), thiosulfate disproportionation II (cytochrome), thiosulfate disproportionation III (quinone), thiosulfate disproportionation IV (rhodanese), thiosulfate oxidation I (to tetrathionate), thiosulfate oxidation II (via tetrathionate), thiosulfate oxidation III (multienzyme complex), thiosulfate oxidation IV (multienzyme complex) more

Show all BRENDA pathways known for thiosulfate

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Roles as Enzyme Ligand

In Vivo Substrate in Enzyme-catalyzed Reactions (32 results)

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Show Natural Substrate (32 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.8.2.2

2 thiosulfate + 2 ferricytochrome c = tetrathionate + 2 ferrocytochrome c

765056, 742899, 765356, 764941, 763985, 741526, 742887

4v2k, 3D-view

1.8.2.2

2 thiosulfate + 2 ferricytochrome c = tetrathionate + 2 ferrocytochrome c

765056, 742899, 765356, 764941, 763985, 741526, 742887

4wq9, 3D-view

1.8.2.2

2 thiosulfate + 2 ferricytochrome c = tetrathionate + 2 ferrocytochrome c

765056, 742899, 765356, 764941, 763985, 741526, 742887

4wqc, 3D-view

1.8.2.2

2 thiosulfate + 2 ferricytochrome c = tetrathionate + 2 ferrocytochrome c

765056, 742899, 765356, 764941, 763985, 741526, 742887

4wqe, 3D-view

1.8.2.2

thiosulfate + cytochrome c = tetrathionate + reduced cytochrome c

394120, 288769

4v2k, 3D-view

1.8.2.2

thiosulfate + cytochrome c = tetrathionate + reduced cytochrome c

394120, 288769

4wq9, 3D-view

1.8.2.2

thiosulfate + cytochrome c = tetrathionate + reduced cytochrome c

394120, 288769

4wqc, 3D-view

1.8.2.2

thiosulfate + cytochrome c = tetrathionate + reduced cytochrome c

394120, 288769

4wqe, 3D-view

1.8.2.2

thiosulfate + ferricytochrome c = tetrathionate + ferrocytochrome c

676077, 673503

4v2k, 3D-view

1.8.2.2

thiosulfate + ferricytochrome c = tetrathionate + ferrocytochrome c

676077, 673503

4wq9, 3D-view

1.8.2.2

thiosulfate + ferricytochrome c = tetrathionate + ferrocytochrome c

676077, 673503

4wqc, 3D-view

1.8.2.2

thiosulfate + ferricytochrome c = tetrathionate + ferrocytochrome c

676077, 673503

4wqe, 3D-view

1.8.2.2

thiosulfate + oxidized acceptor = tetrathionate + reduced acceptor

764763

4v2k, 3D-view

1.8.2.2

thiosulfate + oxidized acceptor = tetrathionate + reduced acceptor

764763

4wq9, 3D-view

1.8.2.2

thiosulfate + oxidized acceptor = tetrathionate + reduced acceptor

764763

4wqc, 3D-view

1.8.2.2

thiosulfate + oxidized acceptor = tetrathionate + reduced acceptor

764763

4wqe, 3D-view

1.8.2.2

16 entries

1.8.2.5

thiosulfate + 2 ferrocytochrome c3 = sulfite + hydrogen sulfide + 2 ferricytochrome c3

739959

-

1.8.5.2

2 thiosulfate + caldariellaquinone + 2 H+ = tetrathionate + caldariellaquinol

656833

-

1.8.5.2

2 thiosulfate + ubiquinone-2 = tetrathionate + ubiquinol-2

765755

-

1.8.5.2

thiosulfate + 6-decylubiquinone = tetrathionate + 6-decylubiquinol

656833

-

1.8.5.2

3 entries

1.8.99.B2

2 thiosulfate + ubiquinone = tetrathionate + ubiquinol

742121

-

2.5.1.144

O-acetyl-L-serine + thiosulfate = S-sulfo-L-cysteine + acetate

748910, 748967, 749025, 747281, 748058, 748059, 761117

-

2.5.1.47

O-acetyl-L-Ser + S2O32- = S-sulfocysteine + ?

725881

-

2.5.1.65

O-phospho-L-serine + thiosulfate = S-sulfocysteine + phosphate

738534

-

2.8.1.1

thiosulfate + cyanide = sulfite + thiocyanate

645514, 645546, 645500, 737706, 645534, 645536, 645537, 645539, 738551, 739155, 645532, 645533, 645495, 645535, 645511, 645540, 645501, 645503, 645504, 645505, 645506, 645507, 645508, 645510, 645519, 645522, 645524, 645525, 645526, 645527, 645528, 645529, 645531, 645543, 645545, 645542, 645497, 645515, 645496, 645521, 645523, 645516, 645530, 739474, 645499, 645541, 645512, 645513, 645498, 645517, 645520, 645509, 645544, 645518, 645502, 645538, 661492, 663433, 690262

-

2.8.1.2

thiosulfate + cyanide = SO32- + thiocyanate

738988

-

2.8.1.3

thiosulfate + glutathione = sulfite + glutathione disulfide + sulfide

645570, 645571, 645572

-

2.8.1.5

thiosulfate + 2 dithioerythritol = sulfite + dithioerythritol disulfide + sulfide

645578, 645575, 645577

-

2.8.5.1

3-phospho-L-serine + thiosulfate = S-sulfo-L-cysteine + phosphate

747281, 748092

-

2.8.5.2

[SoxY protein]-L-cysteine + thiosulfate + 2 ferricytochrome c = [SoxY protein]-S-sulfosulfanyl-L-cysteine + 2 ferrocytochrome c + 2 H+

747062, 747161, 749103, 748504

-

2.8.5.2

[SoxY protein]-S-sulfanyl-L-cysteine + thiosulfate + 2 ferricytochrome c = [SoxY protein]-S-(2-sulfodisulfanyl)-L-cysteine + 2 ferrocytochrome c + 2 H+

747062, 747161, 749103, 748504

-

2.8.5.2

2 entries

7.3.2.3

ATP + H2O + thiosulfate/out = ADP + phosphate + thiosulfate/in

441605

-

In Vivo Product in Enzyme-catalyzed Reactions (7 results)

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Show Natural Product (7 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.13.11.18

5 sulfur + 2 O2 + 2 H2O + 4 H+ = sulfite + thiosulfate + 2 sulfide

0

-

1.8.99.B2

tetrathionate + a reduced electron acceptor = 2 thiosulfate + an oxidized electron acceptor

0

-

1.8.99.B2

tetrathionate + reduced electron acceptor = 2 thiosulfate + oxidized electron acceptor

0

-

1.8.99.B2

2 entries

2.8.1.2

3-mercaptopyruvate + HSO3- = pyruvate + S2O32-

0

-

3.12.1.1

trithionate + H2O = sulfate + thiosulfate

288770, 288769

-

3.12.1.1

trithionate + H2O = thiosulfate + sulfate

0

-

3.12.1.1

2 entries

7.3.2.3

ATP + H2O + thiosulfate/out = ADP + phosphate + thiosulfate/in

441605

-

Substrate in Enzyme-catalyzed Reactions (101 results)

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Show Substrate (101 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.8.2.2

2 thiosulfate + 2 ferricyanide = tetrathionate + 2 ferrocyanide

765056, 724861, 742887, 763985, 724028, 726008

4v2k, 3D-view

1.8.2.2

2 thiosulfate + 2 ferricyanide = tetrathionate + 2 ferrocyanide

765056, 724861, 742887, 763985, 724028, 726008

4wq9, 3D-view

1.8.2.2

2 thiosulfate + 2 ferricyanide = tetrathionate + 2 ferrocyanide

765056, 724861, 742887, 763985, 724028, 726008

4wqc, 3D-view

1.8.2.2

2 thiosulfate + 2 ferricyanide = tetrathionate + 2 ferrocyanide

765056, 724861, 742887, 763985, 724028, 726008

4wqe, 3D-view

1.8.2.2

2 thiosulfate + 2 ferricytochrome c = tetrathionate + 2 ferrocytochrome c

765056, 742899, 765356, 764941, 763985, 741526, 742887

4v2k, 3D-view

1.8.2.2

2 thiosulfate + 2 ferricytochrome c = tetrathionate + 2 ferrocytochrome c

765056, 742899, 765356, 764941, 763985, 741526, 742887

4wq9, 3D-view

1.8.2.2

2 thiosulfate + 2 ferricytochrome c = tetrathionate + 2 ferrocytochrome c

765056, 742899, 765356, 764941, 763985, 741526, 742887

4wqc, 3D-view

1.8.2.2

2 thiosulfate + 2 ferricytochrome c = tetrathionate + 2 ferrocytochrome c

765056, 742899, 765356, 764941, 763985, 741526, 742887

4wqe, 3D-view

1.8.2.2

thiosulfate + 2 ferrocytochrome c3 = sulfite + hydrogen sulfide + 2 ferricytochrome c3

740640

4v2k, 3D-view

1.8.2.2

thiosulfate + 2 ferrocytochrome c3 = sulfite + hydrogen sulfide + 2 ferricytochrome c3

740640

4wq9, 3D-view

1.8.2.2

thiosulfate + 2 ferrocytochrome c3 = sulfite + hydrogen sulfide + 2 ferricytochrome c3

740640

4wqc, 3D-view

1.8.2.2

thiosulfate + 2 ferrocytochrome c3 = sulfite + hydrogen sulfide + 2 ferricytochrome c3

740640

4wqe, 3D-view

1.8.2.2

thiosulfate + cytochrome c = tetrathionate + reduced cytochrome c

394120, 288769

4v2k, 3D-view

1.8.2.2

thiosulfate + cytochrome c = tetrathionate + reduced cytochrome c

394120, 288769

4wq9, 3D-view

1.8.2.2

thiosulfate + cytochrome c = tetrathionate + reduced cytochrome c

394120, 288769

4wqc, 3D-view

1.8.2.2

thiosulfate + cytochrome c = tetrathionate + reduced cytochrome c

394120, 288769

4wqe, 3D-view

1.8.2.2

thiosulfate + ferricyanide = tetrathionate + ferrocyanide

659545, 394116, 394117, 394078, 394115, 690014, 676077

4v2k, 3D-view

1.8.2.2

thiosulfate + ferricyanide = tetrathionate + ferrocyanide

659545, 394116, 394117, 394078, 394115, 690014, 676077

4wq9, 3D-view

1.8.2.2

thiosulfate + ferricyanide = tetrathionate + ferrocyanide

659545, 394116, 394117, 394078, 394115, 690014, 676077

4wqc, 3D-view

1.8.2.2

thiosulfate + ferricyanide = tetrathionate + ferrocyanide

659545, 394116, 394117, 394078, 394115, 690014, 676077

4wqe, 3D-view

1.8.2.2

thiosulfate + ferricytochrome c = tetrathionate + ferrocytochrome c

676077, 673503

4v2k, 3D-view

1.8.2.2

thiosulfate + ferricytochrome c = tetrathionate + ferrocytochrome c

676077, 673503

4wq9, 3D-view

1.8.2.2

thiosulfate + ferricytochrome c = tetrathionate + ferrocytochrome c

676077, 673503

4wqc, 3D-view

1.8.2.2

thiosulfate + ferricytochrome c = tetrathionate + ferrocytochrome c

676077, 673503

4wqe, 3D-view

1.8.2.2

thiosulfate + high-potential non-heme iron protein = tetrathionate + reduced high-potential non-heme iron protein

394117

4v2k, 3D-view

1.8.2.2

thiosulfate + high-potential non-heme iron protein = tetrathionate + reduced high-potential non-heme iron protein

394117

4wq9, 3D-view

1.8.2.2

thiosulfate + high-potential non-heme iron protein = tetrathionate + reduced high-potential non-heme iron protein

394117

4wqc, 3D-view

1.8.2.2

thiosulfate + high-potential non-heme iron protein = tetrathionate + reduced high-potential non-heme iron protein

394117

4wqe, 3D-view

1.8.2.2

thiosulfate + oxidized acceptor = tetrathionate + reduced acceptor

764763, 394128, 394123, 394124, 394117, 394119, 394122, 394116, 394120, 394078, 288769, 394115, 394121, 394118, 394126, 394125

4v2k, 3D-view

1.8.2.2

thiosulfate + oxidized acceptor = tetrathionate + reduced acceptor

764763, 394128, 394123, 394124, 394117, 394119, 394122, 394116, 394120, 394078, 288769, 394115, 394121, 394118, 394126, 394125

4wq9, 3D-view

1.8.2.2

thiosulfate + oxidized acceptor = tetrathionate + reduced acceptor

764763, 394128, 394123, 394124, 394117, 394119, 394122, 394116, 394120, 394078, 288769, 394115, 394121, 394118, 394126, 394125

4wqc, 3D-view

1.8.2.2

thiosulfate + oxidized acceptor = tetrathionate + reduced acceptor

764763, 394128, 394123, 394124, 394117, 394119, 394122, 394116, 394120, 394078, 288769, 394115, 394121, 394118, 394126, 394125

4wqe, 3D-view

1.8.2.2

thiosulfate + reduced methyl viologen = sulfite + hydrogen sulfide + oxidized methyl viologen

740640

4v2k, 3D-view

1.8.2.2

thiosulfate + reduced methyl viologen = sulfite + hydrogen sulfide + oxidized methyl viologen

740640

4wq9, 3D-view

1.8.2.2

thiosulfate + reduced methyl viologen = sulfite + hydrogen sulfide + oxidized methyl viologen

740640

4wqc, 3D-view

1.8.2.2

thiosulfate + reduced methyl viologen = sulfite + hydrogen sulfide + oxidized methyl viologen

740640

4wqe, 3D-view

1.8.2.5

thiosulfate + 2 ferrocytochrome c3 = sulfite + hydrogen sulfide + 2 ferricytochrome c3

739959

-

1.8.2.5

thiosulfate + reduced benzyl viologen = sulfite + hydrogen sulfide + oxidized benzyl viologen

740591

-

1.8.2.5

thiosulfate + reduced methyl viologen = sulfite + hydrogen sulfide + oxidized methyl viologen

740591, 739959, 740639, 740631

-

1.8.5.2

2 thiosulfate + caldariellaquinone + 2 H+ = tetrathionate + caldariellaquinol

656833

-

1.8.5.2

2 thiosulfate + ubiquinone-2 = tetrathionate + ubiquinol-2

765755

-

1.8.5.2

thiosulfate + 6-decylubiquinone = tetrathionate + 6-decylubiquinol

656833

-

1.8.5.2

thiosulfate + ferricyanide + H+ = tetrathionate + ferrocyanide

724028

-

1.8.5.2

thiosulfate + ferricyanide = tetrathionate + ferrocyanide

656833

-

1.8.2.2

36 entries

1.8.2.5

3 entries

1.8.5.2

5 entries

1.8.5.5

thiosulfate + menaquinol = sulfite + hydrogen sulfide + menaquinone

725273

-

1.8.99.B2

2 thiosulfate + ferricyanide = tetrathionate + ferrocyanide

737877, 742121, 741675

-

1.8.99.B2

2 thiosulfate + ubiquinone = tetrathionate + ubiquinol

742121

-

1.8.99.B2

thiosulfate + oxidized acceptor = tetrathionate + reduced acceptor

394129

-

2.5.1.144

azaserine + thiosulfate = ?

748059

-

2.5.1.144

O-acetyl-L-serine + thiosulfate = S-sulfo-L-cysteine + acetate

748910, 748967, 749025, 747281, 748058, 748059, 761117, 746931

-

2.5.1.47

O-acetyl-L-Ser + S2O32- = S-sulfocysteine + ?

725881

-

2.5.1.47

O-acetyl-L-Ser + thiosulfate = S-sulfocysteine + sodium acetate

637347, 637385

-

2.5.1.47

O-acetyl-L-serine + thiosulfate = S-sulfo-L-cysteine + acetate

706226, 721306

-

2.5.1.47

O-acetyl-L-serine + thiosulfate = S-sulfo-L-cysteine + acetate + H+

637347

-

1.8.99.B2

3 entries

2.5.1.144

2 entries

2.5.1.47

4 entries

2.5.1.65

O-phospho-L-serine + thiosulfate = S-sulfocysteine + phosphate

738193, 738534

-

2.8.1.1

4-(dimethylamino)-4'-azobenzene sulfinate + thiosulfate = 4-(dimethylamino)-4'-azobenzene thiosulfonate + SO32-

645505

-

2.8.1.1

5-dimethylamino-1-naphthalene sulfinate + thiosulfate = 5-dimethylamino-1-naphthalene thiosulfonate + SO32-

645505

-

2.8.1.1

thioredoxin + thiosulfate = ?

645532

-

2.8.1.1

thiosulfate + 2 glutathione = sulfite + glutathione disulfide + sulfide

761486

-

2.8.1.1

thiosulfate + 2-mercaptoethanol = ?

645519

-

2.8.1.1

thiosulfate + a thiol = ?

645519

-

2.8.1.1

thiosulfate + benzene thiosulfonate = ?

645513

-

2.8.1.1

thiosulfate + borohydride = ?

645502, 645503

-

2.8.1.1

thiosulfate + cyanide = sulfite + thiocyanate

645514, 645546, 645500, 645502, 737706, 645534, 645536, 645537, 645538, 645539, 738551, 739155, 645518, 645532, 645533, 645495, 645535, 677214, 645511, 645540, 645501, 645503, 645504, 645505, 645506, 645507, 645508, 645510, 645519, 645522, 645524, 645525, 645526, 645527, 645528, 645529, 645531, 645543, 645545, 673274, 675044, 645542, 645520, 660889, 661492, 645497, 645515, 690262, 645496, 645521, 645523, 645516, 645530, 739474, 645499, 645541, 645512, 645513, 645498, 645517, 673600, 724480, 662068, 760422, 645509, 645544, 762459, 761486, 663433

-

2.8.1.1

thiosulfate + D,L-homocysteine = ?

645519

-

2.8.1.1

thiosulfate + dihydrolipoate = ?

645503, 645507, 645496, 645513, 645518

-

2.8.1.1

thiosulfate + dithionite = ?

645502

-

2.8.1.1

thiosulfate + dithiothreitol = ?

645519, 760422

-

2.8.1.1

thiosulfate + glutathione = ?

760422, 645519

-

2.8.1.1

thiosulfate + glutathione = sulfite + glutathione disulfide

762111

-

2.8.1.1

thiosulfate + L-cysteine = ?

645519

-

2.8.1.1

thiosulfate + monothiol = ?

645503

-

2.8.1.1

thiosulfate + N-acetyl-L-cysteine = ?

645519

-

2.8.1.1

thiosulfate + sulfite = sulfite + thiosulfate

645502, 645503

-

2.8.1.1

thiosulfate + thioredoxin = ?

761486

-

2.8.1.1

thiosulfate + thiosulfinate = ?

645503

-

2.8.1.2

3-mercaptopyruvate + thiosulfate = pyruvate + H2S

724231

-

2.8.1.2

thiosulfate + 2-mercaptoethanol = sulfate + ?

704585

-

2.8.1.2

thiosulfate + cyanide = SO32- + thiocyanate

738988

-

2.8.1.2

thiosulfate + cyanide = sulfite + thiocyanate

762459

-

2.8.1.2

thiosulfate + glutathione = sulfite + glutathione disulfide

762111

-

2.8.1.2

thiosulfate + thioredoxin = ?

645569

-

2.8.1.2

thiosulfate + [3-mercaptopyruvate sulfurtransferase]-L-cysteine = sulfate + [3-mercaptopyruvate sulfurtransferase]-S-sulfanyl-L-cysteine

762422, 760486

-

2.8.1.3

thiosulfate + cyanide = ?

645519

-

2.8.1.3

thiosulfate + cyanide = sulfite + thiocyanate

761486

-

2.8.1.3

thiosulfate + dithiothreitol = ?

645519

-

2.8.1.3

thiosulfate + glutathione = ? + glutathione disulfide

761486

-

2.8.1.3

thiosulfate + glutathione = sulfite + glutathione disulfide + sulfide

645570, 645571, 645572

-

2.8.1.3

thiosulfate + thioredoxin = ?

761486

-

2.8.1.5

thiosulfate + 2 dithioerythritol = sulfite + dithioerythritol disulfide + sulfide

645578, 645575, 645577

-

2.8.1.5

thiosulfate + 2 dithiothreitol = sulfite + dithiothreitol disulfide + sulfide

742170

-

2.8.1.5

thiosulfate + dithiothreitol = sulfite + oxidized dithiothreitol + sulfide

725273

-

2.8.1.5

thiosulfate + menaquinol = sulfite + oxidized menaquinol + sulfide

725273

-

2.8.1.5

thiosulfate + methylviologen = sulfide + ?

645576

-

2.8.1.5

thiosulfate + NAD(P)H = H2S + NAD(P)+ + sulfite

645579

-

2.8.1.5

thiosulfate + NADH = H2S + NAD+ + sulfite

645579

-

2.8.1.1

21 entries

2.8.1.2

7 entries

2.8.1.3

6 entries

2.8.1.5

7 entries

2.8.5.1

3-phospho-L-serine + thiosulfate = S-sulfo-L-cysteine + phosphate

747281, 748092

-

2.8.5.2

[SoxY protein]-L-cysteine + thiosulfate + 2 ferricytochrome c = [SoxY protein]-S-sulfosulfanyl-L-cysteine + 2 ferrocytochrome c + 2 H+

747062, 747161, 749103, 748504

-

2.8.5.2

[SoxY protein]-S-sulfanyl-L-cysteine + thiosulfate + 2 ferricytochrome c = [SoxY protein]-S-(2-sulfodisulfanyl)-L-cysteine + 2 ferrocytochrome c + 2 H+

747062, 747161, 749103, 748504

-

2.8.5.2

2 entries

3.1.6.20

horse heart cytochrome c + thiosulfate = ?

748074

-

7.3.2.3

ATP + H2O + thiosulfate/out = ADP + phosphate + thiosulfate/in

441605, 441606, 441608, 441607

-

Product in Enzyme-catalyzed Reactions (30 results)

top print hide

Show Product (30 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.13.11.18

5 sulfur + 2 O2 + 2 H2O + 4 H+ = sulfite + thiosulfate + 2 sulfide

0

-

1.13.11.18

sulfur + O2 + H2O = thiosulfate

0

-

1.13.11.55

S + O2 = SO32- + S2O32- + H2S

0

-

1.13.11.55

S + OH- + O2 = HSO3- + S2O32- + HS- + H+

0

-

1.8.2.2

tetrathionate + reduced methyl viologen = 2 thiosulfate + methyl viologen

0

4v2k, 3D-view

1.8.2.2

tetrathionate + reduced methyl viologen = 2 thiosulfate + methyl viologen

0

4wq9, 3D-view

1.8.2.2

tetrathionate + reduced methyl viologen = 2 thiosulfate + methyl viologen

0

4wqc, 3D-view

1.8.2.2

tetrathionate + reduced methyl viologen = 2 thiosulfate + methyl viologen

0

4wqe, 3D-view

1.8.2.2

tetrathionate + reduced methylviologen = 2 thiosulfate + methylviologen

0

4v2k, 3D-view

1.8.2.2

tetrathionate + reduced methylviologen = 2 thiosulfate + methylviologen

0

4wq9, 3D-view

1.8.2.2

tetrathionate + reduced methylviologen = 2 thiosulfate + methylviologen

0

4wqc, 3D-view

1.8.2.2

tetrathionate + reduced methylviologen = 2 thiosulfate + methylviologen

0

4wqe, 3D-view

1.13.11.18

2 entries

1.13.11.55

2 entries

1.8.2.2

8 entries

1.8.5.2

tetrathionate + reduced methylene blue = thiosulfate + oxidized methylene blue

0

-

1.8.5.4

sulfide + sulfite + coenzyme Q = thiosulfate + reduced coenzyme Q

0

-

1.8.5.4

sulfide + sulfite + ubiquinone-1 = thiosulfate + ubiquinol-1

0

-

1.8.5.4

2 entries

1.8.5.5

sulfite + hydrogen sulfide + menaquinone = thiosulfate + menaquinol

0

-

1.8.5.8

hydrogen sulfide + sulfite + coenzyme Q1 = thiosulfate + reduced coenzyme Q1

0

-

1.8.99.B2

tetrathionate + a reduced electron acceptor = 2 thiosulfate + an oxidized electron acceptor

0

-

1.8.99.B2

tetrathionate + reduced electron acceptor = 2 thiosulfate + oxidized electron acceptor

0

-

1.8.99.B2

tetrathionate + reduced methyl viologen = 2 thiosulfate + oxidized methyl viologen

0

-

1.8.99.B2

3 entries

2.8.1.1

thiosulfate + sulfite = sulfite + thiosulfate

0

-

2.8.1.2

3-mercaptopyruvate + HSO3- = pyruvate + S2O3-

0

-

2.8.1.2

3-mercaptopyruvate + HSO3- = pyruvate + S2O32-

0

-

3.12.1.1

trithionate + H2O = sulfate + thiosulfate

288770, 288769

-

3.12.1.1

trithionate + H2O = thiosulfate + sulfate

0

-

3.12.1.B1

pentathionate + H2O = 2 sulfur + thiosulfate + sulfate + 2 H+

0

-

3.12.1.B1

tetrathionate + H2O = pentathionate + thiosulfate + sulfate

0

-

3.12.1.B1

tetrathionate + H2O = sulfur + thiosulfate + sulfate + 2 H+

0

-

3.12.1.B1

tetrathionate + H2O = thiosulfate + sulfate + sulfur + 2 H+

0

-

2.8.1.2

2 entries

3.12.1.1

2 entries

3.12.1.B1

4 entries

7.3.2.3

ATP + H2O + thiosulfate/out = ADP + phosphate + thiosulfate/in

441605, 0

-

Activator in Enzyme-catalyzed Reactions (3 results)

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Show Activating Compound (3 entries)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

2.5.1.2

greater reactivation at 33 mM than at 3.3 mM

636851

-

2.7.7.4

activates SO42–dependent reaction in presence of 0.15 mM of 3'-phosphoadenosine-5'-phosphate

643258

1jec, 3D-view

3.1.1.20

2.2fold induction

653585

-

Inhibitor in Enzyme-catalyzed Reactions (29 results)

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Show Inhibitors (29 entries)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

1.13.11.20

competitive inhibitor, binding structure, overview

743088

4xez, 3D-view

1.13.11.20

competitive inhibitor, binding structure, overview

743088

4xff, 3D-view

1.13.11.20

competitive inhibitor, binding structure, overview

743088

5ezw, 3D-view

1.13.11.20

competitive inhibitor, binding structure, overview

743088

5i0s, 3D-view

1.13.11.20

competitive inhibitor, binding structure, overview

743088

5i0t, 3D-view

1.13.11.20

5 entries

1.2.98.1

-

390487

-

1.8.2.2

inhibitory above 0.75 mM

740640

4v2k, 3D-view

1.8.2.2

inhibitory above 0.75 mM

740640

4wq9, 3D-view

1.8.2.2

inhibitory above 0.75 mM

740640

4wqc, 3D-view

1.8.2.2

inhibitory above 0.75 mM

740640

4wqe, 3D-view

1.8.2.2

4 entries

2.7.1.90

-

642097

-

2.7.3.2

0.5 mM thiosulfate administration decreases the enzyme activity 30 min after administration. Thiosulfate also decreases the activity of the enzyme in vitro in striatum of rats, which is prevented by the thiol reducing agents dithiothreitol, the antioxidants glutathione, melatonin, trolox, and lipoic acid; thiosulfate (1 M) inhibits creatine kinase activity in rat striatum via thiol group oxidation is prevented by the thiol reducing agents dithiothreitol GSH, melatonin, trolox and lipoic acid

762017

-

2.7.7.4

-

641208, 643258, 643276

1jec, 3D-view

2.7.7.4

1 mM, 62% inhibition

643258

1jec, 3D-view

2.7.7.4

dead-end inhibitor, competitive with SO42- or MoO42-, noncompetitive against MgATP2-

643266

1jec, 3D-view

2.7.7.4

noncompetitive mixed-type inhibition with respect to MgATP2-

641204

1jec, 3D-view

2.7.7.4

competitive with molybdate and noncompetitive with MgATP

662282

1jec, 3D-view

2.8.1.1

non competitive against cyanide

645539

-

2.8.1.1

substrate inhibition at high concentrations

645513

-

2.8.1.1

substrate inhibition at low concentrations of cyanide

645532

-

2.7.7.4

5 entries

2.8.1.1

3 entries

2.8.1.5

above 0.5 mM

645575

-

3.1.6.14

-

135581

-

3.1.6.4

-

135645

-

3.12.1.1

-

288770

-

3.12.1.B1

product inhibition, 40% inhibition at 1 mM

725029

-

4.1.1.59

1 mM, 15% loss of activity

747847

-

4.2.1.104

-

210682

-

5.5.1.5

negligible effect near the pH optimum but inhibits to a greater extent on the acid side of the optimum

3718

-

7.3.2.3

-

697446

-

Metals and Ions (1 result)

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Show Metals Ions (1 entry)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

3.2.1.1

stimulates

393404

-

3D Structure of Enzyme-Ligand-Complex (PDB) (116 results)

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Show 3D Structure of Enzyme-Ligand-Complex (PDB) (116 entries)

EC NUMBER

ENZYME 3D STRUCTURE

1.13.11.20

4xez, 3D-view

1.13.11.20

4xff, 3D-view

1.13.11.20

5ezw, 3D-view

1.13.11.20

5i0s, 3D-view

1.13.11.20

5i0t, 3D-view

1.13.11.20

4xez, 3D-view

1.13.11.20

4xff, 3D-view

1.13.11.20

5ezw, 3D-view

1.13.11.20

5i0s, 3D-view

1.13.11.20

5i0t, 3D-view

1.13.11.20

4xez, 3D-view

1.13.11.20

4xff, 3D-view

1.13.11.20

5ezw, 3D-view

1.13.11.20

5i0s, 3D-view

1.13.11.20

5i0t, 3D-view

1.13.11.20

4xez, 3D-view

1.13.11.20

4xff, 3D-view

1.13.11.20

5ezw, 3D-view

1.13.11.20

5i0s, 3D-view

1.13.11.20

5i0t, 3D-view

1.13.11.20

4xez, 3D-view

1.13.11.20

4xff, 3D-view

1.13.11.20

5ezw, 3D-view

1.13.11.20

5i0s, 3D-view

1.13.11.20

5i0t, 3D-view

1.13.11.20

4xez, 3D-view

1.13.11.20

4xff, 3D-view

1.13.11.20

5ezw, 3D-view

1.13.11.20

5i0s, 3D-view

1.13.11.20

5i0t, 3D-view

1.13.11.20

4xez, 3D-view

1.13.11.20

4xff, 3D-view

1.13.11.20

5ezw, 3D-view

1.13.11.20

5i0s, 3D-view

1.13.11.20

5i0t, 3D-view

1.13.11.20

35 entries

1.15.1.1

1q0k, 3D-view

1.8.2.2

4v2k, 3D-view

1.8.2.2

4wq9, 3D-view

1.8.2.2

4wqc, 3D-view

1.8.2.2

4wqe, 3D-view

1.8.2.2

4v2k, 3D-view

1.8.2.2

4wq9, 3D-view

1.8.2.2

4wqc, 3D-view

1.8.2.2

4wqe, 3D-view

1.8.2.2

4v2k, 3D-view

1.8.2.2

4wq9, 3D-view

1.8.2.2

4wqc, 3D-view

1.8.2.2

4wqe, 3D-view

1.8.2.2

4v2k, 3D-view

1.8.2.2

4wq9, 3D-view

1.8.2.2

4wqc, 3D-view

1.8.2.2

4wqe, 3D-view

1.8.2.2

4v2k, 3D-view

1.8.2.2

4wq9, 3D-view

1.8.2.2

4wqc, 3D-view

1.8.2.2

4wqe, 3D-view

1.8.2.2

4v2k, 3D-view

1.8.2.2

4wq9, 3D-view

1.8.2.2

4wqc, 3D-view

1.8.2.2

4wqe, 3D-view

1.8.2.2

4v2k, 3D-view

1.8.2.2

4wq9, 3D-view

1.8.2.2

4wqc, 3D-view

1.8.2.2

4wqe, 3D-view

1.8.2.2

28 entries

2.4.2.1

2b94, 3D-view

2.7.7.4

1jec, 3D-view

2.9.1.1

3w1j, 3D-view

2.9.1.1

3wcn, 3D-view

2.9.1.1

3wco, 3D-view

2.9.1.1

3w1j, 3D-view

2.9.1.1

3wcn, 3D-view

2.9.1.1

3wco, 3D-view

2.9.1.1

3w1j, 3D-view

2.9.1.1

3wcn, 3D-view

2.9.1.1

3wco, 3D-view

2.9.1.1

3w1j, 3D-view

2.9.1.1

3wcn, 3D-view

2.9.1.1

3wco, 3D-view

2.9.1.1

3w1j, 3D-view

2.9.1.1

3wcn, 3D-view

2.9.1.1

3wco, 3D-view

2.9.1.1

3w1j, 3D-view

2.9.1.1

3wcn, 3D-view

2.9.1.1

3wco, 3D-view

2.9.1.1

3w1j, 3D-view

2.9.1.1

3wcn, 3D-view

2.9.1.1

3wco, 3D-view

2.9.1.1

21 entries

3.1.3.48

3s4o, 3D-view

4.1.1.49

6asm, 3D-view

4.1.1.49

6at2, 3D-view

4.1.1.49

6at3, 3D-view

4.1.1.49

6at4, 3D-view

4.1.1.49

6asm, 3D-view

4.1.1.49

6at2, 3D-view

4.1.1.49

6at3, 3D-view

4.1.1.49

6at4, 3D-view

4.1.1.49

6asm, 3D-view

4.1.1.49

6at2, 3D-view

4.1.1.49

6at3, 3D-view

4.1.1.49

6at4, 3D-view

4.1.1.49

6asm, 3D-view

4.1.1.49

6at2, 3D-view

4.1.1.49

6at3, 3D-view

4.1.1.49

6at4, 3D-view

4.1.1.49

6asm, 3D-view

4.1.1.49

6at2, 3D-view

4.1.1.49

6at3, 3D-view

4.1.1.49

6at4, 3D-view

4.1.1.49

6asm, 3D-view

4.1.1.49

6at2, 3D-view

4.1.1.49

6at3, 3D-view

4.1.1.49

6at4, 3D-view

4.1.1.49

6asm, 3D-view

4.1.1.49

6at2, 3D-view

4.1.1.49

6at3, 3D-view

4.1.1.49

6at4, 3D-view

4.1.1.49

28 entries

Enzyme Kinetic Parameters

k_cat Value (Turnover Number) (28 results)

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Show Turnover Number (28 entries)

EC NUMBER

TURNOVER NUMBER [1/S]

TURNOVER NUMBER MAXIMUM [1/S]

COMMENTARY

LITERATURE

1.8.2.2

350

-

recombinant mutant K208N, pH 5.0, 30°C, with ferricyanide

742887

1.8.2.2

370

-

recombinant mutant K208G, pH 5.0, 30°C, with ferricyanide

742887

1.8.2.2

604

-

pH 4.0, 42°C

726008

1.8.2.2

660

-

recombinant mutant K208N, pH 4.0, 30°C, with ferricyanide

742887

1.8.2.2

760

-

recombinant mutant M209G, pH 5.0, 30°C, with ferricyanide

742887

1.8.2.2

1070

-

recombinant mutant K208G, pH 4.0, 30°C, with ferricyanide

742887

1.8.2.2

1330

-

recombinant mutant M209G, pH 4.0, 30°C, with ferricyanide

742887

1.8.2.2

2100

-

recombinant wild-type enzyme, pH 5.0, 30°C, with ferricyanide

742887

1.8.2.2

2300

-

-

394128

1.8.2.2

8500

-

at pH 7

394126

1.8.2.2

11000

-

-

676077

1.8.2.2

14000

-

pH 4.0, 30°C

724861

1.8.2.2

14000

-

recombinant wild-type enzyme, pH 4.0, 30°C, with ferricyanide

742887

1.8.2.2

250000

-

at least, at pH 3

394126

1.8.5.2

167

-

-

656833

1.8.5.2

167

-

80°C, pH 6.0

656833

2.5.1.47

0.72

-

30°C, pH 8.0

721306

2.5.1.47

24

-

synthesis of S-sulfo-L-cysteine

637385

2.8.1.1

2.8

-

pH 9

645520

2.8.1.1

4

-

pH 9

645520

2.8.1.1

10.7

-

pH 9

645520

2.8.1.1

230

-

2°C, pH 8.6

645532

2.8.1.1

260

-

-

645518

2.8.1.1

400

-

in 100 mM Tris-HCl, pH 9.0, 10 mM KCN, at 85°C

724480

1.8.2.2

14 entries

1.8.5.2

2 entries

2.5.1.47

2 entries

2.8.1.1

6 entries

2.8.1.2

11.3

-

pH 8.4, 30°C

704585

2.8.1.3

0.43

-

37°C, pH 7.4

761486

2.8.5.1

0.457

-

mutant enzyme R243A, at pH 9.0 and 22°C

748092

2.8.5.1

0.913

-

wild type enzyme, at pH 9.0 and 22°C

748092

2.8.5.1

2 entries

K_M Value (93 results)

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Show KM Value (93 entries)

EC NUMBER

KM VALUE [MM]

KM VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

1.8.2.2

0.004

-

with cytochrome c as electron acceptor

288769

1.8.2.2

0.005

-

cytochrome c as electron acceptor

394124

1.8.2.2

0.1

-

ferricyanide as electron acceptor

394124

1.8.2.2

0.11

-

with ferricyanide as electron acceptor

288769

1.8.2.2

0.12

-

at pH 7.5

394128

1.8.2.2

0.14

-

recombinant wild-type enzyme, pH 5.0, 30°C, with ferricyanide

742887

1.8.2.2

0.14

-

with native cytochrome c as electron acceptor

394078

1.8.2.2

0.16

-

with ferricyanide as electron acceptor

394078

1.8.2.2

0.17

-

recombinant mutant K208N, pH 5.0, 30°C, with ferricyanide

742887

1.8.2.2

0.2

-

pH 4.0, 42°C

726008

1.8.2.2

0.46

-

recombinant mutant K208G, pH 5.0, 30°C, with ferricyanide

742887

1.8.2.2

0.54

-

at pH 7

394126

1.8.2.2

0.62

-

-

394115

1.8.2.2

0.67

-

-

394116

1.8.2.2

0.9

-

-

394125

1.8.2.2

0.9

-

recombinant mutant M209G, pH 4.0, 30°C, with ferricyanide

742887

1.8.2.2

1.08

-

recombinant mutant M209G, pH 5.0, 30°C, with ferricyanide

742887

1.8.2.2

1.1

-

recombinant mutant K208G, pH 4.0, 30°C, with ferricyanide

742887

1.8.2.2

1.1

-

recombinant wild-type enzyme, pH 4.0, 30°C, with ferricyanide

742887

1.8.2.2

1.3

-

recombinant mutant K208N, pH 4.0, 30°C, with ferricyanide

742887

1.8.2.2

1.57

-

pH 6.1-6.3, 30°C

394122

1.8.2.2

8

-

recombinant protein, pH 2.5, 50°C

724028

1.8.2.2

15

-

native protein, pH 2.5, 50°C

724028

1.8.2.2

23 entries

1.8.2.5

0.5

-

37°C, pH 7.6

739959

1.8.5.2

2.6

-

-

656833

1.8.5.2

2.6

-

80°C, pH 6.0

656833

1.8.5.2

8

-

recombinant enzyme, at pH 2.5 and 50°C

724028

1.8.5.2

15

-

native enzyme, at pH 2.5 and 70°C

724028

1.8.5.2

4 entries

1.8.99.B2

0.81

-

-

394129

2.5.1.144

1.9

-

pH and temperature not specified in the publication

746931

2.5.1.144

2.7

-

at pH 7.6, temperature not specified in the publication

748059

2.5.1.47

0.93

-

-

706226

2.5.1.47

21

-

synthesis of S-sulfo-L-cysteine

637385

2.5.1.47

22

-

30°C, pH 8.0

721306

2.5.1.65

0.044

-

pH 7.0, 22°C, recombinant wild-type enzyme

738534

2.5.1.65

0.214

-

pH 7.0, 22°C, recombinant mutant R243A enzyme

738534

2.5.1.65

0.374

-

dephosphorylation, pH 7.0, 22°C, recombinant wild-type enzyme

738534

2.8.1.1

0.53

-

40°C, pH 9.5

645517

2.8.1.1

0.7

-

pH 9

645520

2.8.1.1

1

-

-

645516

2.8.1.1

1

-

25°C, pH 7.3

660889

2.8.1.1

1

-

apparent value, in 100 mM Tris-HCl, pH 9.0, 10 mM KCN, at 85°C

724480

2.8.1.1

1.1

-

pH 9

645520

2.8.1.1

2.5

-

mutant E102D, 30°C, pH 5.0

677214

2.8.1.1

2.89

-

pH 8.0, 37°C

762459

2.8.1.1

3.2

-

17°C, pH 8.5

645519

2.8.1.1

3.4

-

wild-type, 30°C, pH 5.0

677214

2.8.1.1

3.7

-

pH 7.5, wild-type

645527

2.8.1.1

4

-

-

645519

2.8.1.1

4

-

25°C, pH 8.5

645503

2.8.1.1

4.58

-

37°C, pH 6.5, cytosolic enzyme of p-dimethylaminoazobenzene-treated mice

645538

2.8.1.1

4.6

-

25°C, pH 8.6

645533

2.8.1.1

4.8

-

mutant P285A, 30°C, pH 5.0

677214

2.8.1.1

5.6

-

mutant rhodanese

645531

2.8.1.1

5.7

-

pH 9.0, 80°C

673600

2.8.1.1

7.4

-

25°C, pH 8.6

660889

2.8.1.1

7.4

-

pH 9

645520

2.8.1.1

7.9

-

recombinant rhodanese

645531

2.8.1.1

8.3

-

25°C, pH 8.5

645513

2.8.1.1

8.3

-

25°C, pH 9.4

645536

2.8.1.1

9.2

-

recombinant rhodanese

645531

2.8.1.1

9.3

-

liver rhodanese

645531

2.8.1.1

15.9

-

liver rhodanese

645508

2.8.1.1

16.8

-

recombinant rhodanese

645508

2.8.1.1

19.5

-

-

662068

2.8.1.1

22

-

cosubstrate cyanide, 37°C, pH 7.4

761486

2.8.1.1

22

-

cosubstrate thioredoxin, 37°C, pH 7.4

761486

2.8.1.1

22.7

-

-

645500

2.8.1.1

26.9

-

mitochondrial enzyme

645498

2.8.1.1

31.75

-

37°C, pH 6.5, mitochondrial enzyme of p-dimethylaminoazobenzene-treated mice

645538

2.8.1.1

35.7

-

-

645500

2.8.1.1

65.66

-

37°C, pH 6.5, cytosolic enzyme of untreated mice

645538

2.8.1.1

73.2

-

pH 7.5, R186L

645527

2.8.1.1

78

-

2°C, pH 8.6

645532

2.8.1.1

127.8

-

cytosolic

645500

2.8.1.1

190

-

37°C, pH 6.5, mitochondrial enzyme of untreated mice

645538

2.8.1.1

236

-

25°C, cytosolic enzyme of cholestatic liver

645540

2.8.1.1

247

-

25°C, cytosolic enzyme of apparently operated liver

645540

2.8.1.1

252

-

25°C, mitochondrial enzyme of cholestatic liver

645540

2.8.1.1

265

-

25°C, mitochondrial enzyme of apparently operated liver

645540

2.8.1.1

581

-

25°C, microsomal enzyme of cholestatic liver

645540

2.8.1.1

603

-

25°C, microsomal enzyme of apparently operated liver

645540

2.8.1.2

1.7

-

pH 7.3, 37°C

645569

2.8.1.2

266

-

pH 8.4, 30°C

704585

2.8.1.3

2.9

-

pH 8.1, 37°C

645572

2.8.1.3

3.2

-

pH 8.5, 27°C

645519

2.8.1.3

17

-

cosubstrate glutathione, 37°C, pH 7.4

761486

2.8.1.5

0.1

-

with dithioerythritol as second substrate

645577

2.8.1.5

0.156

-

pH 9, 37°C, with dithioerythritol as second substrate, isoenzyme TSR II

645575

2.8.1.5

0.164

-

pH 9, 37°C, with dithioerythritol as second substrate, isoenzyme TSR I

645575

2.8.1.5

0.29

-

pH 6, 45°C

645579

2.8.5.1

0.0439

-

wild type enzyme, at pH 9.0 and 22°C

748092

2.8.5.1

0.2137

-

mutant enzyme R243A, at pH 9.0 and 22°C

748092

2.5.1.144

2 entries

2.5.1.47

3 entries

2.5.1.65

3 entries

2.8.1.1

45 entries

2.8.1.2

2 entries

2.8.1.3

3 entries

2.8.1.5

4 entries

2.8.5.1

2 entries

K_i Value (3 results)

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Show KI Value (3 entries)

EC NUMBER

KI VALUE [MM]

KI VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

2.7.7.4

0.36

-

pH 8.0, 30°C

641208

2.7.7.4

0.4

-

pH 8.0, 30°C

641208, 643276

2.7.7.4

1.13

-

pH 8.0, 30°C

641204

2.7.7.4

3 entries

References & Links

Literature References (173)

top print hide

Show Reference (173 entries)

BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

PAGES

3718

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Metabolism of aromatic compounds by fungi. Kinetic properties and mechanism of 3-carboxy-cis,cis-muconate cyclase from Aspergillus niger

1975

Thatcher, D.R.; Cain, R.B.

Eur. J. Biochem.

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135581

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N-Acetylglucosamine-6-sulfate sulfatase from human urine

1979

Basner, R.; Kresse, H.; von Figura, K.

J. Biol. Chem.

254

1151-1158

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Purification and properties of N-acetylgalactosamine 6-sulphate sulphatase from human placenta

1979

Gloessl, J.; Truppe, W.; Kresse, H.

Biochem. J.

181

37-46

210682

3651424

Interaction of mono- and dianions with cyanase: evidence for apparent half-site binding

1987

Anderson, P.M.; Johnson, W.V.; Endrizzi, J.A.; Little, R.M.; Korte, J.J.

Biochemistry

26

3938-3943

288769

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Cellular location and partial purification of the 'thiosulphate-oxidizing enzyme' and the 'trithionate hydrolase' from Thiobacillus tepidarius

1988

Lu, W.P.; Kelly, D.P.

J. Gen. Microbiol.

134

877-885

288770

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Purification and partial characterization from the acidophilic sulphur oxidizer Thiobacillus acidophilus

1992

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Eur. J. Biochem.

209

367-374

390487

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Properties of formaldehyde dismutation catalyzing enzyme of Pseudomonas putida F61

1984

Kato, N.; Kobayashi, H.; Shimano, M.; Sakazawa, C.

Agric. Biol. Chem.

48

2017-2023

393404

16346366

Purification and characterization of alpha-amylase from Bacillus licheniformis CUMC305

1983

Krishnan, T.; Chandra, A.K.

Appl. Environ. Microbiol.

46

430-437

394078

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Properties of an enzymatic complex active in sulfite and thiosulfate oxidation by Rhodotorula sp.

1985

Kurek, E.J.

Arch. Microbiol.

143

277-282

394115

-

The role of thiosulfate in sulfur metabolism of Rhodopseudomonas globiformis

1981

Then, J.; Truper, H.G.

Arch. Microbiol.

130

143-146

394116

40955

Partial purification and characterization of thiosulfate oxidase from Pseudomonas aeruginosa

1979

Schook, L.B.; Berk, R.S.

J. Bacteriol.

140

306-308

394117

-

A high potential nonheme iron protein (HiPIP)-Linked, thiosulfate-oxidizing enzyme derived from Chromatium vinosum

1979

Fukumori, Y.; Yamanaka, T.

Curr. Microbiol.

3

117-120

394118

-

Kinetic and energetic aspects of inorganic sulphur compound oxidation by Thiobacillus tepidarius

1988

Lu, W.P.; Kelly, D.P.

J. Gen. Microbiol.

134

865-876

394119

6020561

Metabolism of thiosulfate and tetrathionate by heterotrophic bacteria from soil

1967

Trudinger, P.A.

J. Bacteriol.

93

550-559

394120

4215368

Mechanisms of inorganic oxidation and energy coupling

1974

Suzuki, I.

Annu. Rev. Microbiol.

28

85-101

394121

13778251

Thiosulfate oxidation and cytochromes in Thiobacillus X

1961

Trudinger, P.A.

Biochem. J.

78

680-686

394122

16346367

Some properties of thiosulfate-oxidizing enzyme from marine heterotroph 16B

1983

Tuttle, J.H.; Schwartz, J.H.; Whited, G.M.

Appl. Environ. Microbiol.

46

438-445

394123

5018699

Thiosulfate oxidase from an Alcaligenes grown on mercaptosuccinate

1972

Hall, M.R.; Berk, R.S.

Can. J. Microbiol.

18

235-245

394124

5438323

Enzymes involved in the metabolism of thiosulfate by Thiobacillus thioparus. 3. Properties of thiosulfate-oxidizing enzyme and proposed pathway of thiosulfate oxidation

1970

Lyric, R.M.; Suzuki, I.

Can. J. Biochem.

48

355-363

394125

5687645

The thiosulfate-oxidizing enzyme of Ferrobacillus ferrooxidans (Thiobacillus ferrooxidans)

1968

Silver, M.; Lundgren, D.G.

Can. J. Biochem.

46

1215-1220

394126

-

Purification and partial characterization of thiosulfate dehydrogenase from Thiobacillus acidophilus

1993

Meulenberg, R.; Pronk, J.T.; Hazeu, W.; van Dijken, J.P.; Frank, J.; Bos, P.; Kuenen, J.G.

J. Gen. Microbiol.

139

2033-2039

394128

9082913

Purification and characterization of a periplasmic thiosulfate dehydrogenase from the obligately autotrophic Thiobacillus sp. W5

1996

Visser, J.M.; De Jong, G.A.H.; Robertson, L.A.; Kuenen, J.G.

Arch. Microbiol.

166

372-378

394129

11272812

Purification and properties of thiosulfate dehydrogenase from Acidithiobacillus thiooxidans JCM7814

2001

Nakamura, K.; Nakamura, M.; Yoshikawa, H.; Amano, Y.

Biosci. Biotechnol. Biochem.

65

102-108

441605

7608089

Sulfate and thiosulfate transport in Escherichia coli K-12: evidence for a functional overlapping of sulfate- and thiosulfate-binding proteins

1995

Sirko, A.; Zatyka, M.; Sadowy, E.; Hulanicka, D.

J. Bacteriol.

177

4134-4136

441606

2002055

Engineered interdomain disulfide in the perplasmic receptor for sulfate transport reduces flexibility. Site-directed mutagenesis and ligand-binding studies

1991

Jacobson, B.L.; He, J.J.; Vermersch, P.S.; Lemon, D.D.; Quiocho, F.A.

J. Biol. Chem.

266

5220-5225

441607

1708375

Characterization and mutagenesis of sulfur-regulated genes in a Cyanobacterium: evidence for function in sulfate transport

1991

Laudenbach, D.E.; Grossmann, A.R.

J. Bacteriol.

173

2739-2750

441608

2188959

Sulfate and thiosulfate transport in Escherichia coli K-12: identification of a gene encoding a novel protein involved in thiosulfate binding

1990

Hryniewicz, M.; Sirko, A.; Palucha, A.; Boeck, A.; Hulanicka, D.

J. Bacteriol.

172

3358-3366

636851

-

The purification and properties of a thiaminase I enzyme from nardoo (Marsilea Drumondii)

1977

McCleary, B.V.; Chick, B.F.

Phytochemistry

16

207-213

637347

6373737

Enzymatic proof for the identity of the S-sulfocysteine synthase and cysteine synthase B of Salmonella typhimurium

1984

Nakamura, T.; Iwahashi, A.; Eguchi, Y.

J. Bacteriol.

158

1122-1127

637385

12644499

Characterization of a novel thermostable O-acetylserine sulfhydrylase from Aeropyrum pernix K1

2003

Mino, K.; Ishikawa, K.

J. Bacteriol.

185

2277-2284

641204

2537056

Rat liver ATP-sulfurylase: purification, kinetic characterization, and interaction with arsenate, selenate, phosphate, and other inorganic oxyanions

1989

Yu, M.; Martin, R.L.; Jain, S.; Chen, L.J.; Segel, I.H.

Arch. Biochem. Biophys.

269

156-174

641208

2997125

Comparative stability and catalytic and chemical properties of the sulfate-activating enzymes from Penicillium chrysogenum (mesophile) and Penicillium duponti (thermophile)

1985

Renosto, F.; Schultz, T.; Re, E.; Mazer, J.; Chandler, C.J.; Barron, A.; Segel, I.H.

J. Bacteriol.

164

674-683

642097

16667036

Properties of pyrophosphate:D-fructose-6-phosphate phosphotransferase from endosperm of developing wheat (Triticum aestivum L.) grains

1989

Mahajan, R.; Singh, R.

Plant Physiol.

91

421-426

643258

2162344

Regulation of inorganic sulfate activation in filamentous fungi. Allosteric inhibition of ATP sulfurylase by 3-phosphoadenosine-5-phosphosulfate

1990

Renosto, F.; Martin, R.L.; Wailes, L.M.; Daley, L.A.; Segel, I.H.

J. Biol. Chem.

265

10300-10308

643266

6312889

ATP sulfurylase from Penicillium chrysogenum: measurements of the true specific activity of an enzyme subject to potent product inhibition and a reassessment of the kinetic mechanism

1983

Seubert, P.A.; Hoang, L.; Renosto, F.; Segel, I.H.

Arch. Biochem. Biophys.

225

679-691

643276

-

Sulfate activation in Rhodobacter sulfidophilus

1985

Cooper, B.P.; Trüper, H.G.

Arch. Microbiol.

141

384-391

645495

6938201

Identity of beta-mercaptopyruvate sulfurtransferase and rhodanese in human erythrocytes

1980

Scott, E.M.; Wright, R.C.

Biochem. Biophys. Res. Commun.

97

1334-1338

645496

8490572

Properties of Azotobacter vinelandii rhodanese

1993

Pagani, S.; Sessa, G.; Sessa, F.; Colnaghi, R.

Biochem. Mol. Biol. Int.

29

595-604

645497

-

Porphyrin biosynthesis in Rp. palustris. X. Purification and some properties of rhodanese

1987

Vazquez, E.S.; Buzaleh, A.M.; Wider, E.A.; Battle, A.M.Del C.

Int. J. Biochem.

19

1193-1197

645498

-

Comparison of some molecular and catalytic properties of mitochondrial and cytosolic rhodanese and mercaptopyruvate sulphurtransferase from frog (Rana temporaria) liver

1984

Wrobel, M.; Frendo, J.

Bull. Pol. Acad. Sci. Biol. Sci.

32

303-313

645499

6586594

Rhodanese from Cercopithecus aethiops (vervet monkey) liver. I. Purification and some physical characteristics

1984

Van Rensburg, L.J.; Schabort, J.C.

Int. J. Biochem.

16

539-546

645500

6286464

A comparison of some biochemical properties of liver thiosulphate sulphurtransferase from guinea pig (Lepus caniculus) & albino rat

1982

Anosike, E.O.; Jack, A.S.

Indian J. Biochem. Biophys.

19

13-16

645501

5047825

Crystalline rhodanese from beef kidney

1972

Cannella, C.; Pecci, L.; Federici, G.

Ital. J. Biochem.

21

1-7

645502

4583640

Rhodanese

1973

Westley, J.

Adv. Enzymol. Relat. Areas Mol. Biol.

39

327-368

645503

6948991

Thiosulfate: cyanide sulfurtransferase (rhodanese)

1981

Westley, J.

Methods Enzymol.

77

285-291

645504

5135514

Crystallographic data for rhodanese from bovine liver

1971

Drenth, J.; Smit, J.D.G.

Biochem. Biophys. Res. Commun.

45

1320-1322

645505

3477679

Chromogenic and fluorigenic substrates for sulfurtransferases

1987

Burrous, M.R.; Lane, J.; Westley, A.; Westley, J.

Methods Enzymol.

143

235-239

645506

4426888

Inhibition of bovine liver rhodanese by alpha-ketoglutarate

1974

Oi, S.

J. Biochem.

76

455-458

645507

6402017

The inhibition of rhodanese by lipoate and iron-sulfur proteins

1983

Pagani, S.; Bonomi, F.; Cerletti, P.

Biochim. Biophys. Acta

742

116-121

645508

1627606

Recombinant bovine rhodanese: purification and comparison with bovine liver rhodanese

1992

Miller, D.M.; Kurzban, G.P.; Mendoza, J.A.; Chirgwin, J.M.; Hardies, S.C.; Horowitz, P.M.

Biochim. Biophys. Acta

1121

286-292

645509

2002017

Expression of cloned bovine adrenal rhodanese

1991

Miller, D.M.; Delgado, R.; Chirgwin, J.M.

J. Biol. Chem.

266

4686-4691

645510

6930969

Some comparisons between solution and crystal properties of thiosulfate sulfurtransferase

1980

Horowitz, P.M.; Patel, K.

Biochem. Biophys. Res. Commun.

94

419-423

645511

1213990

Inhibition of rat liver rhodanese by di-, tricarboxylic, and alpha-keto acids

1975

Oi, S.

J. Biochem.

78

825-834

645512

-

Purification of tapioca leaf rhodanese

1976

Boey, C.G.; Yeoh, H.H.; Chew, M.Y.

Phytochemistry

15

1343-1344

645513

-

Purification and some properties of Trametes sanguinea rhodanese

1973

Oi, S.

Agric. Biol. Chem.

37

629-635

645514

1953758

Cloning and sequence analysis of the human liver rhodanese: comparison with the bovine and chicken enzymes

1991

Pallini, R.; Guazzi, G.C.; Cannella, C.; Cacace, M.G.

Biochem. Biophys. Res. Commun.

180

887-893

645515

6931629

Purification and characterization of rhodanese from Acinetobacter calcoaceticus

1980

Vandenbergh, P.A.; Berk, R.S.

Can. J. Microbiol.

26

281-286

645516

-

Purification and some properties of thiosulphate-cleaving enzyme from Thiobacillus novellus

1989

Fukumori, Y.; Hoshiko, K.; Yamanaka, T.

FEMS Microbiol. Lett.

65

159-164

645517

-

Properties of a soluble thiosulfate sulfur transferase (rhodanese) of the marine methanogen Methanosarcina frisia

1991

Turkowsky, A.; Blotevogel, K.H.; Fischer, U.

FEMS Microbiol. Lett.

81

251-256

645518

3553189

Properties of an Escherichia coli rhodanese

1987

Alexander, K.; Volini, M.

J. Biol. Chem.

262

6595-6604

645519

3480285

Isolation and characterization of a prokaryotic sulfurtransferase

1987

Aird, B.A.; Heinrikson, R.L.; Westley, J.

J. Biol. Chem.

262

17327-17335

645520

12482606

Identification and characterization of single-domain thiosulfate sulfurtransferases from Arabidopsis thaliana

2002

Bauer, M.; Papenbrock, J.

FEBS Lett.

532

427-431

645521

12821142

Inhibition of Azotobacter vinelandii rhodanese by NO-donors

2003

Spallarossa, A.; Forlani, F.; Pagani, S.; Salvati, L.; Visca, P.; Ascenzi, P.; Bolognesi, M.; Bordo, D.

Biochem. Biophys. Res. Commun.

306

1002-1007

645522

10788632

Mutagenic analysis of Thr-232 in rhodanese from Azotobacter vinelandii highlighted the differences of this prokaryotic enzyme from the known sulfurtransferases

2000

Pagani, S.; Forlani, F.; Carpen, A.; Bordo, D.; Colnaghi, R.

FEBS Lett.

472

307-311

645523

14519133

Azotobacter vinelandii rhodanese: Selenium loading and ion interaction studies

2003

Melino, S.; Cicero, D.O.; Orsale, M.; Forlani, F.; Pagani, S.; Paci, M.

Eur. J. Biochem.

270

4208-4215

645524

10762072

Rhodanese as a thioredoxin oxidase

2000

Nandi, D.L.; Horowitz, P.M.; Westley, J.

Int. J. Biochem. Cell Biol.

32

465-473

645525

12433928

Active rhodanese lacking nonessential sulfhydryl groups contains an unstable C-terminal domain and can be bound, inactivated, and reactivated by GroEL*

2003

Ybarra, J.; Bhattacharyya, A.M.; Panda, M.; Horowitz, P.M.

J. Biol. Chem.

278

1693-1699

645526

10318804

NH2-terminal sequence truncation decreases the stability of bovine rhodanese, minimally perturbs its crystal structure, and enhances interaction with GroEL under native conditions

1999

Trevino, R.J.; Gliubich, F.; Berni, R.; Cianci, M.; Chirgwin, J.M.; Zanotti, G.; Horowitz, P.M.

J. Biol. Chem.

274

13938-13947

645527

8132546

The sulfurtransferase activity and structure of rhodanese are affected by site-directed replacement of Arg-186 or Lys-249

1994

Luo, G.X.; Horowitz, P.M.

J. Biol. Chem.

269

8220-8225

645528

8106382

Mutations of noncatalytic sulfhydryl groups influence the stability, folding, and oxidative susceptibility of rhodanese

1994

Miller-Martin, D.M.; Chirgwin, J.M.; Horowitz, P.M.

J. Biol. Chem.

269

3423-3428

645529

11368014

An additional serine residue at the C terminus of rhodanese destabilizes the enzyme

2001

Kramer, G.; Ramachandiran, V.; Horowitz, P.; Hardesty, B.

Arch. Biochem. Biophys.

385

332-337

645530

-

Distribution of rhodanese in tissues of goat (Capra hircus)

2003

Nazifi, S.; Aminlari, M.; Alaibakhsh, M.A.

Comp. Biochem. Physiol. B

134B

515-518

645531

8535164

Chinese hamster rhodanese cDNA: activity of the expressed protein is not blocked by a C-terminal extension

1995

Trevino, R.J.; Hunt, J.; Horowitz, P.M.; Chirgwin, J.M.

Protein Expr. Purif.

6

693-699

645532

10735872

Characterization of a 12-kilodalton rhodanese encoded by glpE of Escherichia coli and its interaction with thioredoxin

2000

Ray, W.K.; Zeng, G.; Potters, M.B.; Mansuri, A.M.; Larson, T.J.

J. Bacteriol.

182

2277-2284

645533

11997041

PspE (phage-shock protein E) of Escherichia coli is a rhodanese

2002

Adams, H.; Teertstra, W.; Koster, M.; Tommassen, J.

FEBS Lett.

518

173-176

645534

-

Effects of thiazolidine-4(R)-carboxylates and other low-molecular-weight sulfur compounds on the activity of mercaptopyruvate sulfurtransferase, rhodanese, and cystathionase in Ehrlich ascites tumor cell and tumor-bearing mouse liver

1997

Wrobel, M.; Wlodek, L.

Amino Acids

12

309-314

645535

11788560

Mucosal protection against sulphide: Importance of the enzyme rhodanese

2002

Picton, R.; Eggo, M.C.; Merrill, G.A.; Langman, M.J.S.; Singh, S.

Gut

50

201-205

645536

-

Purification and characterization of mouse liver rhodanese

1995

Lee, C.Y.; Hwang, J.H.; Lee, Y.S.; Cho, K.S.

J. Biochem. Mol. Biol.

28

170-176

645537

10763118

Rhodanese activity and total sulfur content in frog and mouse liver

2000

Wrobel, M.; Papla, B.

Folia Histochem. Cytobiol.

38

11-17

645538

7641082

Isolation and partial purification of mitochondrial and cytosolic rhodanese from liver of normal and p-dimethylaminoazobenzene treated mice

1995

Vazquez, E.; Polo, C.; Stedile, G.; Schebor, C.; Karahanian, E.; Batlle, A.

Int. J. Biochem. Cell Biol.

27

523-529

645539

9224564

Mitochondrial and cytosolic rhodanese from liver of DAB-treated mice. III. Inhibition kinetic studies

1997

Vazquez, E.; Gazzaniga, S.; Polo, C.; Batlle, A.

Cancer Biochem. Biophys.

15

285-293

645540

-

Thiosulfate sulfurtransferase and UDP-glucuronosyltransferase activities in cholestatic rat liver induced by common bile duct ligation

1997

Ihm, J.S.; Kim, Y.H.

Exp. Mol. Med.

29

197-201

645541

-

Characterization of the rhodanese enzyme in Trichoderma spp

2003

Ezzi, M.I.; Pascual, J.A.; Gould, B.J.; Lynch, J.M.

Enzyme Microb. Technol.

32

629-634

645542

8291063

The cyanide-metabolizing enzyme rhodanese in different parts of the respiratory systems of sheep and dog

1994

Aminlari, M.; Vaseghi, T.; Ali Kargar, M.

Toxicol. Appl. Pharmacol.

124

67-71

645543

9405422

Renaturation of rhodanese by translational elongation factor (EF) Tu. Protein refolding by EF-Tu flexing

1997

Kudlicki, W.; Coffman, A.; Kramer, G.; Hardesty, B.

J. Biol. Chem.

272

32206-32210

645544

10788330

The crystal structure of a sulfurtransferase from Azotobacter vinelandii highlights the evolutionary relationship between the rhodanese and phosphatase enzyme families

2000

Bordo, D.; Deriu, D.; Colnaghi, R.; Carpen, A.; Pagani, S.; Bolognesi, M.

J. Mol. Biol.

298

691-704

645545

9761843

Structure of sulfur-substituted rhodanese at 1.36 A resolution

1998

Gliubich, F.; Berni, R.; Colapietro, M.; Barba, L.; Zanotti, G.

Acta Crystallogr. Sect. D

54

481-486

645546

11254178

Tissue and intracellular distribution of rhodanese and mercaptopyruvate sulfurtransferase in ruminants and birds

2001

Al-Qarawi, A.A.; Mousa, H.M.; Ali, B.H.

Vet. Res.

32

63-70

645569

12419809

3-Mercaptopyruvate sulfurtransferase of Leishmania contains an unusual C-terminal extension and is involved in thioredoxin and antioxidant metabolism

2003

Williams, R.A.; Kelly, S.M.; Mottram, J.C.; Coombs, G.H.

J. Biol. Chem.

278

1480-1486

645570

383018

Purification and steady-state kinetic analysis of yeast thiosulfate reductase

1979

Uhteg, L.; Westley, J.

Arch. Biochem. Biophys.

195

211-222

645571

6849932

Improved purification and sulfhydryl analysis of thiosulfate reductase

1983

Chauncey, T.R.; Westley, J.

Biochim. Biophys. Acta

744

304-311

645572

6361026

The catalytic mechanism of yeast thiosulfate reductase

1983

Chauncey, T.R.; Westley, J.

J. Biol. Chem.

258

15037-15045

645575

24253096

Isolation and characterization of thiosulfate reductases from the green alga Chlorella fusca

1984

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