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Ligand arsenite

Basic Ligand Information

Molecular Structure

Show all BRENDA pathways known for arsenite

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Roles as Enzyme Ligand

In Vivo Substrate in Enzyme-catalyzed Reactions (11 results)

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Show Natural Substrate (11 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.20.2.1

arsenite + cytochrome c-551 + H2O = arsenate + reduced cytochrome c-551

658195

-

1.20.2.1

arsenite + cytochrome c552 + H2O = arsenate + reduced cytochrome c552

714304

-

1.20.4.1

arsenite + acceptor = arsenate + reduced acceptor

745405

1sjz, 3D-view

1.20.4.1

arsenite + acceptor = arsenate + reduced acceptor

745405

1sk0, 3D-view

1.20.99.1

arsenite + acceptor = arsenate + reduced acceptor

746413, 744726, 745124, 745908, 746165, 744115, 658052, 287858

-

1.20.99.1

arsenite + azurin + H2O = arsenate + reduced azurin

658961

-

1.20.99.1

arsenite + cytochrome c + H2O = arsenate + reduced cytochrome c

658961

-

1.20.99.1

arsenite + cytochrome c-551 = arsenate + reduced cytochrome c-551

658195

-

1.20.2.1

2 entries

1.20.4.1

2 entries

1.20.99.1

4 entries

2.1.1.137

S-adenosyl-L-methionine + arsenite = S-adenosyl-L-homocysteine + methylarsonate

485149, 485151, 485152, 733203, 733950, 485148, 733740, 701300, 733425, 733451, 733865, 734199, 735126, 735309, 695519, 733887, 733175, 733333, 674763, 673066, 676841, 697642

-

7.3.2.7

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

210282, 696278, 718867, 718868, 719037, 719612, 733473, 718876, 733712, 719496, 697072, 210285, 210286, 210281, 210279, 687482, 687554, 686653, 689052, 689739, 699223, 719132

-

7.3.2.7

ATP + H2O + arsenite[side 1] = ADP + phosphate + arsenite[side 2]

751204, 750678

-

7.3.2.7

2 entries

In Vivo Product in Enzyme-catalyzed Reactions (14 results)

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Show Natural Product (14 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.20.4.1

arsenate + glutaredoxin = arsenite + glutaredoxin disulfide + H2O

0

1sjz, 3D-view

1.20.4.1

arsenate + glutaredoxin = arsenite + glutaredoxin disulfide + H2O

0

1sk0, 3D-view

1.20.4.1

arsenate + reduced acceptor = arsenite + acceptor

0

1sjz, 3D-view

1.20.4.1

arsenate + reduced acceptor = arsenite + acceptor

0

1sk0, 3D-view

1.20.4.1

arsenate + reduced glutaredoxin = arsenite + oxidized glutaredoxin

639364, 639365, 639366, 639367, 639371

1sjz, 3D-view

1.20.4.1

arsenate + reduced glutaredoxin = arsenite + oxidized glutaredoxin

639364, 639365, 639366, 639367, 639371

1sk0, 3D-view

1.20.4.1

arsenate + reduced glutathione = arsenite + glutathione

0

1sjz, 3D-view

1.20.4.1

arsenate + reduced glutathione = arsenite + glutathione

0

1sk0, 3D-view

1.20.4.1

8 entries

1.20.4.3

arseno-mycothiol + mycoredoxin = arsenite + mycothiol-mycoredoxin disulfide

0

-

1.20.4.4

arsenate + thioredoxin = arsenite + thioredoxin disulfide + H2O

0

-

1.20.99.1

arsenate + acetate = arsenite + ?

287859

-

1.20.99.1

arsenate + reduced acceptor = arsenite + acceptor

0

-

7.3.2.7

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

0

-

7.3.2.7

ATP + H2O + arsenite[side 1] = ADP + phosphate + arsenite[side 2]

0

-

1.20.99.1

2 entries

7.3.2.7

2 entries

Substrate in Enzyme-catalyzed Reactions (25 results)

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Show Substrate (25 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.20.2.1

arsenite + cytochrome c + H2O = arsenate + reduced cytochrome c

714304

-

1.20.2.1

arsenite + cytochrome c-551 + H2O = arsenate + reduced cytochrome c-551

658195

-

1.20.2.1

arsenite + cytochrome c552 + H2O = arsenate + reduced cytochrome c552

714304

-

1.20.2.1

arsenite + H2O + 2,6-dichlorophenolindophenol = arsenate + reduced 2,6-dichlorophenolindophenol

658195, 713822, 715352

-

1.20.4.1

arsenite + acceptor = arsenate + reduced acceptor

745405

1sjz, 3D-view

1.20.4.1

arsenite + acceptor = arsenate + reduced acceptor

745405

1sk0, 3D-view

1.20.9.1

arsenite + 2,6-dichlorophenol indophenol = arsenate + reduced 2,6-dichlorophenol indophenol

696599

-

1.20.9.1

arsenite + H2O + azurin(ox) = arsenate + azurin(red)

690420, 692109

-

1.20.9.1

arsenite + H2O + azurin(oxidized) = arsenate + azurin(reduced)

287857, 287858

-

1.20.99.1

arsenite + acceptor = arsenate + reduced acceptor

287858, 658052, 746413, 744726, 745124, 745908, 746165, 744115

-

1.20.99.1

arsenite + azurin + H2O = arsenate + reduced azurin

658961

-

1.20.99.1

arsenite + cytochrome c + H2O = arsenate + reduced cytochrome c

658961

-

1.20.99.1

arsenite + cytochrome c-551 = arsenate + cytochrome c-551

658195

-

1.20.99.1

arsenite + cytochrome c-551 = arsenate + reduced cytochrome c-551

658195

-

1.20.99.1

arsenite + oxidized 2,6-dichlorophenolindophenol = arsenate + reduced 2,6-dichlorophenolindophenol

696045

-

2.1.1.137

S-adenosyl-L-methionine + arsenite = S-adenosyl-L-homocysteine + methylarsenate

757317

-

2.1.1.137

S-adenosyl-L-methionine + arsenite = S-adenosyl-L-homocysteine + methylarsenate(III)

755717

-

2.1.1.137

S-adenosyl-L-methionine + arsenite = S-adenosyl-L-homocysteine + methylarsonate

673463, 485149, 657702, 658442, 673066, 674763, 718712, 719012, 485151, 485152, 733203, 733950, 485148, 733740, 658444, 659168, 697642, 701300, 733425, 733451, 733865, 734199, 735126, 735309, 695519, 733887, 733175, 733333, 757684, 676841

-

2.1.1.137

S-adenosyl-L-methionine + arsenite = S-adenosyl-L-homocysteine + methylarsonate + dimethylarsinate + trimethylarsine

718946

-

2.1.1.137

S-adenosyl-L-methionine + arsenite = S-adenosyl-L-homocysteine + methylarsonate + dimethylarsinous acid + dimethylarsinic acid

721075

-

2.1.1.137

S-adenosyl-L-methionine + arsenite = S-adenosyl-L-homocysteine + monomethylarsonate + dimethylarsinic acid

718748, 719007

-

2.1.1.137

S-adenosyl-L-methionine + arsenite = S-adenosyl-L-homocysteine + monomethylarsonous acid + monomethylarsonic acid + dimethylarsinic acid

721074

-

7.3.2.7

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

210285, 210288, 210279, 210280, 210281, 210282, 210283, 210284, 210286, 210287, 689739, 696278, 718867, 718868, 719037, 719612, 733473, 718876, 733712, 719496, 686653, 697072, 699223, 687482, 687554, 689052, 719132

-

7.3.2.7

ATP + H2O + arsenite[side 1] = ADP + phosphate + arsenite[side 2]

751204, 750678

-

1.20.2.1

4 entries

1.20.4.1

2 entries

1.20.9.1

3 entries

1.20.99.1

6 entries

2.1.1.137

7 entries

7.3.2.7

2 entries

7.6.2.2

ATP + H2O + arsenite[side 1] = ADP + phosphate + arsenite[side 2]

747619

-

Product in Enzyme-catalyzed Reactions (41 results)

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Show Product (41 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.2.1.12

arsenate + GSH + NAD+ + glyceraldehyde 3-phosphate = arsenite + ?

0

-

1.20.4.1

arsenate + glutaredoxin 1 = arsenite + glutaredoxin 1 disulfide + H2O

0

1sjz, 3D-view

1.20.4.1

arsenate + glutaredoxin 1 = arsenite + glutaredoxin 1 disulfide + H2O

0

1sk0, 3D-view

1.20.4.1

arsenate + glutaredoxin 2 = arsenite + glutaredoxin 1 disulfide + H2O

0

1sjz, 3D-view

1.20.4.1

arsenate + glutaredoxin 2 = arsenite + glutaredoxin 1 disulfide + H2O

0

1sk0, 3D-view

1.20.4.1

arsenate + glutaredoxin 2 = arsenite + glutaredoxin 2 disulfide + H2O

0

1sjz, 3D-view

1.20.4.1

arsenate + glutaredoxin 2 = arsenite + glutaredoxin 2 disulfide + H2O

0

1sk0, 3D-view

1.20.4.1

arsenate + glutaredoxin 3 = arsenite + glutaredoxin 1 disulfide + H2O

0

1sjz, 3D-view

1.20.4.1

arsenate + glutaredoxin 3 = arsenite + glutaredoxin 1 disulfide + H2O

0

1sk0, 3D-view

1.20.4.1

arsenate + glutaredoxin 3 = arsenite + glutaredoxin 3 disulfide + H2O

0

1sjz, 3D-view

1.20.4.1

arsenate + glutaredoxin 3 = arsenite + glutaredoxin 3 disulfide + H2O

0

1sk0, 3D-view

1.20.4.1

arsenate + glutaredoxin = arsenite + glutaredoxin disulfide + H2O

0

1sjz, 3D-view

1.20.4.1

arsenate + glutaredoxin = arsenite + glutaredoxin disulfide + H2O

0

1sk0, 3D-view

1.20.4.1

arsenate + glutaredoxin C7 = arsenite + glutaredoxin C7 disulfide + H2O

0

1sjz, 3D-view

1.20.4.1

arsenate + glutaredoxin C7 = arsenite + glutaredoxin C7 disulfide + H2O

0

1sk0, 3D-view

1.20.4.1

arsenate + glutaredoxin C72.1 = arsenite + glutaredoxin C72.1 disulfide + H2O

0

1sjz, 3D-view

1.20.4.1

arsenate + glutaredoxin C72.1 = arsenite + glutaredoxin C72.1 disulfide + H2O

0

1sk0, 3D-view

1.20.4.1

arsenate + glutathione = arsenite + glutathione disulfide + H2O

0

1sjz, 3D-view

1.20.4.1

arsenate + glutathione = arsenite + glutathione disulfide + H2O

0

1sk0, 3D-view

1.20.4.1

arsenate + reduced acceptor = arsenite + acceptor

0

1sjz, 3D-view

1.20.4.1

arsenate + reduced acceptor = arsenite + acceptor

0

1sk0, 3D-view

1.20.4.1

arsenate + reduced glutaredoxin = arsenite + oxidized glutaredoxin

0, 639363, 639364, 639365, 639366, 639367, 639371

1sjz, 3D-view

1.20.4.1

arsenate + reduced glutaredoxin = arsenite + oxidized glutaredoxin

0, 639363, 639364, 639365, 639366, 639367, 639371

1sk0, 3D-view

1.20.4.1

arsenate + reduced glutathione + NAD+ + glyceraldehyde-3-phosphate = arsenite + glutathione + ?

0

1sjz, 3D-view

1.20.4.1

arsenate + reduced glutathione + NAD+ + glyceraldehyde-3-phosphate = arsenite + glutathione + ?

0

1sk0, 3D-view

1.20.4.1

arsenate + reduced glutathione = arsenite + glutathione

0

1sjz, 3D-view

1.20.4.1

arsenate + reduced glutathione = arsenite + glutathione

0

1sk0, 3D-view

1.20.4.1

26 entries

1.20.4.2

arsenate + glutathione = arsenite + reduced glutathione

0

-

1.20.4.3

arseno-mycothiol + mycoredoxin = arsenite + mycothiol-mycoredoxin disulfide

0

-

1.20.4.4

arsenate + thioredoxin = arsenite + thioredoxin disulfide + H2O

0

-

1.20.9.1

arsenate + azurin(red) = arsenite + H2O + azurin(ox)

0

-

1.20.99.1

arsenate + ? = arsenite + ?

0

-

1.20.99.1

arsenate + acetate = arsenite + ?

287859

-

1.20.99.1

arsenate + benzyl viologen = arsenite + oxidized benzyl viologen

0

-

1.20.99.1

arsenate + methyl viologen = arsenite + oxidized methyl viologen

0

-

1.20.99.1

arsenate + reduced acceptor = arsenite + acceptor

0

-

1.20.99.1

arsenate + reduced dithiothreitol = arsenite + dithiothreitol

0

-

1.20.99.1

arsenate + reduced glutaredoxin = arsenite + acceptor

0

-

7.3.2.7

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

210285, 210288, 210279, 210280, 210281, 0, 210282, 210283, 210284, 210286, 210287

-

7.3.2.7

ATP + H2O + arsenite[side 1] = ADP + phosphate + arsenite[side 2]

0

-

1.20.99.1

7 entries

7.3.2.7

2 entries

7.6.2.2

ATP + H2O + arsenite[side 1] = ADP + phosphate + arsenite[side 2]

0

-

Activator in Enzyme-catalyzed Reactions (4 results)

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Show Activating Compound (4 entries)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

1.2.3.4

5 mM concentration slight activation

288394

-

2.7.11.24

treatment of worms with arsenite, a toxic ROS-producing compound, induces a robust phosphorylation of PMK-1, induction of oxidative stress-responsive genes, and eventual lethality. Activation of PMK-1 following arsenite treatment is dependent on SEK-1 but independent of NSY-1, differing from the NSY-1/SEK-1/PMK-1 cascade used during infection and osmotic stress

740759

-

7.3.2.7

activates 3fold the ATPase activity of wild-type ArsA, activation rates of mutants, overview

696278

-

7.3.2.7

allosteric activation

210282, 210287

-

7.3.2.7

2 entries

Inhibitor in Enzyme-catalyzed Reactions (92 results)

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Show Inhibitors (92 entries)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

1.1.1.25

-

286389

-

1.1.1.40

weak

286722

-

1.1.1.86

slight inhibition

639170

-

1.1.3.4

-

695790

-

1.1.99.20

-

389908

-

1.13.11.28

-

439516

-

1.13.12.5

-

698372

-

1.13.99.1

-

6866

-

1.14.11.1

-

439283

-

1.14.13.16

-

439017

-

1.17.1.4

50% inhibition of hypoxanthine-NADP+-activity at 1 mM

644566

3nvv, 3D-view

1.17.1.4

90% loss of the ferricyanide-linked activity in the presence of 1.78 mM

644593

3nvv, 3D-view

1.17.1.4

gradual inhibition of xanthine-2,6-dichloroindophenol-activity, paralleled by a corresponding increase of NADH-2,6-dichloroindophenol-activity

644579

3nvv, 3D-view

1.17.1.4

inhibition of xanthine or pterine oxidation at 0.3 mM, diaphorase activity unaffected

644604

3nvv, 3D-view

1.17.1.4

4 entries

1.17.3.2

-

393008, 644642, 644648

3nvv, 3D-view

1.2.1.105

probably bind the dithiol group in the lipoic acid

349005

-

1.2.1.18

-

288060

-

1.2.1.24

-

288150, 288170

-

1.2.1.3

47% residual activity at 1 mM arsenite at pH 9.5, 28% residual activity at 2 mM arsenite at pH 7.4

726464

-

1.2.1.88

-

392053, 392055

-

1.2.1.88

both isoforms

392065

-

1.2.3.1

-

390405

1sij, 3D-view

1.2.3.1

65% inhibition at 20 mM

390375

1sij, 3D-view

1.2.3.1

82-95% inhibition of sulfoxide reductase and aldehyde oxidase activity at 0.1 mM

390402

1sij, 3D-view

1.2.3.4

5 mM concentration 12% inhibition

288393

-

1.2.3.4

concentration higher than 5 mM

288394

-

1.2.7.5

50% inhibition at 0.5 mM

11935

-

1.2.7.5

50% inhibition at 1 mM

11938

-

1.2.1.88

2 entries

1.2.3.1

3 entries

1.2.3.4

2 entries

1.2.7.5

2 entries

1.2.7.B2

5 mM, 50% inhibition after min

644682

-

1.2.99.7

5 mM, complete inhibition

11936

3l4p, 3D-view

1.2.99.7

irreversible inhibitor, complete inhibition at 0.024 mM

712240

3l4p, 3D-view

1.20.1.1

-

287853

-

1.20.1.1

4 mM, 90% residual activity

728004

-

1.20.4.1

-

639363, 639366

1sjz, 3D-view

1.20.4.1

-

639363, 639366

1sk0, 3D-view

1.20.4.1

noncompetitive

660258

1sjz, 3D-view

1.20.4.1

noncompetitive

660258

1sk0, 3D-view

1.2.99.7

2 entries

1.20.1.1

2 entries

1.20.4.1

4 entries

1.20.4.4

pH 7.5, 37°C

639368

-

1.21.4.1

-

2121

-

1.3.3.4

slight inhibition

390982

-

1.3.99.16

-

12565

-

1.7.1.4

-

392931

-

1.7.1.4

0.5 mM, 62% inhibition

392929

-

1.7.1.4

10 mM, 24% inhibition

392923

-

1.7.1.4

3 entries

1.8.1.11

low inhibition

394702, 394703

-

1.8.1.12

+ NADPH, slightly

394761

-

1.8.1.2

-

287801, 392964, 392968, 392969, 392971

-

1.8.1.4

0.3 mM, 50% inhibition

394001

-

1.8.1.4

activity of lipoamide dehydrogenase in isolated mitochondria is sensitive to arsenite, but not arsenate

743450

-

1.8.1.4

in presence of NADH, inhibition is reversed by dithiols and less effectively by monothiols

348981

-

1.8.1.4

reversible inactivation of lipoamide-reducing reaction, no decrease in diaphorase activity

394007

-

1.8.1.7

-

394708, 394713

-

1.8.1.7

inhibition increased by NADPH

394741

-

1.8.1.7

slightly

394759

-

1.8.1.8

-

680424

-

1.8.1.8

0.15 mM, complete inhibition

437710

-

1.8.1.4

4 entries

1.8.1.7

3 entries

1.8.1.8

2 entries

1.8.1.9

-

394915, 394920, 394921, 394931, 394940

-

1.8.2.1

1 mM, 83% inhibition

394081

-

1.8.2.1

1 mM, complete inhibition

394088

-

1.8.3.1

-

393008, 393009, 393014

-

1.8.3.1

7.4 mM, 50% inhibition

668531

-

1.8.2.1

2 entries

1.8.3.1

2 entries

1.8.4.13

strong inhibition

393070

-

1.8.4.2

-

394854

-

2.1.1.137

the enzyme activity is completely inhibited by elevated concentrations of the substrate arsenite (0.2 mM)

721074

-

2.1.1.21

-

485233

-

2.3.1.168

strong inhibition

644839

-

2.3.1.179

1 mM, 42% inhibition

486924

-

2.3.1.180

45% inhibition at 5 mM, 98% inhibition at 20 mM

486931

-

2.3.1.38

-

285675, 486866

-

2.3.1.41

-

285675

-

2.3.1.41

synthase II and I

486924

-

2.3.1.41

synthase III

486931

-

2.3.1.41

weak at 1 mM

486920

-

2.3.1.41

4 entries

2.3.2.24

specific for vicinal sulfhydryl sites in proteins, irreversible or very slow reversible, instead of other inhibition with arsenite which is usually rapidly reversed upon addition of competitive dithiol compounds

724254

-

2.3.3.10

in presence of CoA, residual activity 25%

488092

-

2.7.11.10

inhibition of IKKbeta

673483

-

3.1.16.1

weak inhibitor with RNA core as substrate

134135

-

3.1.2.12

-

80982, 80985, 80987

-

3.1.3.43

together with NADH

94880

-

3.1.3.8

-

114267, 114268

-

3.1.4.37

-

135382

-

3.1.7.1

-

95169

-

3.1.7.6

1 mM

95169

-

3.4.22.1

i.e. arsenic trioxide, inhibits CatB in glioblastoma cells, 20% inhibition at 0.022 mM, 50% at 0.020 mM

707625

-

3.5.1.30

-

172030

-

3.5.1.30

characteristic of enzymes with essential vicinal sulfhydryl groups

172031

-

3.5.1.30

2 entries

3.6.1.1

-

209829

-

4.1.1.39

-

4491

-

4.1.3.16

-

5237

-

4.6.1.18

-

134523

-

5.6.2.2

-

692633

-

6.1.1.9

-

542

-

3D Structure of Enzyme-Ligand-Complex (PDB) (35 results)

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Show 3D Structure of Enzyme-Ligand-Complex (PDB) (35 entries)

EC NUMBER

ENZYME 3D STRUCTURE

1.17.1.4

3nvv, 3D-view

1.17.3.2

3nvv, 3D-view

1.2.3.1

1sij, 3D-view

1.2.99.7

3l4p, 3D-view

1.20.4.1

1sjz, 3D-view

1.20.4.1

1sk0, 3D-view

1.20.4.1

1sjz, 3D-view

1.20.4.1

1sk0, 3D-view

1.20.4.1

1sjz, 3D-view

1.20.4.1

1sk0, 3D-view

1.20.4.1

1sjz, 3D-view

1.20.4.1

1sk0, 3D-view

1.20.4.1

1sjz, 3D-view

1.20.4.1

1sk0, 3D-view

1.20.4.1

1sjz, 3D-view

1.20.4.1

1sk0, 3D-view

3.6.3.16

1ihu, 3D-view

3.6.3.16

1ii0, 3D-view

3.6.3.16

1ii9, 3D-view

3.6.3.16

1ihu, 3D-view

3.6.3.16

1ii0, 3D-view

3.6.3.16

1ii9, 3D-view

3.6.3.16

1ihu, 3D-view

3.6.3.16

1ii0, 3D-view

3.6.3.16

1ii9, 3D-view

3.6.3.16

1ihu, 3D-view

3.6.3.16

1ii0, 3D-view

3.6.3.16

1ii9, 3D-view

3.6.3.16

1ihu, 3D-view

3.6.3.16

1ii0, 3D-view

3.6.3.16

1ii9, 3D-view

3.6.3.16

1ihu, 3D-view

3.6.3.16

1ii0, 3D-view

3.6.3.16

1ii9, 3D-view

1.20.4.1

12 entries

3.6.3.16

18 entries

5.2.1.8

6dun, 3D-view

Enzyme Kinetic Parameters

k_cat Value (Turnover Number) (3 results)

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Show Turnover Number (3 entries)

EC NUMBER

TURNOVER NUMBER [1/S]

TURNOVER NUMBER MAXIMUM [1/S]

COMMENTARY

LITERATURE

1.20.2.1

8.6

-

pH 5.5, temperature not specified in the publication

715352

1.20.2.1

30.4

-

pH 5.5, temperature not specified in the publication

658195

1.20.2.1

2 entries

1.20.99.1

30.4

-

pH 5.5, calculated with an Mr of 309000 Da

658195

K_M Value (34 results)

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Show KM Value (34 entries)

EC NUMBER

KM VALUE [MM]

KM VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

1.20.2.1

0.035

-

pH 5.5, temperature not specified in the publication

658195

1.20.2.1

0.061

-

pH 5.5, temperature not specified in the publication

715352

1.20.9.1

0.026

-

pH 6.0

696599

1.20.9.1

0.07

-

-

287857

1.20.99.1

0.035

-

pH 5.5, calculated with an Mr of 309000 Da

658195

1.20.99.1

0.061

-

pH 5.5

658195

2.1.1.137

0.0012

-

mutant enzyme G134A, at pH 7.0 and 37°C

733425

2.1.1.137

0.0016

-

mutant enzyme C334S, in PBS (25 mM, pH 7.0), at 37°C

719012

2.1.1.137

0.0016

-

mutant enzyme M287T, in the presence of 1 mM glutathione, in 100 mM Tris-HCl buffer (pH 7.4), at 37°C

721075

2.1.1.137

0.0016

-

wild type enzyme, in the presence of 1 mM glutathione, in 100 mM Tris-HCl buffer (pH 7.4), at 37°C

721075

2.1.1.137

0.0018

-

mutant enzyme R83A, at pH 7.0 and 37°C

733425

2.1.1.137

0.00188

-

mutant enzyme C271S, in PBS (25 mM, pH 7.0), at 37°C

719012

2.1.1.137

0.002

-

-

485148

2.1.1.137

0.002

-

mutant enzyme M287T, in 100 mM Tris-HCl buffer (pH 7.4), at 37°C

721075

2.1.1.137

0.0022

-

mutant enzyme V157A, at pH 7.0 and 37°C

733425

2.1.1.137

0.00232

-

mutant enzyme C360S, in PBS (25 mM, pH 7.0), at 37°C

719012

2.1.1.137

0.0026

-

mutant enzyme R57A, at pH 7.0 and 37°C

733425

2.1.1.137

0.0027

-

mutant enzyme S81A, at pH 7.0 and 37°C

733425

2.1.1.137

0.0032

-

mutant enzyme V161A, at pH 7.0 and 37°C

733425

2.1.1.137

0.0032

-

wild type enzyme, at pH 7.0 and 37°C

733425, 733865

2.1.1.137

0.0032

-

wild type enzyme, in PBS (25 mM, pH 7.0), at 37°C

719012

2.1.1.137

0.0041

-

wild type enzyme, in 100 mM Tris-HCl buffer (pH 7.4), at 37°C

721075

2.1.1.137

0.0044

-

mutant enzyme D150N, at pH 7.0 and 37°C

733865

2.1.1.137

0.0045

-

37°C, pH 8.0, Thr287 allozyme

674763

2.1.1.137

0.006

-

-

485151

2.1.1.137

0.007

-

mutant enzyme T104A, at pH 7.0 and 37°C

733425

2.1.1.137

0.007

-

mutant enzyme Y135A, at pH 7.0 and 37°C

733425

2.1.1.137

0.0076

-

mutant enzyme Y58A, at pH 7.0 and 37°C

733425

2.1.1.137

0.0087

-

mutant enzyme G82A, at pH 7.0 and 37°C

733425

2.1.1.137

0.0089

-

37°C, pH 8.0, Trp173 allozyme

674763

2.1.1.137

0.0096

-

mutant enzyme L77A, at pH 7.0 and 37°C

733425

2.1.1.137

0.0118

-

37°C, pH 8.0, wild-type enzyme

674763

2.1.1.137

0.0185

-

mutant enzyme C375S, in PBS (25 mM, pH 7.0), at 37°C

719012

1.20.2.1

2 entries

1.20.9.1

2 entries

1.20.99.1

2 entries

2.1.1.137

27 entries

7.3.2.7

0.1

-

-

210287

K_i Value (4 results)

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Show KI Value (4 entries)

EC NUMBER

KI VALUE [MM]

KI VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

1.20.4.4

0.5

-

pH 7.5, 37°C

639368

1.8.1.2

0.08

0.12

-

392968

1.8.1.7

2.2

9

at 50% inhibition value

394708

1.8.1.7

3

-

at 50% inhibition value

394708

1.8.1.7

2 entries

References & Links

Literature References (197)

top print hide

Show Reference (197 entries)

BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

PAGES

542

6337152

A novel thiol-dependent arsenite-sensitive valyl-tRNA synthetase activity from yeast

1983

Black, S.

J. Biol. Chem.

258

2112-2114

2121

13475375

Studies on the enzymic reduction of amino acids. II. Purification and properties of a D-proline reductase and a proline racemase from Clostridium sticklandii

1957

Stadtman, T.C.; Elliott, P.

J. Biol. Chem.

228

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4491

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Ribulose-diphosphate carboxylase from spinach leaves

1975

Siegel, M.I.; Lane, M.D.

Methods Enzymol.

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5237

14089442

The metabolism of gamma-hydroxyglutamate in rat liver. 1. Enzymic synthesis of gamma-hydroxy-alpha-ketoglutarate from pyruvate and glyoxylate

1963

Kuratomi, K.; Fukunaga, K.

Biochim. Biophys. Acta

78

617-628

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Biochemical studies on inositol. V. Purification and properties of the enzyme that cleaves inositol to D-glucuronic acid

1959

Charalampous, F.C.

J. Biol. Chem.

234

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11935

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Purification, characterization, and metabolic function of tungsten-containing aldehyde ferredoxin oxidoreductase from the hyperthermophilic and proteolytic archaeon Thermococcus strain ES-1

1995

Heider, J.; Ma, K.; Adams, M.W.W.

J. Bacteriol.

177

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11936

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Purification and characterization of a benzylviologen-linked tungsten-containing aldehyde oxidoreductase from Desulfovibrio gigas

1995

Hensgens, C.M.H.; Hagen, W.R.; Hansen, T.A.

J. Bacteriol.

177

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11938

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The novel tungsten-iron-sulfur protein of the hyperthermophilic archaebacterium, Pyrococcus furiosus, is an aldehyde ferredoxin oxidoreductase. Evidence for its participation in a unique glycolytic pathway

1991

Mukund, S.; Adams, M.W.W.

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266

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12565

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Purification and characterization of isoquinoline 1-oxidoreductase from Pseudomonas diminuata 7, a novel molybdenum-containing hydroxylase

1994

Lehmann, M.; Tshisuaka, B.; Fetzner, S.; Roger, P.; Lingens, F.

J. Biol. Chem.

269

11254-11260

80982

4436331

Purification and properties of S-formylglutathione hydrolase from human liver

1974

Uotila, L.; Koivusalo, M.

J. Biol. Chem.

249

7664-7672

80985

7188860

Purificaton and characterization of S-formylglutathione hydrolase from a methanol-utilizing yeast, Kloeckera sp. No. 2201

1980

Kato, N.; Sakazawa, C.; Nishizawa, T.; Tani, Y.; Yamada, H.

Biochim. Biophys. Acta

611

323-332

80987

6276656

S-Formylglutathione hydrolase

1981

Uotila, L.; Koivusalo, M.

Methods Enzymol.

77

320-325

94880

2836411

Component requirements for NADH inhibition and spermine stimulation of pyruvate dehydrogenase phosphatase activity

1988

Rahmatullah, M.; Roche, T.E.

J. Biol. Chem.

263

8106-8110

95169

4288361

Testicular sterols. V. Preparation and partial purification of a microsomal prenol pyrophosphate pyrophophohydrolase

1966

Tsai, S.C.; Gaylor, J.L.

J. Biol. Chem.

241

4043-4050

114267

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Purification and general properties of extracellular phytase from Aspergillus flaviceps

1987

Youssef, K.A.; Ghareib, M.; Nour el Dein, M.M.

Zentralbl. Mikrobiol.

142

397-402

114268

-

Isolation and characterization of intracellular phytase from Macrophormina physeolina

1988

Ghareib, M.; Youssef, K.A.; Nour el Dein, M.M.

Zentralbl. Mikrobiol.

143

397-403

134135

-

Spleen acid exonuclease

1971

Bernardi, A.; Bernardi, G.

The Enzymes, 3rd Ed. (Boyer, P. D. , ed. )

4

329-336

134523

-

The ribonucleases: occurence, structure and properties

1961

Anfinsen, C.B.; White, F.H.

The Enzymes, 2nd Ed. (Boyer, P. D. ; Lardy, H. ; Myrbäck, K. , eds. )

5

95-122

135382

-

2'3'-cyclic nucleotide 3'-phosphodiesterase

1978

Sims, N.R.; Carnegie, P.R.

Adv. Neurochem.

3

1-41

172030

-

delta-Aminovaleramidase (Pseudomonas putida)

1971

Reitz, M.S.; Rodwell, V.W.

Methods Enzymol.

17

158-165

172031

5432799

delta-Aminovaleramidase of Pseudomonas putida

1970

Reitz, M.S.; Rodwell, V.W.

J. Biol. Chem.

245

3091-3096

209829

1309654

Characterization of a mitochondrial inorganic pyrophosphatase in Saccharomyces cerevisiae

1992

Lundin, M.; Deopujari, S.W.; Lichko, L.; da Silva, L.P.; Baltscheffsky, H.

Biochim. Biophys. Acta

1098

217-223

210279

10089335

Crystallization and preliminary X-ray analysis of the catalytic subunit of the ATP-dependent arsenite pump encoded by the Escherichia coli plasmid R773

1999

Zhou, T.; Rosen, B.P.; Gatti, D.L.

Acta Crystallogr. Sect. D

55

921-924

210280

1703401

Molecular analysis of an anion pump: purification of the ArsC protein

1991

Rosen, B.P.; Weigel, U.; Monticello, R.A.; Edwards, B.P.F.

Arch. Biochem. Biophys.

284

381-385

210281

7629056

Mechanism of metalloregulation of an anion-translocating ATPase

1995

Rosen, B.P.; Bhattacharjee, H.; Shi, W.

J. Bioenerg. Biomembr.

27

85-91

210282

10318792

Asp45 is a Mg2+ ligand in the ArsA ATPase

1999

Zhou, T.; Rosen, B.P.

J. Biol. Chem.

274

13854-13858

210283

9242630

Tryptophan fluorescence reports nucleotide-induced conformational changes in a domain of the ArsA ATPase

1997

Zhou, T.; Rosen, B.P.

J. Biol. Chem.

272

19731-19737

210284

8674982

The arsenical resistance operon of IncN plasmid R46

1996

Bruhn, D.F.; Li, J.; Silver, S.; Roberto, F.; Rosen, B.P.

FEMS Microbiol. Lett.

139

149-153

210285

8991852

Bacterial resistance to toxic metal ions - a review

1996

Silver, S.

Gene

179

9-19

210286

2185215

Differential mRNA stability controls relative gene expression within the plasmid-encoded arsenical resistance operon

1990

Owolabi, J.B.; Rosen, B.P.

J. Bacteriol.

172

2367-2371

210287

7929243

ATP-dependent arsenite transport in everted membrane vesicles of Escherichia coli

1994

Dey, S.; Dou, D.; Rosen, B.P.

J. Biol. Chem.

269

25442-25446

210288

1531541

Plasmid-encoded resistance to arsenite and antimon

1992

Kaur, P.; Rosen, B.P.

Plasmid

27

29-40

285675

6833216

The purification and function of acetyl coenzyme A:acyl carrier protein transacylase

1983

Shimakata, T.; Stumpf, P.K.

J. Biol. Chem.

258

3592-3598

286389

4380104

5-Dehydroshikimate reductase in the tea plant (Camellia sinensis L.). Properties and distribution

1966

Sanderson, G.W.

Biochem. J.

98

248-252

286722

13563505

Purification and properties of pigeon liver malic enzyme

1958

Rutter, W.J.; Lardy, H.A.

J. Biol. Chem.

233

374-382

287801

-

Metal-containing flavoprotein dehydrogenases

1976

Hatefi, Y.; Stiggall, D.L.

The Enzymes, 3rd Ed. (Boyer, P. D. , ed. )

13

175-297

287853

11278981

Purification and characterization of a novel phosphorus-oxidizing enzyme from Pseudomonas stutzeri WM88

2001

Costas, A.M.G.; White, A.K.; Metcalf, W.W.

J. Biol. Chem.

276

17429-17436

287857

1331097

The purification and characterization of arsenite oxidase from Alcaligenes faecalis, a molybdenum-containing hydroxylase

1992

Anderson, G.L.; Williams, J.; Hille, R.

J. Biol. Chem.

267

23674-23682

287858

11250197

Crystal structure of the 100 kDa arsenite oxidase from Alcaligenes faecalis in two crystal forms at 1.64 A and 2.03 A

2001

Ellis, P.J.; Conrads, T.; Hille, R.; Kuhn, P.

Structure

9

125-132

287859

9738904

Purification and characterization of the respiratory arsenate reductase of Chrysiogenes arsenatis

1998

Krafft, T.; Macy, J.M.

Eur. J. Biochem.

255

647-653

288060

13846369

Aldehyde oxidation

1960

Yamada, E.W.; Jakoby, W.B.

J. Biol. Chem.

235

589-594

288150

2596851

Potato tuber succinate semialdehyde dehydrogenase: purification and characterization

1989

Satya Narayan, V.; Madhusudanan Nair, P.

Arch. Biochem. Biophys.

275

469-477

288170

13860092

Succinic semialdehyde dehydrogenase: purification and properties of the enzyme from monkey brain

1961

Albers, R.W.; Koval, G.J.

Biochim. Biophys. Acta

52

29-35

288393

-

Occurence of an oxalate oxidase in Sorghum leaves

1984

Pundir, C.S.; Nath, R.

Phytochemistry

9

1871-1874

288394

5961854

Purification and properties of oxalic acid oxidase

1966

Chiriboga, J.

Arch. Biochem. Biophys.

116

516-523

348981

-

Purification and resolution of the pyruvate dehydrogenase complex (Escherichia coli)

1966

Reed, L.J.; Willms, C.R.

Methods Enzymol.

9

247-265

349005

-

alpha-Ketoglutarate dehydrogenase from pig heart

1969

Sanadi, D.R.

Methods Enzymol.

13

52-55

389908

-

Purification and characterization of constitutive polyethylene glycol (PEG) dehydrogenase of a PEG 4000-utilizing Flavobacterium sp. No. 203

1989

Yamanaka, H.; Kawai, F.

J. Ferment. Bioeng.

67

324-330

390375

10679276

Biochemical/spectroscopic characterization and preliminary x-ray analysis of a new aldehyde oxidoreductase isolated from Desulfovibrio desulfuricans ATCC 27774

2000

Duarte, R.O.; Archer, M.; Dias, J.M.; Bursakov, S.; Huber, R.; Moura, I.; Romao, M.J.; Moura, J.J.G.

Biochem. Biophys. Res. Commun.

268

745-749

390402

6688361

Sulfoxide reductase activity of liver aldehyde oxidase

1983

Tatsumi, K.; Kitamura, S.; Yamada, H.

Biochim. Biophys. Acta

747

86-92

390405

6259169

Superoxide production by an unusual aldehyde oxidase in guinea pig granulocytes. Characterization and cytochemical localization

1981

Badwey, J.A.; Robinson, J.M.; Karnovsky, M.J.; Karnovsky, M.L.

J. Biol. Chem.

256

3479-3486

390982

234450

The enzymic conversion of protoporphyrinogen IX to protoporphyrin IX. Protoporphyrinogen oxidase activity in mitochondrial extracts of Saccharomyces cerevisiae

1975

Poulson, R.; Polglase, W.J.

J. Biol. Chem.

250

1269-1274

392053

-

DELTA1-pyrroline-5-carboxylate dehydrogenase (ox liver) (oxidation of DELTA1-pyrroline-5-carboxylate to glutamate)

1971

Strecker, H.J.

Methods Enzymol.

17B

262-265

392055

13681370

Hydroxyproline metabolism. IV. Enzymatic synthesis of gamma-hydroxyglutamate from DELTA1-pyrroline-3-hydroxy-5-carboxylate

1960

Adams, E.; Goldstone, A.

J. Biol. Chem.

235

3504-3512

392065

9418013

Enzymes of DELTA1-pyrroline-5-carboxylate metabolism in the camel tick Hyalomma dromedarii during embryogenesis. Purification and characterization of DELTA1-pyrroline-5-carboxylate dehydrogenases

1997

Fahmy, A.S.; Mohamed, S.A.; Girgis, R.B.; Abdel-Ghaffar, F.A.

Comp. Biochem. Physiol. B

118

229-237

392923

217342

Purification and properties of nitrite reductase from Escherichia coli K12

1978

Coleman, K.J.; Cornish-Bowden, A.; Cole, J.A.

Biochem. J.

175

483-493

392929

14463130

A triphosphopyridine nucleotide-specific nitrite reductase from Escherichia coli

1961

Lazzarini, R.A.; Atkinson, D.E.

J. Biol. Chem.

236

3330-3335

392931

150863

Preparation and some properties of homogeneous Neurospora crassa assimilatory NADPH-nitrite reductase

1978

Greenbaum, P.; Prodouz, K.N.; Garrett, R.H.

Biochim. Biophys. Acta

526

52-64

392964

4150390

Reduced nicotinamide adenine dinucleotide phosphate-sulfite reductase of enterobacteria. 3. The Escherichia coli hemoflavoprotein: catalytic parameters and the sequence of electron flow

1974

Siegel, L.M.; Davis, P.S.; Kamin, H.

J. Biol. Chem.

249

1572-1586

392968

-

TPNH-Sulfite reductase (Escherichia coli)

1971

Siegel, L.M.; Kamin, H.

Methods Enzymol.

17B

539-545

392969

-

Sulfite reductase (bakers¦ yeast)

1971

Yoshimoto, A.; Naiki, N.; Sato, R.

Methods Enzymol.

17B

520-528

392971

4384979

Studies on yeast sulfite reductase. I. Purification and characterization

1968

Yoshimoto, A.; Sato, R.

Biochim. Biophys. Acta

153

555-575

393008

-

Molybdenum iron-sulfur flavin hydroxylases and related enzymes

1975

Bray, R.C.

The Enzymes, 3rd Ed. (Boyer, P. D. , ed. )

12

299-419

393009

4374241

Hepatic sulfite oxidase. Identification of the molybdenum center as the site of irreversible inactivation by ferricyanide

1974

Kessler, D.L.; Rajagopalan, K.V.

Biochim. Biophys. Acta

370

399-409

393014

5542006

Hepatic sulfite oxidase. Purification and properties

1971

Cohen, H.J.; Fridovich, I.

J. Biol. Chem.

246

359-366

393070

-

A specific enzymatic reduction of L(-)methionine sulfoxide and a related nonspecific reduction of disulfides

1960

Black, S.; Harte, E.M.; Hudson, B.; Wartolofsky, L.

J. Biol. Chem.

235

2910-2916

394001

-

Isolation und Eigenschaften von Liponsäuredehydrogenase aus Chloroplasten

1968

Jacobi, G.; Öhlers, U.

Z. Pflanzenphysiol.

58

193-206

394007

9143318

Catalytic properties of lipoamide dehydrogenase from Mycobacterium smegmatis

1997

Marcinkeviciene, J.; Blanchard, J.S.

Arch. Biochem. Biophys.

340

168-176

394081

5438321

Enzymes involved in the metabolism of thiosulfate by Thiobacillus thioparus. I. Survey of enzymes and properties of sulfite: cytochrome c oxidoreductase

1970

Lyric, R.M.; Suzuki, I.

Can. J. Biochem.

48

334-343

394088

-

Purification and properties of membrane-bound sulfite dehydrogenase from Thiobacillus thiooxidans JCM7814

1995

Nakamura, K.; Yoshikawa, H.; Okubo, S.; Kurosawa, H.; Amano, Y.

Biosci. Biotechnol. Biochem.

59

11-15

394702

440099

Asparagusate dehydrogenase and lipoyl deydrogenase from Asparagus

1979

Yanagawa, H.

Methods Enzymol.

62

172-181

394703

180003

Asparagusate dehydrogenases and lipoyl dehydrogenase from Asparagus mitochondria. Physical, chemical, and enzymatic properties

1976

Yanagawa, H.; Egami, F.

J. Biol. Chem.

251

3637-3644

394708

-

Glutathione reductase

1989

Schirmer, R.H.; Krauth-Siegel, R.L.; Schulz, G.E.

Coenzymes and cofactors, Glutathione, Chem. Biochem. Med. Aspects Pt. A (Dolphin D, Poulson R, Avromonic O, eds. ) John Wiley & Sons, New York

3

553-596

394713

4385907

Purification and properties of a disulfide reductase obtained from Achromobacter starkeyi

1968

Ruiz-Herrera, J.; Amezcua-Ortega, R.; Trujillo, A.

J. Biol. Chem.

243

4083-4088

394741

6425264

Purification and properties of glutathione reductase from the cyanobacterium Anabaena sp. strain 7119

1984

Serrano, A.; Rivas, J.; Losada, M.

J. Bacteriol.

158

317-324

394759

-

Occurrence of two isoforms of glutathione reductase in the green alga Chlamydomonas reinhardtii

1993

Serrano, A.; Llobell, A.

Planta

190

199-205

394761

8168518

Mechanism of inhibition of trypanothione reductase and glutathione reductase by trivalent organic arsenicals

1994

Cunningham, M.L.; Zvelebil, M.J.J.M.; Fairlamb, A.H.

Eur. J. Biochem.

221

285-295

394854

10847613

A method for measuring disulfide reduction by cultured mammalian cells: relative contributions of glutathione-dependent and glutathione-independent mechanisms

2000

Biaglow, J.E.; Donahue, J.; Tuttle, S.; Held, K.; Chrestensen, C.; Mieyal, J.

Anal. Biochem.

281

77-86

394915

11539727

Thioredoxin and NADP-thioredoxin reductase from cultured carrot cells

1987

Johnson, T.C.; Cao, R.Q.; Kung, J.E.; Buchanan, B.B.

Planta

171

321-331

394920

6373736

Thioredoxin system of the photosynthetic anaerobe Chromatium vinosum

1984

Johnson, T.C.; Crawford, N.A.; Buchanan, B.B.

J. Bacteriol.

158

1061-1069

394921

7159551

Rat liver thioredoxin and thioredoxin reductase: purification and characterization

1982

Luthman, M.; Holmgren, A.

Biochemistry

21

6628-6633

394931

14245401

Enzymatic synthesis of desoxyribonucleotides. V. Purification and properties of thioredoxin reductase from Escherichia coli B

1964

Moore, E.C.; Reichard, P.; Thelander, L.

J. Biol. Chem.

239

3445-3452

394940

8577704

A new selenoprotein from human lung adenocarcinoma cells: purification, properties, and thioredoxin reductase activity

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