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Ligand arsenate

Basic Ligand Information

Molecular Structure

Pathway Source

Pathways

BRENDA

non-pathway related

MetaCyc

arsenate detoxification I, arsenate detoxification II, arsenate detoxification III, arsenate detoxification IV (mycothiol), arsenate detoxification V, arsenate reduction (respiratory), arsenic detoxification (mammals), arsenic detoxification (plants), arsenic detoxification (yeast), arsenite to oxygen electron transfer, arsenite to oxygen electron transfer (via azurin), arsonoacetate degradation more

Show all BRENDA pathways known for arsenate

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Roles as Enzyme Ligand

In Vivo Substrate in Enzyme-catalyzed Reactions (10 results)

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Show Natural Substrate (10 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.2.1.107

D-glyceraldehyde 3-phosphate + arsenate + NAD+ = 1-arsono-3-phospho-D-glycerate + NADH + H+

761823, 761413, 761416, 762496, 761820, 760554, 761057, 761821, 761822, 761019, 760551, 743740, 761917, 761800

-

1.20.4.1

arsenate + glutaredoxin = arsenite + glutaredoxin disulfide + H2O

746123, 745329

-

1.20.4.1

arsenate + reduced acceptor = arsenite + acceptor

660258

-

1.20.4.1

arsenate + reduced glutaredoxin = arsenite + oxidized glutaredoxin

639364, 639365, 639366, 639367, 639371

-

1.20.4.1

arsenate + reduced glutathione = arsenite + glutathione

660258

-

1.20.4.1

4 entries

1.20.4.4

arsenate + thioredoxin = arsenite + thioredoxin disulfide + H2O

745640, 639368, 639370

-

1.20.99.1

arsenate + acetate = arsenite + ?

287859

-

1.20.99.1

arsenate + reduced acceptor = arsenite + acceptor

745852, 657473, 660461, 660525, 660404

-

2.8.4.2

arsenate + mycothiol = arseno-mycothiol

698899

-

2.8.4.2

arsenate + mycothiol = arseno-mycothiol + H2O

726005, 737533

-

1.20.99.1

2 entries

2.8.4.2

2 entries

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

1.20.2.1

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

0

-

1.20.2.1

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

0

-

1.20.2.1

2 entries

1.20.4.1

arsenite + acceptor = arsenate + reduced acceptor

0

-

1.20.99.1

arsenite + acceptor = arsenate + reduced acceptor

0

-

1.20.99.1

arsenite + azurin + H2O = arsenate + reduced azurin

0

-

1.20.99.1

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

0

-

1.20.99.1

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

0

-

1.20.99.1

4 entries

Substrate in Enzyme-catalyzed Reactions (65 results)

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Show Substrate (65 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.2.1.107

D-glyceraldehyde 3-phosphate + arsenate + NAD+ = 1-arsono-3-phospho-D-glycerate + NADH + H+

761823, 761413, 761416, 762496, 761820, 760554, 761057, 761821, 761822, 761019, 760551, 743740, 761917, 761800

-

1.2.1.107

DL-glyceraldehyde 3-phosphate + arsenate + NAD+ = 1-arsono-3-phospho-D-glycerate + NADH + H+

760549

-

1.2.1.11

L-aspartate 4-semialdehyde + arsenate + NADP+ = ?

390200

1ta4, 3D-view

1.2.1.11

L-aspartate 4-semialdehyde + HasO42- + NADP+ = ?

390180

1ta4, 3D-view

1.2.1.12

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

657393

-

1.2.1.12

D-glyceraldehyde 3-phosphate + arsenate + NAD+ = 1-arseno-3-phosphoglycerate + NADH + H+

741758

-

1.2.1.12

D-glyceraldehyde 3-phosphate + arsenate + NAD+ = 3-phospho-D-glyceroyl arsenate + NADH

287932, 287950, 287934, 287937, 287979, 287969, 287970, 287930, 287938

-

1.2.1.12

D-glyceraldehyde 3-phosphate + arsenate + NAD+ = 3-phospho-D-glyceroyl arsenate + NADH + H+

287974, 726827

-

1.2.1.107

2 entries

1.2.1.11

2 entries

1.2.1.12

4 entries

1.2.1.13

D-glyceraldehyde 3-phosphate + arsenate + NADP+ = 3-phospho-D-glyceroyl arsenate + NADPH

288024, 287999, 11537, 11539, 287995

-

1.2.3.3

pyruvate + arsenate + O2 + H2O = acetyl arsenate + CO2 + H2O2

390437

-

1.20.4.1

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

639367

-

1.20.4.1

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

639367

-

1.20.4.1

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

639367

-

1.20.4.1

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

639367

-

1.20.4.1

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

639367

-

1.20.4.1

arsenate + glutaredoxin = arsenite + glutaredoxin disulfide + H2O

746123, 745405, 745329

-

1.20.4.1

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

746123

-

1.20.4.1

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

746123

-

1.20.4.1

arsenate + glutathione = arsenite + glutathione disulfide + H2O

745405

-

1.20.4.1

arsenate + reduced acceptor = arsenite + acceptor

660258

-

1.20.4.1

arsenate + reduced glutaredoxin = arsenite + oxidized glutaredoxin

693214, 727076, 727580, 639366, 639363, 639364, 639367, 639365, 639371, 728218

-

1.20.4.1

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

677207

-

1.20.4.1

arsenate + reduced glutathione = arsenite + glutathione

660258, 676606

-

1.20.4.1

13 entries

1.20.4.2

arsenate + glutathione = arsenite + reduced glutathione

287855

-

1.20.4.4

arsenate + thioredoxin = arsenite + thioredoxin disulfide + H2O

745640, 732190, 639368, 639369, 639370, 705110, 705113, 706565, 715567, 727086, 726005

-

1.20.9.1

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

287859

-

1.20.99.1

arsenate + ? = arsenite + ?

639373

-

1.20.99.1

arsenate + acetate = arsenite + ?

287859

-

1.20.99.1

arsenate + benzyl viologen = arsenite + oxidized benzyl viologen

696045

-

1.20.99.1

arsenate + methyl viologen = arsenite + oxidized methyl viologen

696045

-

1.20.99.1

arsenate + reduced acceptor = arsenite + acceptor

657473, 660404, 660525, 745852, 713790, 660461, 716477, 714217

-

1.20.99.1

arsenate + reduced dithiothreitol = arsenite + dithiothreitol

745852

-

1.20.99.1

arsenate + reduced glutaredoxin = arsenite + acceptor

693852, 694407

-

1.20.99.1

7 entries

2.1.3.3

arsenate + L-citrulline = carbamoylarsenate + L-ornithine

485938

-

2.1.3.6

arsenate + N-carbamoylputrescine = ?

209399, 485950, 485949

-

2.3.1.8

acetyl-CoA + arsenate = CoA + acetyl arsenate

706839, 706840

-

2.3.1.8

arsenate + acetyl-CoA = acetyl arsenate + CoA

487513, 487515, 487520, 487535

-

2.3.1.8

2 entries

2.4.1.1

maltohexaose + arsenate = maltopentaose + glucose 1-arsenate

488295

-

2.4.1.20

cellobiose + arsenate = D-glucose + alpha-D-glucose 1-arsenate

637865

-

2.4.1.231

alpha,alpha-trehalose + arsenate = alpha-D-glucose + alpha-D-glucose 1-arsenate

674984

-

2.4.1.231

alpha,alpha-trehalose + arsenate = alpha-D-glucose 1-arsenate + alpha-D-glucose

644898, 644897, 674984

-

2.4.1.7

alpha-D-glucose 1-phosphate + arsenate = ?

679850, 684969, 686739

-

2.4.1.7

alpha-D-glucose 1-phosphate + arsenate = alpha-D-glucose 1-arsenate + phosphate

703198

-

2.4.1.7

glucose-1-phosphate + arsenate = glucose-1-arsenate + phosphate

637842, 637843

-

2.4.1.7

glycosyl-glucose + arsenate = glucose-1-arsenate + glucose

637842

-

2.4.1.7

sucrose + arsenate = D-fructose + alpha-D-glucose 1-arsenate

702001

-

2.4.1.231

2 entries

2.4.1.7

5 entries

2.4.1.8

maltose + arsenate = D-glucose + D-glucose + arsenate

489387, 489389, 489392, 489403, 489391

-

2.4.2.1

adenosine + arsenate = adenine + alpha-D-ribose 1-arsenate

489688

3enz, 3D-view

2.4.2.1

guanosine + arsenate = guanine + alpha-D-ribose 1-arsenate

489688

3enz, 3D-view

2.4.2.1

inosine + arsenate = hypoxanthine + ribose 1-arsenate

489688, 489697

3enz, 3D-view

2.4.2.1

xanthosine + arsenate = xanthine + alpha-D-ribose 1-arsenate

489654, 489707

3enz, 3D-view

2.4.2.1

4 entries

2.4.2.16

uric acid ribonucleoside + arsenate = urate + D-ribose 1-phosphate

639636

-

2.4.2.28

S-methyl-5'-thioadenosine + arsenate = adenine + S-methyl-5-thio-alpha-D-ribose 1-arsenate

674184

-

2.4.2.3

uridine + arsenate = ?

638509

-

2.4.2.4

thymidine + arsenate = ?

638443, 638450, 638444, 638449

-

2.7.1.90

arsenate + D-fructose 1,6-bisphosphate = ?

642074, 642100, 642080, 642082

-

2.7.7.103

CTP + arsenate = diphosphate + ?

760601

-

2.7.7.53

ADP + arsenate = AMP + phosphate + ?

209909

-

2.7.7.53

NDP + arsenate = NMP + phosphate + ?

643510, 643513

-

2.7.7.53

P1,P4-bis(5'-adenosyl) tetraphosphate + arsenate = ?

209909, 643507, 643515, 643514

-

2.7.7.53

3 entries

2.7.9.1

ATP + pyruvate + arsenate = ?

645428, 645426

-

2.8.4.2

arsenate + mycothiol = arseno-mycothiol

698899

-

2.8.4.2

arsenate + mycothiol = arseno-mycothiol + H2O

726005, 737533

-

2.8.4.2

2 entries

7.3.2.1

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

734790, 735262

-

7.3.2.7

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

210280

-

Product in Enzyme-catalyzed Reactions (17 results)

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Show Product (17 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.20.2.1

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

0

-

1.20.2.1

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

0

-

1.20.2.1

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

0

-

1.20.2.1

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

0

-

1.20.2.1

4 entries

1.20.4.1

arsenite + acceptor = arsenate + reduced acceptor

0

-

1.20.9.1

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

0

-

1.20.9.1

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

0

-

1.20.9.1

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

287857, 287858

-

1.20.99.1

arsenite + acceptor = arsenate + reduced acceptor

0

-

1.20.99.1

arsenite + azurin + H2O = arsenate + reduced azurin

0

-

1.20.99.1

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

0

-

1.20.99.1

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

0

-

1.20.99.1

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

0

-

1.20.99.1

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

0

-

1.20.9.1

3 entries

1.20.99.1

6 entries

2.4.1.8

maltose + arsenate = D-glucose + D-glucose + arsenate

489387, 489389, 0, 489403, 489391

-

7.3.2.1

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

0

-

7.3.2.7

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

210280

-

Activator in Enzyme-catalyzed Reactions (22 results)

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Show Activating Compound (22 entries)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

1.1.3.15

increasing activity up to 0.1 M, inhibition of ferricyanide-linked assay above 0.1 M

389695

-

1.17.1.5

activates less than phosphate

644534

-

1.2.1.12

best at 10 mM and up to 30 mM

743740

-

1.20.4.1

10 mM increases enzyme activity by 1.6fold

693214

-

1.20.99.1

-

694407

-

1.20.99.1

dramatically increases expression of ACR2.1

694407

-

1.20.99.1

enzyme activity increases by 108% with arsenate exposure under P-deficient condition and by 130% under P-sufficient condition

693852

-

1.20.99.1

3 entries

1.21.4.2

absolutely required for protein C activity

636467, 636469, 636472

-

1.3.7.1

crude enzyme fractions: pyruvate, ferredoxin, CoA and phosphate or arsenate required for maximal activity

391150

-

1.5.1.15

0.8 mM 104% activity

392078

-

2.1.3.3

potent activator in the concentration range of 0-10 mM

485937

-

2.6.1.31

activation, less effective than phosphate

639962

-

2.7.1.11

50 mM, 2.9fold activation of cytosolic PFK

640445

-

2.7.1.36

hyperbolic activation curve, 13% activation at 25 mM, 87% activation at 500 mM

641436

-

2.7.6.1

0.1 M, 43% of the activity with phosphate

642708

-

2.7.6.1

can partially replace phosphate in activation

642712

-

2.7.6.1

2 entries

2.8.4.1

in absence of reducing agents

393255

-

3.2.1.28

-

679765

-

4.1.2.13

causes further enhancement of enzyme activity when added iin 1-10 mM amounts in the standard assay medium containing KCl. Activity with 12 mM arsenate, is threefold higher than the original aldolase activity

727401

-

4.2.1.2

activates

33728

-

5.4.2.6

increasemM s activity

3333, 3335

-

6.3.1.2

activates gamma-glutamyl transferase reaction

37487

-

Inhibitor in Enzyme-catalyzed Reactions (74 results)

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Show Inhibitors (74 entries)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

1.1.1.37

uncompetitive inhibition

700562

-

1.1.1.44

-

286854

-

1.1.3.15

inhibition of glycolate-ferricyanide or glyoxylate-ferricyanide assay above 0.1 M

389695

-

1.11.1.18

competitive inhibitor

672310

-

1.13.12.7

-

484833, 484844

-

1.13.12.7

lowers the flash height and extends the light emission for a given amount of ATP

484830, 484845

-

1.13.12.7

reversible inhibition

484836

-

1.13.12.7

3 entries

1.14.13.22

-

438970

-

1.2.1.107

the enzyme is allosterically inhibited at concentrations above 10 mM

761019

-

1.2.1.12

linear substrate inhibition, competitive versus phosphate

741758

-

1.2.1.88

-

392055

-

1.4.1.B2

addition of any of the neutral salts causes a parabolic inhibition. A direct comparison of arsenate and chloride ion shows that arsenate is not as inhibitory even though it has a higher ionic strength. Arsenate interacts with the enzyme differently from chloride and bromide. Sulfate, which is a large ion like arsenate, is as inhibitory as chloride (at equivalent ionic strength) with NAD+ as coenzyme, but it is much less effective than chloride with NADP+ as coenzyme

696177

-

1.6.1.1

complete inhibition of activity in either direction

392580

-

1.6.2.6

-

394514

-

1.8.3.1

100 mM, EPR spectra

393030

-

2.1.2.5

weak

485765

-

2.1.3.3

competitive vs. carbamoylphosphate, noncompetitive vs. ornithine

485898

-

2.1.3.6

competitive vs. carbamoylphosphate

485950

-

2.2.1.1

-

485995

-

2.3.1.8

-

487518, 487526, 94495

-

2.3.1.8

50% inhibition at 10 mM

487529

-

2.3.1.8

2 entries

2.4.1.1

-

488294

-

2.4.99.16

-

717816

-

2.7.1.1

catalytically active 51 kDa C fragment of hexokinase

640236

-

2.7.1.77

strong competitive inhibitor

641996

-

2.7.7.35

-

643247

-

2.7.7.35

kinetics

643246

-

2.7.7.35

2 entries

2.7.7.5

-

643453, 643454

-

3.1.1.41

40% inhibition at 1 mM

649397

-

3.1.3.1

-

94572, 94606, 94616

-

3.1.3.1

1 mM Na2HAsO4, 80% inhibition of isoenzyme I, 22% inhibition of isoenzyme II, 40% inhibition of isoenzyme III

94607

-

3.1.3.1

competitive

94613

-

3.1.3.1

irreversible inhibitor

713744

-

3.1.3.1

4 entries

3.1.3.12

10 mM, 10% inhibition

134588, 134594

-

3.1.3.14

-

81020

-

3.1.3.15

-

170824

-

3.1.3.2

-

134710, 134716, 134732, 134747, 134750, 134752, 134756, 134757, 134783

-

3.1.3.2

1 mM, 14% residual activity

729509

-

3.1.3.2

5 mM, complete inhibition

653570

-

3.1.3.2

8% residual activity at 5 mM

682408

-

3.1.3.2

-

134733, 134762

-

3.1.3.2

5 entries

3.1.3.26

-

94799

-

3.1.3.38

-

81095

-

3.1.3.41

competitive. 10 mM, 39% residual activity

751293

-

3.1.3.48

inhibition of protein tyrosine phosphatase activity

666291

-

3.1.3.8

-

114267, 114268, 716570, 749619

-

3.1.3.8

the enzyme of Pteris vittata shows partial resistance to arsenate in contrast to enzymes from other ferns, e.g. Pteris ensiformis and Nephrolepis exaltata

716570

-

3.1.3.8

2 entries

3.1.4.37

-

135382

-

3.2.1.38

-

136323

-

3.2.2.4

-

171839

-

3.4.21.7

organometallic complexes composed of humic acid and arsenic acid show enhanced inhibition of plasmin activity as compared with either arsenic or humic acid alone

653880

-

3.5.1.2

0.5 M, 74% inhibition

209025

-

3.5.1.67

no inhibition

172075

-

3.5.1.67

very slight inhibition

172073

-

3.5.1.67

2 entries

3.5.1.9

strong inhibition for formamidase I, slight inhibition for formamidase II at 1 mM

209244

-

3.6.1.2

slight inhibition

209938

-

4.2.1.24

inhibition of 5-aminolevulinic acid dehydratase activity by arsenic in excised etiolated maize leaf segments during greening. KNO3, chloramphenical, cycloheximide, DTNB and levulinic aciddecrease inhibition. GSH increase inhibition

666162

-

4.2.2.10

1 mM, 92% of initial activity

747235

-

4.2.3.3

-

137601

-

5.3.1.1

-

661085, 748029

-

5.3.1.1

competitive inhibition

727027

-

5.3.1.1

-

2570, 2573, 678177, 690232

-

5.3.1.1

competitive

2562

-

5.3.1.1

4 entries

5.3.1.5

-

2743

-

5.3.4.1

-

3044

-

5.4.2.7

-

3346

-

5.5.1.5

-

3718

-

6.3.4.4

-

1549

-

7.3.2.1

96% inhibition at 0.04 mM

669115

-

7.3.2.1

strong inhibition

670171

-

7.3.2.1

As(V) downregulates genes transcriptionally regulated by Pi starvation, being particularly efficient in the repression of the Pi/As(V) uptake system. The repression occurs conversely to the activation of As(V)-responsive genes, overview

689460

-

7.3.2.1

As(V) represses the activation of genes specifically involved in Pi uptake, while inducing others transcriptionally regulated by As(V), suggesting that converse signaling pathways are involved in plant responses to As(V) and low phosphate availability, As(V) downregulates genes transcriptionally regulated by Pi starvation, being particularly efficient in the repression of the Pi/As(V) uptake system. The repression occurs conversely to the activation of As(V)-responsive genes, overview

689460

-

7.6.2.2

competitive

210398

-

7.6.2.2

competitive inhibitor of daunorubicin transport

210402

-

7.3.2.1

4 entries

7.6.2.2

2 entries

Metals and Ions (12 results)

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Show Metals Ions (12 entries)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

2.3.2.15

-

487893

-

2.3.2.15

activation, wild-type and AtPCS2-enzyme

487890

-

2.3.2.15

activator

675651

-

2.7.1.105

activation

640290

-

2.7.1.105

can replace phosphate

640288

-

2.7.1.105

requirement

640288

-

2.3.2.15

3 entries

2.7.1.105

3 entries

2.7.7.89

activation

81112

-

3.2.1.26

or phosphate is required

136101

-

3.2.1.3

stimulates at 10 mM, 1 mM and 0.1 mM

136200

-

3.5.1.2

50 mM, 800% of the relative activity without addition

655601

-

3.5.99.6

activates

648219

-

6.3.2.9

increases storage stability

653712

-

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

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

EC NUMBER

ENZYME 3D STRUCTURE

1.2.1.11

1ta4, 3D-view

2.4.2.1

3enz, 3D-view

3.6.4.12

3we3, 3D-view

Enzyme Kinetic Parameters

k_cat Value (Turnover Number) (49 results)

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Show Turnover Number (49 entries)

EC NUMBER

TURNOVER NUMBER [1/S]

TURNOVER NUMBER MAXIMUM [1/S]

COMMENTARY

LITERATURE

1.20.4.4

0.061

-

C15A ArsC mutant, at 2 microM AsO43-

639370

1.20.4.4

0.061

-

pH 7.5, 37°C, mutant enzyme C15A, at 0.002 mM arsenate

639370

1.20.4.4

0.075

-

pH 7.5, 37°C, wild-type enzyme, at 0.002 mM arsenate

639370

1.20.4.4

0.075

-

wild-type ArsC, at 2 microM AsO43-

639370

1.20.4.4

0.08

-

C15A ArsC mutant, at 10 mM AsO43-

639370

1.20.4.4

0.08

-

pH 7.5, 37°C, mutant enzyme C15A, at 10 mM arsenate

639370

1.20.4.4

0.09

-

wild-type, pH 8.0, 37°C

726005

1.20.4.4

0.165

-

pH 7.5, 37°C, wild-type enzyme, at 10 mM arsenate

639370

1.20.4.4

0.165

-

wild-type ArsC, at 10 mM AsO43-

639370

1.20.4.4

0.5

-

N-terminally truncated mutant, pH 8.0, 37°C

726005

1.20.4.4

0.58

-

wild-type Staphylococcus aureus, condition: 150 mM NaCl, study about the impact of potassium and the tetrahedral oxyanion sulfate on the steady-state kinetic parameters

705113

1.20.4.4

0.7

-

H62Q mutant Staphylococcus aureus, condition: 150 mM KCl, study about the impact of potassium and the tetrahedral oxyanion sulfate on the steady-state kinetic parameters

705113

1.20.4.4

0.75

-

H62Q mutant Staphylococcus aureus, condition: 150 mM NaCl, study about the impact of potassium and the tetrahedral oxyanion sulfate on the steady-state kinetic parameters

705113

1.20.4.4

0.75

-

pH 7.0, 60°C

727086

1.20.4.4

0.9

-

wild-type Staphylococcus aureus, condition: 150 mM KCl, study about the impact of potassium and the tetrahedral oxyanion sulfate on the steady-state kinetic parameters

705113

1.20.4.4

1.3

-

wild-type Bacillus subtilis, condition: 150 mM NaCl, study about the impact of potassium and the tetrahedral oxyanion sulfate on the steady-state kinetic parameters

705113

1.20.4.4

1.6

-

wild-type Bacillus subtilis, condition: 150 mM KCl, study about the impact of potassium and the tetrahedral oxyanion sulfate on the steady-state kinetic parameters

705113

1.20.4.4

1.6

-

wild-type Bacillus subtilis, condition: 50 mM K2SO4, study about the impact of potassium and the tetrahedral oxyanion sulfate on the steady-state kinetic parameters

705113

1.20.4.4

1.98

-

H62Q mutant Staphylococcus aureus, condition: 50 mM Na2SO4, study about the impact of potassium and the tetrahedral oxyanion sulfate on the steady-state kinetic parameters

705113

1.20.4.4

2

-

wild-type Bacillus subtilis, condition: 50 mM Na2SO4, study about the impact of potassium and the tetrahedral oxyanion sulfate on the steady-state kinetic parameters

705113

1.20.4.4

2.1

-

pH 7.6, 37°C, presence of 150 mM NaCl

732190

1.20.4.4

2.9

-

pH 7.6, 37°C, presence of 50 mM K2SO4

732190

1.20.4.4

2.9

-

wild-type Staphylococcus aureus, condition: 50 mM Na2SO4, study about the impact of potassium and the tetrahedral oxyanion sulfate on the steady-state kinetic parameters

705113

1.20.4.4

3.03

-

H62Q mutant Staphylococcus aureus, condition: 50 mM K2SO4, study about the impact of potassium and the tetrahedral oxyanion sulfate on the steady-state kinetic parameters

705113

1.20.4.4

3.2

-

pH 7.6, 37°C, presence of 150 mM KCl

732190

1.20.4.4

3.65

-

wild-type Staphylococcus aureus, condition: 50 mM K2SO4, study about the impact of potassium and the tetrahedral oxyanion sulfate on the steady-state kinetic parameters

705113

1.20.4.4

26 entries

1.20.9.1

14400

-

-

287859

1.20.99.1

0.012

-

pH 8.5, 30°C, 2 mM glutathione

714217

1.20.99.1

0.017

-

pH 8.5, 30°C, 2 mM glutathione

714217

1.20.99.1

0.025

-

pH 8.5, 30°C, 5 mM glutathione

714217

1.20.99.1

0.03

-

mutant C70S

694407

1.20.99.1

0.03

-

pH 8.5, 30°C, 5 mM glutathione

714217

1.20.99.1

0.05

-

mutant C71S

694407

1.20.99.1

0.14

-

-

694407

1.20.99.1

0.33

-

-

694407

1.20.99.1

14400

-

-

287859

1.20.99.1

9 entries

2.4.1.1

4.9

-

maltohexaose arsenolysis

488295

2.4.1.231

1.15

-

-

674984

2.4.1.7

0.0065

-

pH 7.0, 30°C, arsenolysis, mutant D295E

679850

2.4.1.7

0.0252

-

pH 7.0, 30°C, arsenolysis, mutant D295N

679850

2.4.1.7

170

-

pH 7.0, 30°C, arsenolysis, wild-type enzyme

679850, 686739

2.8.4.2

0.12

-

isoform ArsC2, pH 8.0, presence of sulfate

698899

2.8.4.2

0.17

-

isoform ArsC2, pH 8.0, presence of phosphate

698899

2.8.4.2

0.23

-

isoform ArsC1, pH 8.0, presence of sulfate

698899

2.8.4.2

0.28

-

isoform ArsC2, pH 8.0

698899

2.8.4.2

0.28

-

isoform ArsC2, pH and temperature not specified in the publication

726005

2.8.4.2

0.53

-

isoform ArsC1, pH 8.0

698899

2.8.4.2

0.53

-

isoform ArsC1, pH and temperature not specified in the publication

726005

2.8.4.2

0.6

-

isoform ArsC1, pH 8.0, presence of phosphate

698899

2.4.1.7

3 entries

2.8.4.2

8 entries

K_M Value (77 results)

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Show KM Value (77 entries)

EC NUMBER

KM VALUE [MM]

KM VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

1.2.1.107

0.46

-

at pH 7.0 and 25°C

761917

1.2.1.107

18

-

at pH 8.0 and 40°C

761019

1.2.1.11

1.6

-

-

390200

1.2.1.11

6

-

-

390180

1.2.1.12

1

-

-

287974

1.2.1.12

1.54

-

pH 8.9

287979

1.2.1.12

1.7

-

pH 8.0

287979

1.2.1.12

8.3

-

45°C, pH 7.8

726827

1.2.1.13

30

-

-

288024, 287995

1.2.1.13

43

-

-

11539

1.2.1.13

88

-

-

287999

1.2.1.13

120

-

-

11537

1.2.1.107

2 entries

1.2.1.11

2 entries

1.2.1.12

4 entries

1.2.1.13

4 entries

1.2.3.3

1.25

-

electron acceptor: oxygen

390437

1.20.4.1

0.0002

-

mutant C13A, pH 7.5, temperature not specified in the publication

727076

1.20.4.1

0.0002

-

mutant C35A, pH 7.5, temperature not specified in the publication

727076

1.20.4.1

0.0002

-

wild-type, pH 7.5, temperature not specified in the publication

727076

1.20.4.1

2.3

-

pH 6.5, 30°C

660258

1.20.4.1

2.33

-

pH 6.5, 30°C

660258

1.20.4.1

4.3

-

at pH 9.0, temperature not specified in the publication

745405

1.20.4.1

8

-

-

639366

1.20.4.1

28

-

pH 6.5

676606

1.20.4.1

8 entries

1.20.4.2

109

-

-

287855

1.20.4.4

-999

-

pH 7.5, 37°C, at low substrate concentrations the Km-value for arsenate is 0.0008 mM. Above 1 mM arsenate, a second increase in rate with increasing substrate is observed, with an apparent Km of 2 mM arsenate

639368

1.20.4.4

0.000066

-

pH 7.5, 37°C, wild-type enzyme

639370

1.20.4.4

0.000066

-

wild-type

639370

1.20.4.4

0.000134

-

C15A mutant

639370

1.20.4.4

0.000134

-

pH 7.5, 37°C, mutant enzyme C15A

639370

1.20.4.4

0.0008

-

high affinity

639368

1.20.4.4

0.006

-

pH 7.6, 37°C, presence of 150 mM KCl

732190

1.20.4.4

0.007

-

pH 7.6, 37°C, presence of 50 mM K2SO4

732190

1.20.4.4

0.008

-

pH 7.6, 37°C, presence of 150 mM NaCl

732190

1.20.4.4

0.009

-

wild-type Staphylococcus aureus, condition: 150 mM KCl, study about the impact of potassium and the tetrahedral oxyanion sulfate on the steady-state kinetic parameters

705113

1.20.4.4

0.022

-

wild-type Staphylococcus aureus, condition: 150 mM NaCl, study about the impact of potassium and the tetrahedral oxyanion sulfate on the steady-state kinetic parameters

705113

1.20.4.4

0.032

-

wild-type, pH 8.0, 37°C

726005

1.20.4.4

0.047

-

wild-type Bacillus subtilis, condition: 50 mM K2SO4, study about the impact of potassium and the tetrahedral oxyanion sulfate on the steady-state kinetic parameters

705113

1.20.4.4

0.054

-

wild-type Bacillus subtilis, condition: 150 mM KCl, study about the impact of potassium and the tetrahedral oxyanion sulfate on the steady-state kinetic parameters

705113

1.20.4.4

0.058

-

wild-type Bacillus subtilis, condition: 150 mM NaCl, study about the impact of potassium and the tetrahedral oxyanion sulfate on the steady-state kinetic parameters

705113

1.20.4.4

0.061

-

wild-type Staphylococcus aureus, condition: 50 mM Na2SO4, study about the impact of potassium and the tetrahedral oxyanion sulfate on the steady-state kinetic parameters

705113

1.20.4.4

0.064

-

wild-type Bacillus subtilis, condition: 50 mM Na2SO4, study about the impact of potassium and the tetrahedral oxyanion sulfate on the steady-state kinetic parameters

705113

1.20.4.4

0.08

-

H62Q mutant Staphylococcus aureus, condition: 50 mM Na2SO4, study about the impact of potassium and the tetrahedral oxyanion sulfate on the steady-state kinetic parameters

705113

1.20.4.4

0.081

-

wild-type Staphylococcus aureus, condition: 50 mM K2SO4, study about the impact of potassium and the tetrahedral oxyanion sulfate on the steady-state kinetic parameters

705113

1.20.4.4

0.087

-

H62Q mutant Staphylococcus aureus, condition: 150 mM KCl, study about the impact of potassium and the tetrahedral oxyanion sulfate on the steady-state kinetic parameters

705113

1.20.4.4

0.11

-

N-terminally truncated mutant, pH 8.0, 37°C

726005

1.20.4.4

0.123

-

H62Q mutant Staphylococcus aureus, condition: 150 mM NaCl, study about the impact of potassium and the tetrahedral oxyanion sulfate on the steady-state kinetic parameters

705113

1.20.4.4

0.131

-

H62Q mutant Staphylococcus aureus, condition: 50 mM K2SO4, study about the impact of potassium and the tetrahedral oxyanion sulfate on the steady-state kinetic parameters

705113

1.20.4.4

0.635

-

pH 7.0, 60°C

727086

1.20.4.4

75

-

pH 7.5, temperature not specified in the publication

715567

1.20.4.4

25 entries

1.20.9.1

0.3

-

-

287859

1.20.99.1

0.3

-

-

287859

1.20.99.1

0.9

-

pH 8.5, 30°C, 5 mM glutathione

714217

1.20.99.1

1.7

-

pH 8.5, 30°C, 2 mM glutathione

714217

1.20.99.1

2.5

-

pH 8.5, 30°C, 5 mM glutathione

714217

1.20.99.1

5

-

pH 8.5, 30°C, 2 mM glutathione

714217

1.20.99.1

9.2

-

-

694407

1.20.99.1

9.9

-

mutant C71S

694407

1.20.99.1

12.2

-

-

694407

1.20.99.1

24.4

-

mutant C71S

694407

1.20.99.1

9 entries

1.5.1.15

0.793

-

-

392078

2.1.3.6

4

-

arsenolytic cleavage

485950

2.4.1.1

22.7

-

maltohexaose arsenolysis

488295

2.4.1.8

1.7

-

-

489392

2.4.2.1

0.63

-

-

489688

2.4.2.1

0.8

-

reaction with inosine

489688

2.4.2.1

1.8

-

-

489654

2.4.2.1

3 entries

2.4.2.4

1.3

-

-

638443, 638450

2.7.1.90

3.6

-

pH 7.0, 30°C

642074

2.7.1.90

3.6

-

with D-fructose 1,6-bisphosphate

642074, 642100

2.7.7.53

0.13

-

P1,P4-bis(5'-adenosyl) tetraphosphate-arsenolysis, pH 7.4, 25°C

209909

2.7.7.53

3

-

pH 8.2, 37°C

643507

2.8.4.2

0.036

-

isoform ArsC2, pH 8.0, presence of phosphate

698899

2.8.4.2

0.038

-

isoform ArsC2, pH 8.0, presence of sulfate

698899

2.8.4.2

0.046

-

isoform ArsC1, pH 8.0, presence of sulfate

698899

2.8.4.2

0.082

-

isoform ArsC2, pH 8.0

698899

2.8.4.2

0.082

-

isoform ArsC2, pH and temperature not specified in the publication

726005

2.8.4.2

0.13

-

isoform ArsC1, pH 8.0, presence of phosphate

698899

2.8.4.2

0.142

-

isoform ArsC1, pH 8.0

698899

2.8.4.2

0.142

-

isoform ArsC1, pH and temperature not specified in the publication

726005

2.7.1.90

2 entries

2.7.7.53

2 entries

2.8.4.2

8 entries

K_i Value (38 results)

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Show KI Value (38 entries)

EC NUMBER

KI VALUE [MM]

KI VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

1.1.1.37

8.2

-

for the oxaloacetate reduction

700562

1.1.1.37

77

-

for the malate oxidation

700562

1.1.1.37

2 entries

1.11.1.18

0.12

-

-

672310

1.2.1.12

93

-

pH 8.0, temperature not specified in the publication, recombinant His-tagged wild-type enzyme

741758

2.1.3.6

12

-

-

485950

2.4.1.1

0.5

-

-

488294

2.4.1.1

4.1

-

-

488294

2.7.7.35

0.41

-

ADP/phosphate-exchange reaction

643246, 643247

2.7.7.35

0.41

-

pH 7.8, 30°C

643247

2.7.7.35

0.41

-

pH 7.8, 35°C

643246

2.7.7.35

0.57

-

pH 7.8, 30°C

643247

2.7.7.35

0.57

-

pH 7.8, 35°C

643246

2.7.7.35

0.57

-

phosphorolysis

643246, 643247

3.1.3.1

0.000261

-

pH 9.5, 37°C, standard spectrophotometric assays

713744

3.1.3.1

0.0089

-

pH 9.5, 37°C, ALP immobilized capillary electrophoresis, Ki value is close to the Ki values obtained by the standard spectrophotometric assay

713744

2.4.1.1

2 entries

2.7.7.35

6 entries

3.1.3.1

2 entries

3.1.3.41

0.6

-

pH 3.5, 37°C

751293

5.3.1.1

2

5

above 25 mM, mutant S211A, pH 7.5, 25°C

748029

5.3.1.1

2

5

above 25 mM, mutant Y208A, pH 7.5, 25°C

748029

5.3.1.1

2

5

above 25 mM, mutant Y208F, pH 7.5, 25°C

748029

5.3.1.1

2

5

above 25 mM, mutant Y208S, pH 7.5, 25°C

748029

5.3.1.1

2

5

above 25 mM, mutant Y208T, pH 7.5, 25°C

748029

5.3.1.1

3.8

-

mutant enzyme L7RM, in 30 mM triethanolamine buffer at pH 7.5 and 25°C

727027

5.3.1.1

4.6

-

wild type enzyme, in 30 mM triethanolamine buffer at pH 7.5 and 25°C

727027

5.3.1.1

4.9

-

wild-type, 25°C, pH 7.6

678177

5.3.1.1

4.9

-

wild-type, pH 7.6, 25°C

690232

5.3.1.1

5.1

-

monomeric wild-type, pH 7.6, 25°C

690232

5.3.1.1

5.8

-

mutant P168A, 25°C, pH 7.6

678177

5.3.1.1

6.5

-

wild-type, pH 7.5, 25°C

748029

5.3.1.1

7.8

-

mutant A178L, pH 7.6, 25°C

690232

5.3.1.1

9.6

-

wild type enzyme, in 30 mM triethanolamine buffer at pH 7.5 and 25°C

727027

5.3.1.1

10

-

mutant enzyme L7RM, in 30 mM triethanolamine buffer at pH 7.5 and 25°C

727027

5.3.1.1

11

-

30°C, pH 7.6, wild-type enzyme

661085

5.3.1.1

14

-

mutant S211G, pH 7.5, 25°C

748029

5.3.1.1

17.9

-

monomeric mutant A178L, pH 7.6, 25°C

690232

5.3.1.1

18

-

mutant Y208T/S211G, pH 7.5, 25°C

748029

5.3.1.1

29

-

30°C, pH 7.6, mutant enzyme K174G/T175G/A176G

661085

5.3.1.1

30

-

30°C, pH 7.6, mutant enzyme V167G/W168G

661085

5.3.1.1

31

-

30°C, pH 7.6, mutant enzyme V167G/W168G/K174G/T175G/A176G

661085

5.3.1.1

22 entries

References & Links

Literature References (258)

top print hide

Show Reference (258 entries)

BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

PAGES

1549

4809527

Purification of adenylosuccinate synthetase from rabbit skeletal muscle

1974

Muirhead, K.M.; Bishop, S.H.

J. Biol. Chem.

249

459-464

2562

1128275

Triosephosphate isomerase from human erythrocytes

1975

Gracy, R.W.

Methods Enzymol.

41B

442-447

2570

-

Comparison of a cytosolic and a chloroplast triosephosphate isomerase isoenzyme from rye leaves. I. Purification and catalytic properties

1984

Kurzok, H.G.; Feierabend, J.

Biochim. Biophys. Acta

788

214-221

2573

3311744

Kinetic properties of triose-phosphate isomerase from Trypanosoma brucei brucei

1987

Lambeir, A.M.; Opperdoes, F.R.; Wierenga, R.K.

Eur. J. Biochem.

168

69-74

2743

-

Characterization of extracellular substrate specific glucose and xylose isomerases of Chainia

1984

Vartak, H.G.; Srinivasan, M.C.; Powar, V.K.; Rele, M.V.; Khire, J.M.

Biotechnol. Lett.

6

493-494

3044

-

Protein disulphide-isomerase of mature and developing wheat

1984

De Azevedo, G.M.V.; Brockway, B.E.; Freedman, R.B.; Greenwell, P.; Roden, L.T.

Biochem. Soc. Trans.

12

1043

3333

4212162

Metabolism of trehalose in Euglena gracilis. Partial purification and some properties of phosphoglucomutase acting on beta-glucose 1-phosphate

1974

Belocopitow, E.; Marechal, L.R.

Eur. J. Biochem.

46

631-637

3335

6230052

Partial purification and some properties of beta-phosphoglucomutase from Lactobacillus brevis

1984

Marechal, L.R.; Oliver, G.; Veiga, L.A; de Ruiz Holgado, A.A.P.

Arch. Biochem. Biophys.

228

592-599

3346

6297594

Purification and characterization of phosphopentomutase from rat liver

1983

Barsky, D.L.; Hoffee, P.A.

Biochim. Biophys. Acta

743

162-171

3718

240704

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.

56

193-204

11537

2165475

Glyceraldehyde-3-phosphate dehydrogenase from the hyperthermophilic archaebacterium Pyrococcus woesei: characterization of the enzyme, cloning and sequencing of the gene, and expression in Escherichia coli

1990

Zwickl, P.; Fabry, S.; Bogedain, C.; Haas, A.; Hensel, R.

J. Bacteriol.

172

4329-4338

11539

3569291

Purification and characterization of D-glyceraldehyde-3-phosphate dehydrogenase from the thermophilic archaebacterium Methanothermus fervidus

1987

Fabry, S.; Hensel, R.

Eur. J. Biochem.

165

147-155

33728

-

Fumarase and crotonase

1971

Hill, R.L.; Teipel, J.W.

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

5

539-571

37487

2889467

ADP, chloride ion, and metal ion binding to bovine brain glutamine synthetase

1987

Maurizi, M.R.; Pinkofsky, H.B.; Ginsburg, A.

Biochemistry

26

5023-5031

81020

13345808

Enzymatic formation of glyceryl and phosphoglyceryl methylthiol esters

1956

Black, S.; Wright, N.G.

J. Biol. Chem.

221

171-180

81095

10970181

3-Phosphoglycerate phosphatase in plants. I. Isolation and characterization from sugarcane leaves

1971

Randall, D.D.; Tolbert, N.E.

J. Biol. Chem.

246

5510-5517

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