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• • In Vivo Substrate
  • In Vivo Product
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• Enzyme Kinetic Parameters
• • k_cat Value (Turnover Number)
  • K_M Value
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Ligand dehydroepiandrosterone

Basic Ligand Information

Molecular Structure

Pathway Source

Pathways

KEGG

Microbial metabolism in diverse environments, Ovarian steroidogenesis, Pathways in cancer, Prostate cancer, Steroid degradation, Steroid hormone biosynthesis more

MetaCyc

androgen biosynthesis

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Roles as Enzyme Ligand

In Vivo Substrate in Enzyme-catalyzed Reactions (24 results)

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Show Natural Substrate (24 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.1.1.145

dehydroepiandrosterone + NAD+ = ?

656091

-

1.1.1.145

dehydroepiandrosterone + NAD+ = androst-5-en-3,17-dione + NADH

389383, 389371, 389389, 389401, 655345, 656091, 656577, 656657, 656788, 740914, 740998, 741261, 741423, 389380, 389396, 389393, 389394, 389376, 389391, 389370, 389382, 389400

-

1.1.1.145

dehydroepiandrosterone + NADH + H+ = androsterone + NAD+

656655

-

1.1.3.6

dehydroandrosterone + O2 = ? + H2O2

725869

1coy, 3D-view

1.1.3.6

dehydroepiandrosterone + O2 = androst-5-en-3,17-dione + H2O2

710959

1coy, 3D-view

1.1.1.145

3 entries

1.1.3.6

2 entries

1.14.14.29

dehydroepiandrosterone + NADPH + H+ + O2 = 7alpha-hydroxy-dehydroepiandrosterone + NADP+ + H2O

728174

-

2.8.2.1

3'-phosphoadenylyl sulfate + dehydroepiandrosterone = adenosine 3',5'-bisphosphate + ?

702138

-

2.8.2.14

3'-phosphoadenylyl sulfate + dehydroepiandrosterone = adenosine 3',5'-bisphosphate + ?

702138

-

2.8.2.14

3'-phosphoadenylylsulfate + dehydroepiandrosterone = adenosine 3',5'-bisphosphate + ?

726539

-

2.8.2.14

3'-phosphoadenylylsulfate + dehydroepiandrosterone = adenosine 3',5'-bisphosphate + androst-5-en-17-one 3-sulfate

661602

-

2.8.2.15

3'-phosphoadenylyl sulfate + dehydroepiandrosterone = adenosine 3',5'-bisphosphate + ?

702138

-

2.8.2.15

3'-phosphoadenylyl sulfate + dehydroepiandrosterone = adenosine 3',5'-bisphosphate + dehydroepiandrosterone 3-O-sulfate

673311, 673295, 674394, 677143, 675477, 676256

-

2.8.2.15

3'-phosphoadenylyl sulfate + dehydroepiandrosterone = adenosine 3',5'-bisphosphate + dehydroepiandrosterone 3-sulfate

677268

-

2.8.2.15

3'-phosphoadenylyl sulfate + dehydroepiandrosterone = adenosine 3',5'-bisphosphate + dehydroepiandrosterone O-sulfate

673061

-

2.8.2.15

3'-phosphoadenylyl sulfate + dehydroepiandrosterone = adenosine 3',5'-bisphosphate + dehydroepiandrosterone sulfate

738099, 738552

-

2.8.2.15

3'-phosphoadenylylsulfate + dehydroepiandrosterone = adenosine 3',5'-bisphosphate + androst-5-en-17-one 3-sulfate

662232

-

2.8.2.15

3'-phosphoadenylylsulfate + dehydroepiandrosterone = adenosine 3',5'-bisphosphate + dehydroepiandrosterone 3-sulfate

645733, 645736, 645735, 673295, 724113, 724741, 725980, 724959, 645724, 645739, 645730, 645722, 645731

-

2.8.2.2

3'-phosphoadenylyl sulfate + dehydroepiandrosterone = adenosine 3',5'-bisphosphate + dehydroepiandrosterone 3-sulfate

690709, 691779, 692098, 673295, 694259, 661823, 675680, 675275, 677218

1j99, 3D-view

2.8.2.2

3'-phosphoadenylyl sulfate + dehydroepiandrosterone = adenosine 3',5'-bisphosphate + dehydroepiandrosterone sulfate

675680, 738296

1j99, 3D-view

2.8.2.2

3'-phosphoadenylylsulfate + dehydroepiandrosterone = adenosine 3',5'-bisphosphate + dehydroepiandrosterone 3-sulfate

645781, 645785, 645778, 645790, 645791, 645773, 645774, 645776, 645784, 645792, 645796, 645800, 645793, 645780, 645789, 645782, 645783, 645786, 645779, 645795, 645788

1j99, 3D-view

2.8.2.14

3 entries

2.8.2.15

7 entries

2.8.2.2

3 entries

2.8.2.3

3'-phosphoadenylyl sulfate + dehydroepiandrosterone = adenosine 3',5'-bisphosphate + ?

702138

-

2.8.2.34

3'-phosphoadenylyl 5'-phosphosulfate + dehydroepiandrosterone = adenosine 3',5'-bisphosphate + dehydroepiandrosterone 3-sulfate

659105

-

2.8.2.4

3'-phosphoadenylyl sulfate + dehydroepiandrosterone = adenosine 3',5'-bisphosphate + ?

677219, 702138

-

2.8.2.4

3'-phosphoadenylyl sulfate + dehydroepiandrosterone = adenosine 3',5'-bisphosphate + dehydroepiandrosterone 3-sulfate

677219

-

2.8.2.4

2 entries

In Vivo Product in Enzyme-catalyzed Reactions (5 results)

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Show Natural Product (5 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.14.14.32

7alpha-hydroxypregnenolone + [reduced NADPH-hemoprotein reductase] + O2 = 3beta-hydroxyandrost-5-en-17-one + acetate + [oxidized NADPH-hemoprotein reductase] + H2O

-

-

1.14.14.32

17alpha-hydroxypregnenolone + AH2 + O2 = dehydroepiandrosterone + acetate + A + H2O

-

-

1.14.14.32

17alpha-Hydroxypregnenolone = Dehydroepiandrosterone + acetaldehyde

-

-

3.1.6.2

dehydroepiandrosterone 3-sulfate + H2O = dehydroepiandrosterone + sulfate

-

-

3.1.6.2

dehydroepiandrosterone sulfate + H2O = dehydroepiandrosterone + sulfate

-

-

1.14.14.32

3 entries

3.1.6.2

2 entries

Substrate in Enzyme-catalyzed Reactions (81 results)

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Show Substrate (81 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.1.1.145

3beta-hydroxy-5-androsten-17-one + NAD+ = androstendione + NADH + H+

700557

-

1.1.1.145

5-androsten-3beta-ol-17-one + NAD+ = 5-androsten-3,17-dione + NADH

689697

-

1.1.1.145

androst-5-ene-3beta-ol-17-one + NAD+ = androst-5-ene-3,17-dione + NADH

389402

-

1.1.1.145

dehydroepiandrosterone + NAD+ = ?

670037, 656655, 389370, 662371, 656091

-

1.1.1.145

dehydroepiandrosterone + NAD+ = androst-5-en-3,17-dione + NADH

389383, 389384, 389371, 389389, 389401, 655345, 656091, 656577, 656657, 656788, 688685, 740914, 740998, 741261, 741423, 389380, 389396, 389393, 389394, 389376, 389390, 389391, 389370, 389382, 389400, 740503, 725813, 725820, 724518

-

1.1.1.145

dehydroepiandrosterone + NAD+ = androst-5-en-3,17-dione + NADH + H+

693887, 700182, 685186

-

1.1.1.145

dehydroepiandrosterone + NADH + H+ = androsterone + NAD+

656655

-

1.1.1.145

dehydroepiandrosterone + NADPH = 3beta-hydroxy-5-androsten-17-one + NADP+

389394

-

1.1.1.145

8 entries

1.1.1.148

dehydroepiandrosterone + NADPH = 5-androstene-3alpha,17alpha-diol + NADP+

668078

-

1.1.1.149

dehydroepiandrosterone + NADPH + H+ = ?

740126

-

1.1.1.239

dehydroepiandrosterone + NAD+ = ? + NADH + H+

740637

-

1.1.1.252

5-androstene-3beta-ol-17-one + NADPH + H+ = ? + NADP+

697279

-

1.1.1.270

dehydroepiandrosterone + NADH + H+ = 5-androstene-3,17-dione + NAD+

725813

-

1.1.1.278

dehydroepiandrosterone + NADP+ = ?

691108

-

1.1.1.51

5-androsten-3beta-ol-17-one + NAD(P)+ = 5-androstene-3,17-dione + NAD(P)H + H+

689697

-

1.1.1.51

dehydroepiandrosterone + NAD(P)+ = androst-5-en-3,17-dione + NAD(P)H + H+

699146, 691108

-

1.1.1.51

dehydroepiandrosterone + NAD(P)H + H+ = androstenediol + NAD(P)+

696052

-

1.1.1.51

dehydroepiandrosterone + NAD+ = 4-androstene-3,17-dione + NADH + H+

712201

-

1.1.1.51

dehydroepiandrosterone + NAD+ = androstene-3,17-dione + NADH + H+

713515

-

1.1.1.51

dehydroepiandrosterone + NADH + H+ = ? + NAD+

740637

-

1.1.1.51

dehydroepiandrosterone + NADPH + H+ = androst-5-ene-3beta,17beta-diol + NADP+

700188

-

1.1.1.51

dehydroepiandrosterone + NADPH = 5-androstene-3beta,17beta-diol + NADP+

669905

-

1.1.1.51

dehydroepiandrosterone + NADPH = androstene-3beta,17beta-diol + NADP+

670037, 669905

-

1.1.1.62

3beta-hydroxyandrost-5-en-17-one + NADPH = 3beta,17beta-dihydroxyandrost-5-ene + NADP+

287176

3dhe, 3D-view

1.1.1.62

5-androstene-3beta-ol-17-one + NADPH = 5-androstene-3beta,17beta-diol + NADP+

655524

3dhe, 3D-view

1.1.1.62

dehydroepiandrosterone + NAD(P)H = 5-androstene-3beta,17beta-diol + NAD(P)+

688007

3dhe, 3D-view

1.1.1.62

dehydroepiandrosterone + NAD(P)H = androst-5-ene-3beta,17beta-diol + NAD(P)+

697736

3dhe, 3D-view

1.1.1.62

dehydroepiandrosterone + NADP+ = ?

670265

3dhe, 3D-view

1.1.1.62

dehydroepiandrosterone + NADPH + H+ = 5-androstene-3beta,17beta-diol + NADP+

686263

3dhe, 3D-view

1.1.1.64

dehydroepiandrosterone + NADPH = androst-5-en-3beta,17beta-diol + NADP+

669905

-

1.1.1.64

dehydroepiandrosterone + NADPH = androst-5-ene-3beta,17beta-diol + NADP+

287229

-

1.1.3.6

3beta-hydroxyandrost-5-en-17-one + O2 = androst-5-en-3,17-dione + H2O2

723968

1coy, 3D-view

1.1.3.6

dehydro-epi-androsterone + O2 = ?

655611

1coy, 3D-view

1.1.3.6

dehydroandrosterone + O2 = ? + H2O2

725869

1coy, 3D-view

1.1.3.6

dehydroepiandrosterone + O2 = ?

684653

1coy, 3D-view

1.1.3.6

dehydroepiandrosterone + O2 = androst-5-en-3,17-dione + H2O

710964

1coy, 3D-view

1.1.3.6

dehydroepiandrosterone + O2 = androst-5-en-3,17-dione + H2O2

2892, 287653, 287657, 287648, 287646, 710959

1coy, 3D-view

1.1.3.6

dehydroisoandrosterone + O2 = androst-5-en-3,17-dione + H2O

287672, 657224

1coy, 3D-view

1.1.3.6

trans-dehydroandrosterone + O2 = ?

697914

1coy, 3D-view

1.14.14.29

dehydroepiandrosterone + NADPH + H+ + O2 = 3beta,7alpha-dihydroxy-5-androsten-17-one + NADP+ + H2O

657806

-

1.14.14.29

dehydroepiandrosterone + NADPH + H+ + o2 = 7alpha-hydroxy-dehydroepiandrosterone

686694

-

1.14.14.29

dehydroepiandrosterone + NADPH + H+ + O2 = 7alpha-hydroxy-dehydroepiandrosterone + NADP+ + H2O

686694, 688678, 728174

-

1.14.14.29

dehydroepiandrosterone + NADPH + O2 = 7alpha-hydroxy-dehydroepiandrosterone + NADP+ + H2O

702427

-

1.14.14.29

dehydroepiandrosterone + NADPH + O2 = ? + NADP+ + H2O

702427, 705397

-

1.14.15.30

dehydroepiandrosterone + 2 reduced ferredoxin [iron-sulfur] cluster + H+ + O2 = ?

745648

-

1.14.15.30

dehydroepiandrosterone + NADH + H+ + O2 = 3beta,9alpha-dihydroxy-5-androstene-17-one + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O

745648

-

1.1.1.51

9 entries

1.1.1.62

6 entries

1.1.1.64

2 entries

1.1.3.6

8 entries

1.14.14.29

5 entries

1.14.15.30

2 entries

1.14.15.35

dehydroepiandrostenedione + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2 = ? + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O

727300

-

1.14.15.8

dehydroepiandrosterone + reduced adrenodoxin + O2 = 7beta-hydroxy-dehydroepiandrosterone + oxidized adrenodoxin + H2O

745699

-

2.4.1.173

androst-5-en-3beta-ol-17-one + UDP-glucose = ?

690224

-

2.4.1.173

dehydroepiandrosterone + UDP-glucose = UDP + dehydroepiandrosterone 3-beta-D-glucoside

671624, 672427

-

2.4.1.173

UDP-glucose + dehydroepiandrosterone = UDP + dehydroepiandrosterone 3-beta-D-glucoside

671624

-

2.4.1.173

3 entries

2.4.1.192

androst-5-en-3beta-ol-17-one + UDP-glucose = UDP + androst-5-en-3beta-ol-17-one 3-O-beta-D-glucoside

488871

-

2.8.2.1

3'-phosphoadenylyl sulfate + dehydroepiandrosterone = adenosine 3',5'-bisphosphate + ?

702138

-

2.8.2.1

3'-phosphoadenylylsulfate + dehydroepiandrosterone = adenosine 3',5'-bisphosphate + dehydroepiandrosterone 3-sulfate

645659

-

2.8.2.14

3'-phosphoadenylyl sulfate + dehydroepiandrosterone = adenosine 3',5'-bisphosphate + ?

702138

-

2.8.2.14

3'-phosphoadenylyl-sulfate + dehydroepiandrosterone = adenosine 3',5'-bisphosphate + ?

726539

-

2.8.2.14

3'-phosphoadenylyl-sulfate + dehydroepiandrosterone = adenosine 3',5'-bisphosphate + dehydroepiandrosterone sulfate

645711

-

2.8.2.14

3'-phosphoadenylylsulfate + dehydroepiandrosterone = adenosine 3',5'-bisphosphate + ?

660699, 726539

-

2.8.2.14

3'-phosphoadenylylsulfate + dehydroepiandrosterone = adenosine 3',5'-bisphosphate + androst-5-en-17-one 3-sulfate

661602, 662862

-

2.8.2.15

3'-phosphoadenylyl sulfate + dehydroepiandrosterone = adenosine 3',5'-bisphosphate + ?

702138

-

2.8.2.15

3'-phosphoadenylyl sulfate + dehydroepiandrosterone = adenosine 3',5'-bisphosphate + dehydroepiandrosterone 3-O-sulfate

673311, 673295, 674394, 676256, 677143, 675477, 673061

-

2.8.2.15

3'-phosphoadenylyl sulfate + dehydroepiandrosterone = adenosine 3',5'-bisphosphate + dehydroepiandrosterone 3-sulfate

677268

-

2.8.2.15

3'-phosphoadenylyl sulfate + dehydroepiandrosterone = adenosine 3',5'-bisphosphate + dehydroepiandrosterone O-sulfate

673061

-

2.8.2.15

3'-phosphoadenylyl sulfate + dehydroepiandrosterone = adenosine 3',5'-bisphosphate + dehydroepiandrosterone sulfate

738102, 738099, 738552

-

2.8.2.15

3'-phosphoadenylylsulfate + dehydroepiandrosterone = adenosine 3',5'-bisphosphate + ?

663165

-

2.8.2.15

3'-phosphoadenylylsulfate + dehydroepiandrosterone = adenosine 3',5'-bisphosphate + androst-5-en-17-one 3-sulfate

662232

-

2.8.2.15

3'-phosphoadenylylsulfate + dehydroepiandrosterone = adenosine 3',5'-bisphosphate + dehydroepiandrosterone 3-sulfate

645733, 645736, 645735, 673295, 724113, 724741, 725980, 645722, 645730, 724959, 645739, 645724, 645731

-

2.8.2.1

2 entries

2.8.2.14

5 entries

2.8.2.15

8 entries

2.8.2.18

3'-phosphoadenylylsulfate + dehydroepiandrosterone = adenosine 3',5'-bisphosphate + ?

645722, 645768

-

2.8.2.2

3'-phosphoadenylyl sulfate + dehydroepiandrosterone = adenosine 3',5'-bisphosphate + dehydroepiandrosterone 3-sulfate

690709, 675275, 675604, 691779, 692098, 673295, 694259, 661823, 675680, 677218

1j99, 3D-view

2.8.2.2

3'-phosphoadenylyl sulfate + dehydroepiandrosterone = adenosine 3',5'-bisphosphate + dehydroepiandrosterone sulfate

675680, 738296

1j99, 3D-view

2.8.2.2

3'-phosphoadenylylsulfate + dehydroepiandrosterone = adenosine 3',5'-bisphosphate + ?

660699

1j99, 3D-view

2.8.2.2

3'-phosphoadenylylsulfate + dehydroepiandrosterone = adenosine 3',5'-bisphosphate + androst-5-en-17-one 3-sulfate

660699

1j99, 3D-view

2.8.2.2

3'-phosphoadenylylsulfate + dehydroepiandrosterone = adenosine 3',5'-bisphosphate + dehydroepiandrosterone 3-sulfate

645781, 645785, 645778, 645779, 645780, 645782, 645783, 645786, 645789, 645790, 645791, 645795, 660699, 738101, 645773, 645774, 645776, 645784, 645792, 645788, 645796, 645800, 738032, 738909, 645793

1j99, 3D-view

2.8.2.3

3'-phosphoadenylyl sulfate + dehydroepiandrosterone = adenosine 3',5'-bisphosphate + ?

702138

-

2.8.2.3

3'-phosphoadenylylsulfate + dehydroepiandrosterone = ?

645862

-

2.8.2.2

5 entries

2.8.2.3

2 entries

2.8.2.34

3'-phosphoadenylyl 5'-phosphosulfate + dehydroepiandrosterone = adenosine 3',5'-bisphosphate + dehydroepiandrosterone 3-sulfate

659105, 657890, 657891, 659656

-

2.8.2.4

3'-phosphoadenylyl sulfate + dehydroepiandrosterone = adenosine 3',5'-bisphosphate + ?

677219, 702138

-

2.8.2.4

3'-phosphoadenylyl sulfate + dehydroepiandrosterone = adenosine 3',5'-bisphosphate + dehydroepiandrosterone 3-sulfate

677219

-

2.8.2.4

3'-phosphoadenylylsulfate + dehydroepiandrosterone = adenosine 3',5'-bisphosphate + dehydroepiandrosterone 3-sulfate

645899, 645900, 645906, 645876, 645884, 645902

-

5.3.3.1

dehydroepiandrosterone = 3beta-hydroxy-4-androsten-17-one

652452, 662371

-

5.3.3.1

dehydroepiandrosterone = androstenedione

725807

-

2.8.2.4

3 entries

5.3.3.1

2 entries

Product in Enzyme-catalyzed Reactions (23 results)

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Show Product (23 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.1.1.145

androstenedione + NADPH + H+ = 3beta-hydroxy-5-androsten-17-one + NADP+

-

-

1.1.1.145

dehydroepiandrosterone + NADPH = 3beta-hydroxy-5-androsten-17-one + NADP+

-

-

1.1.1.145

androst-5-en-3,17-dione + NADH = dehydroepiandrosterone + NAD+

-

-

1.1.1.145

3 entries

1.1.1.239

androst-5-ene-3beta,17beta-diol + NAD+ = androst-5-ene-3beta-ol-17-one + NADH

287214

-

1.1.1.270

5-androstene-3,17-dione + NAD+ = dehydroepiandrosterone + NADH + H+

-

-

1.1.1.51

androst-5-ene-3beta,17beta-diol + NADP+ = dehydroepiandrosterone + NADPH

287072, 287073

-

1.1.1.62

5-androstene-3beta,17beta-diol + NAD+ = 5-androstene-3-beta-ol-17-one + NADH

-

3dhe, 3D-view

1.14.14.32

17alpha-hydroxypregnenolone + [reduced NADPH-hemoprotein reductase] + O2 = 3beta-hydroxyandrost-5-en-17-one + acetate + [oxidized NADPH-hemoprotein reductase] + H2

-

-

1.14.14.32

7alpha-hydroxypregnenolone + [reduced NADPH-hemoprotein reductase] + O2 = 3beta-hydroxyandrost-5-en-17-one + acetate + [oxidized NADPH-hemoprotein reductase] + H2O

-

-

1.14.14.32

pregnenolone + [reduced NADPH-hemoprotein reductase] + O2 = 3beta-hydroxyandrost-5-en-17-one + acetate + [oxidized NADPH-hemoprotein reductase] + H2o

-

-

1.14.14.32

17alpha-hydroxypregnenolone + ? + cytochrome b5 = dehydroepiandrosterone + ?

-

-

1.14.14.32

17alpha-hydroxypregnenolone + AH2 + O2 = dehydroepiandrosterone + acetate + A + H2O

-

-

1.14.14.32

17alpha-hydroxypregnenolone + [reduced NADPH-hemoprotein reductase] + O2 = dehydroepiandrosterone + [oxidized NADPH-hemoprotein reductase] + acetate + H2O

-

-

1.14.14.32

17alpha-Hydroxypregnenolone = Dehydroepiandrosterone + acetaldehyde

, 5126, 5131, 390127, 5127, 5130

-

1.14.14.32

17alpha-hydroxyprogesterone + AH2 + O2 = dehydroepiandrosterone + androstenedione + A + H2O

-

-

1.14.14.32

8 entries

3.1.1.79

dehydroepiandrosterone oleate + H2O = dehydroepiandrosterone + oleate

-

-

3.1.6.1

dehydroepiandrosterone 3-sulfate + H2O = dehydroepiandrosterone + sulfate

-

-

3.1.6.2

3beta-hydroxyandrost-5-en-17-one 3-sulfate + H2O = 3beta-hydroxyandrost-5-en-17-one + sulfate

-

-

3.1.6.2

dehydroandrosterone 3-sulfate + H2O = dehydroandrosterone + sulfate

-

-

3.1.6.2

dehydroepiandrosterone 3-sulfate + H2O = dehydroepiandrosterone + sulfate

-

-

3.1.6.2

dehydroepiandrosterone sulfate + H2O = dehydroepiandrosterone + sulfate

-

-

3.1.6.2

dehydroisoandrosterone 3-sulfate + H2O = dehydroisoandrosterone + sulfate

-

-

3.1.6.2

5 entries

3.1.6.8

dehydroisoandrosterone sulfate + H2O = dehydroisoandrosterone + sulfate

-

-

Activator in Enzyme-catalyzed Reactions (1 result)

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Show Activating Compound (1 entry)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

7.6.2.2

stimulation of ATPase-activity arising from co-expression of isoforms ABCG5 and ABCG8

686719

-

Inhibitor in Enzyme-catalyzed Reactions (26 results)

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Show Inhibitors (26 entries)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

1.1.1.145

0.01 mM reduced conversion of pregnenolone to 50%

389382

-

1.1.1.146

treatment of rats induces a shift from isoform 11beta-HSD1 to 11beta-HSD2 expression, increasing conversion from active to inactive glucocorticoids. Dehydroepiandrosterone likely modulates the transcription of 11beta-HSD2 in a phosphatidylinositol-3 kinase/Akt-dependent manner by increasing CCAAT/enhancer-binding protein beta mRNA and protein expression

687317

-

1.1.1.21

i.e. dehydroepiandrosterone

695881

-

1.1.1.49

uncompetitive inhibitor

711462

-

1.1.1.49

non-competitively inhibits

697523

-

1.1.1.49

uncompetitively inhibits bloodstream form cells

696748

-

1.1.1.49

3 entries

1.1.1.B40

treatment of rats induces a shift from isoform 11beta-HSD1 to 11beta-HSD2 expression, increasing conversion from active to inactive glucocorticoids. Dehydroepiandrosterone likely modulates the transcription of 11beta-HSD2 in a phosphatidylinositol-3 kinase/Akt-dependent manner by increasing CCAAT/enhancer-binding protein beta mRNA and protein expression

687317

-

1.14.14.29

inhibits hydroxylation of 5alpha-androstane-3beta,17beta-diol

686694

-

1.14.99.12

-

7389

-

1.3.1.22

good in vitro inhibitory activity, but compound does not bind to the androgen receptors

726491

-

1.4.1.3

-

743356

-

1.4.3.4

at 0.1 mM, inhibition of MAO-A by 44.2%; at 0.1 mM, inhibition of MAO-B by 61.2%

705454

-

2.3.1.26

-

486679

-

2.7.1.33

about 30% residual activity at 0.1 mM (isoform PanK3)

722018

-

2.8.2.15

-

662232

-

2.8.2.15

competitive inhibitor, inhibits cortisol sulfotransferase activity

645722

-

2.8.2.15

i.e. DHEA, substrate inhibition of SULT1A2

673061

-

2.8.2.15

substrate inhibition

677268, 724113

-

2.8.2.18

cortisol as substrate; kinetics

645722

-

2.8.2.18

cortisol as substrate; strong

645768, 645769

-

2.8.2.2

substrate inhibition

645793

1j99, 3D-view

2.8.2.2

substrate inhibition of SULT2A1, structure analysis of SULT2A1/DHEA and SULT2A1/PAP or SULT2A1/ADT, overview

694259

1j99, 3D-view

2.8.2.15

4 entries

2.8.2.18

2 entries

2.8.2.2

2 entries

2.8.2.4

-

645872

-

3.1.6.2

-

135604

-

3.1.6.2

competitive to 16alpha-hydroxydehydroepiandrosterone

135603

-

3.1.6.2

2 entries

5.3.3.1

-

748656

-

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

1.1.1.62

3dhe, 3D-view

1.1.3.6

1coy, 3D-view

2.8.2.2

1j99, 3D-view

Enzyme Kinetic Parameters

k_cat Value (Turnover Number) (67 results)

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Show Turnover Number (67 entries)

EC NUMBER

TURNOVER NUMBER [1/S]

TURNOVER NUMBER MAXIMUM [1/S]

COMMENTARY

LITERATURE

1.1.1.145

0.02

-

wild-type, pH 7.4

688685

1.1.1.145

0.021

-

wild-type, presence of 2-mercatoethanol pH 7.4

688685

1.1.1.145

0.023

-

pH 7.4, 27°C, recombinant isozyme 3beta-HSD1 mutant Q240R

662371

1.1.1.145

0.03

-

mutant C111S, presence of 2-mercatoethanol pH 7.4

688685

1.1.1.145

0.03

-

mutant E192A, pH 7.4, 27°C

725813

1.1.1.145

0.032

-

mutant C111S, pH 7.4

688685

1.1.1.145

0.0333

-

-

389390

1.1.1.145

0.04

-

mutant D61N, pH 7.4, 27°C

725813

1.1.1.145

0.047

-

mutant C111A, presence of 2-mercatoethanol pH 7.4

688685

1.1.1.145

0.048

-

mutant C83A, presence of 2-mercatoethanol pH 7.4

688685

1.1.1.145

0.05

-

mutant C72S, presence of 2-mercatoethanol pH 7.4

688685

1.1.1.145

0.05

-

wild-type 3beta-HSD1, pH 7.4, 27°C

725813

1.1.1.145

0.053

-

mutant C72S, pH 7.4

688685

1.1.1.145

0.055

-

27°C, pH 7.4

656577

1.1.1.145

0.055

-

in 0.02 M potassium phosphate buffer, pH 7.4

700182

1.1.1.145

0.055

-

mutant C83A, pH 7.4

688685

1.1.1.145

0.055

-

pH 7.4, 27°C, recombinant wild-type isozyme 3beta-HSD1

662371

1.1.1.145

0.055

-

wild-type, pH 7.4, 27°C

725820

1.1.1.145

0.06

-

27°C, pH 7.4

656091

1.1.1.145

0.06

-

mutant C111A, pH 7.4

688685

1.1.1.145

0.06

-

mutant E192A, pH 7.4, 27°C

725813

1.1.1.145

0.062

-

pH 7.4, 27°C, recombinant wild-type isozyme 3beta-HSD1

656091

1.1.1.145

0.075

-

mutant Q105M, pH 7.4, 27°C

725820

1.1.1.145

0.075

-

pH 7.4, 27°C, recombinant isozyme 3beta-HSD2 mutant Q105M

662371

1.1.1.145

0.087

-

mutant C72F, pH 7.4

688685

1.1.1.145

0.087

-

mutant C72F, presence of 2-mercatoethanol pH 7.4

688685

1.1.1.145

0.09

-

mutant R195R, pH 7.4, 27°C

725813

1.1.1.145

0.093

-

mutant P195R, pH 7.4, 27°C

725820

1.1.1.145

0.113

-

mutant Q105M, pH 7.4, 27°C

725820

1.1.1.145

0.113

-

pH 7.4, 27°C, recombinant isozyme 3beta-HSD1 mutant Q105M

662371

1.1.1.145

0.115

-

pH 7.4, 27°C, recombinant wild-type isozyme 3beta-HSD2

656091

1.1.1.145

0.118

-

mutant H156Y, pH 7.4, 27°C

725820

1.1.1.145

0.118

-

pH 7.4, 27°C, recombinant wild-type isozyme 3beta-HSD2

662371

1.1.1.145

0.12

-

27°C, pH 7.4

656091

1.1.1.145

0.12

-

27°C, pH 7.4, H156Y mutant 3beta-HSD1

656091

1.1.1.145

0.12

-

mutant R195P, pH 7.4, 27°C

725813

1.1.1.145

0.12

-

pH 7.4, 27°C, recombinant mutant H156Y

656091

1.1.1.145

0.13

-

mutant R195P, pH 7.4, 27°C

725820

1.1.1.145

0.14

-

wild-type 3beta-HSD2, pH 7.4, 27°C

725813

1.1.1.145

0.145

-

wild-type, pH 7.4, 27°C

725820

1.1.1.145

0.217

-

pH 7.4, 27°C, recombinant isozyme 3beta-HSD2 mutant R240Q

662371

1.1.1.145

11.6

-

pH 8.5, 37°C

685186

1.1.1.145

42 entries

1.1.1.149

0.155

-

at pH 7.4 and 37°C

740126

1.1.1.51

0.01

-

pH 7.4, 25°C, recombinant enzyme

740637

1.1.1.62

0.12

-

mutant enzyme L149V

670265

1.1.1.62

0.16

-

wild-type enzyme

670265

1.1.3.6

0.69

-

-

287672

1.1.3.6

0.8

-

assay relies on detection of H2O2 formation

287670

1.1.3.6

0.8

-

H2O2 production assayed, 100 mM phosphate buffer

287674

1.1.3.6

0.8

-

product formation followed at 240 nm in the presence of 0.02 ml H2O2, substrate dissolved in Triton X-100, 100 mM phosphate buffer

287674

1.1.3.6

0.8

-

substrate trans-dehydroandrosterone, detection of product formation at 240 nm. 0.1 M potassium phosphate, 1% Triton X-100, 1.25% propan-2-ol, 25°C and pH 7.5

697914

1.1.3.6

1

-

substrate trans-dehydroandrosterone, rate of H2O2 formation detected with o-dianisidine and horseradish peroxidase. 0.1 M potassium phosphate, 1% Triton X-100, 1.25% propan-2-ol, 25°C and pH 7.5

697914

1.1.3.6

6

-

substrate trans-dehydroandrosterone, rate of H2O2 formation detected with o-dianisidine and horseradish peroxidase. 0.1 M potassium phosphate, 1% Triton X-100, 1.25% propan-2-ol, 25°C and pH 7.5

697914

1.1.3.6

7

-

assay relies on detection of H2O2 formation

287670

1.1.3.6

8.2

-

assay relies on spectroscopic detection of 4-cholesten-3-one formation

287670

1.1.3.6

8.2

-

product formation followed at 240 nm in the presence of 0.02 ml H2O2, substrate dissolved in Triton X-100, 100 mM phosphate buffer

287674

1.1.3.6

8.2

-

substrate trans-dehydroandrosterone, detection of product formation at 240 nm. 0.1 M potassium phosphate, 1% Triton X-100, 1.25% propan-2-ol, 25°C and pH 7.5

697914

1.1.1.62

2 entries

1.1.3.6

11 entries

1.14.14.29

0.033

-

-

686694

2.4.1.173

0.0072

-

for the cytosolic enzyme

672427

2.8.2.15

0.1

-

pH 7.5, 37°C

662232

2.8.2.2

2

-

pH 7.5, 37°C

645774

5.3.3.1

1990

-

mutant Q240R, isoform 1, 27°C, pH 7.4

662371

5.3.3.1

2064

-

mutant R240Q, isoform 2, 27°C, pH 7.4

662371

5.3.3.1

2088

-

mutant Q105M, isoform 1, 27°C, pH 7.4

662371

5.3.3.1

3012

-

wild-type, isoform 1, 27°C, pH 7.4

662371

5.3.3.1

4002

-

mutant Q105M, isoform 2, 27°C, pH 7.4

662371

5.3.3.1

4890

-

wild-type, isoform 2, 27°C, pH 7.4

662371

5.3.3.1

6 entries

K_M Value (147 results)

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Show KM Value (147 entries)

EC NUMBER

KM VALUE [MM]

KM VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

1.1.1.145

0.00009

-

-

389396

1.1.1.145

0.00012

-

3betaHSD VI

389384

1.1.1.145

0.00014

-

3betaHSD I

389383

1.1.1.145

0.00017

-

-

389382

1.1.1.145

0.00042

-

pH 7.5, 37°C

656655

1.1.1.145

0.00049

-

3betaHSD III

389383

1.1.1.145

0.00059

-

37°C, pH 8.4

656655

1.1.1.145

0.0007

-

wild-type, presence of 2-mercatoethanol pH 7.4

688685

1.1.1.145

0.001

-

-

389390

1.1.1.145

0.0016

-

microsomes

389391

1.1.1.145

0.00164

-

mutant Q105M, pH 7.4, 27°C

725820

1.1.1.145

0.0017

-

-

389385

1.1.1.145

0.0018

-

37°C, pH 7.4

656657

1.1.1.145

0.0024

-

type I

389400

1.1.1.145

0.0028

-

mutant C72S, pH 7.4

688685

1.1.1.145

0.0029

-

type II

389400

1.1.1.145

0.0037

-

27°C, pH 7.4

656091, 656577, 656788

1.1.1.145

0.0037

-

in 0.02 M potassium phosphate buffer, pH 7.4

700182

1.1.1.145

0.0037

-

pH 7.4

655345

1.1.1.145

0.0037

-

pH 7.4, 27°C, recombinant wild-type isozyme 3beta-HSD1

656091, 662371

1.1.1.145

0.0037

-

wild type enzyme

389386

1.1.1.145

0.0037

-

wild-type 3beta-HSD1, pH 7.4, 27°C

725813

1.1.1.145

0.0037

-

wild-type, pH 7.4

688685

1.1.1.145

0.0037

-

wild-type, pH 7.4, 27°C

725820

1.1.1.145

0.0044

-

mutant C72S, presence of 2-mercatoethanol pH 7.4

688685

1.1.1.145

0.0045

-

mitochondria

389391

1.1.1.145

0.0045

-

modified enzyme

389386

1.1.1.145

0.005

-

-

389380

1.1.1.145

0.0061

-

pH 7.4, 27°C, recombinant isozyme 3beta-HSD1 mutant Q240R

662371

1.1.1.145

0.0075

-

mutant C83A, presence of 2-mercatoethanol pH 7.4

688685

1.1.1.145

0.0077

-

mutant P195R, pH 7.4, 27°C

725820

1.1.1.145

0.0077

-

mutant R195R, pH 7.4, 27°C

725813

1.1.1.145

0.0082

-

mutant E192A, pH 7.4, 27°C

725813

1.1.1.145

0.01

-

-

389380

1.1.1.145

0.0107

-

mutant R195P, pH 7.4, 27°C

725813, 725820

1.1.1.145

0.011

-

27°C, pH 7.4, S123A mutant 3betaHSD1

656577

1.1.1.145

0.0115

-

mutant C72F, presence of 2-mercatoethanol pH 7.4

688685

1.1.1.145

0.0127

-

mutant C72F, pH 7.4

688685

1.1.1.145

0.0156

-

wild-type 3beta-HSD2, pH 7.4, 27°C

725813

1.1.1.145

0.0156

-

wild-type, pH 7.4, 27°C

725820

1.1.1.145

0.0168

-

mutant C111S, presence of 2-mercatoethanol pH 7.4

688685

1.1.1.145

0.0171

-

mutant C83A, pH 7.4

688685

1.1.1.145

0.0181

-

mutant C111S, pH 7.4

688685

1.1.1.145

0.0237

-

mutant C111A, presence of 2-mercatoethanol pH 7.4

688685

1.1.1.145

0.025

-

pH 7.4, 27°C, recombinant isozyme 3beta-HSD2 mutant Q105M

662371

1.1.1.145

0.0268

-

mutant C111A, pH 7.4

688685

1.1.1.145

0.0327

-

pH 7.4, 27°C, recombinant isozyme 3beta-HSD2 mutant R240Q

662371

1.1.1.145

0.0351

-

mutant E192A, pH 7.4, 27°C

725813

1.1.1.145

0.04

-

mutant Q105M, pH 7.4, 27°C

725820

1.1.1.145

0.0405

-

pH 7.4, 27°C, recombinant isozyme 3beta-HSD1 mutant Q105M

662371

1.1.1.145

0.042

-

27°C, pH 7.4, H156Y mutant

656788

1.1.1.145

0.042

-

27°C, pH 7.4, H156Y mutant 3beta-HSD1

656091

1.1.1.145

0.042

-

pH 7.4, H156Y mutant

655345

1.1.1.145

0.0424

-

mutant H156Y, pH 7.4, 27°C

725820

1.1.1.145

0.0424

-

pH 7.4, 27°C, recombinant mutant H156Y

656091

1.1.1.145

0.047

-

27°C, pH 7.4

655345, 656091, 656788

1.1.1.145

0.0473

-

pH 7.4, 27°C, recombinant wild-type isozyme 3beta-HSD2

656091, 662371

1.1.1.145

0.0643

-

mutant D61N, pH 7.4, 27°C

725813

1.1.1.145

0.114

-

-

389394

1.1.1.145

0.13

-

NAD+ as cofactor

389402

1.1.1.145

0.221

-

pH 8.5, 37°C

685186

1.1.1.145

0.642

-

pH 7.8, 30°C

689697

1.1.1.145

62 entries

1.1.1.149

0.006

-

at pH 7.4 and 37°C

740126

1.1.1.51

0.00001

-

37°C, pH not specified in the publication

713515

1.1.1.51

0.0043

-

pH 7.4, 25°C, recombinant enzyme

740637

1.1.1.51

0.642

-

50°C, pH 7.8

689697

1.1.1.62

0.0172

-

mutant enzyme L149V

670265

1.1.1.62

0.045

-

wild-type enzyme

670265

1.1.1.62

0.0598

-

-

287176

1.1.3.6

0.0036

-

-

2892

1.1.3.6

0.0275

-

-

287672

1.1.3.6

0.2

-

pH 7.5, 37°C, full-length isozyme ChoM2

725869

1.1.3.6

0.2

-

substrate trans-dehydroandrosterone, rate of H2O2 formation detected with o-dianisidine and horseradish peroxidase. 0.1 M potassium phosphate, 1% Triton X-100, 1.25% propan-2-ol, 25°C and pH 7.5

697914

1.1.3.6

0.24

-

pH 7.5, 37°C

725869

1.1.3.6

0.25

-

pH 7.5, 37°C, truncated isozyme ChoM2

725869

1.1.3.6

0.3

-

-

287674

1.1.3.6

0.3

-

assay relies on spectroscopic detection of 4-cholesten-3-one formation

287670

1.1.3.6

0.3

-

substrate trans-dehydroandrosterone, detection of product formation at 240 nm. 0.1 M potassium phosphate, 1% Triton X-100, 1.25% propan-2-ol, 25°C and pH 7.5

697914

1.1.3.6

0.4

-

-

287673

1.1.3.6

0.491

-

pH 7.5, 37°C

710964

1.1.3.6

0.5

-

-

287674

1.1.3.6

0.5

-

assay relies on detection of H2O2 formation

287670

1.1.3.6

0.8

-

-

287674

1.1.3.6

0.8

-

assay relies on detection of H2O2 formation

287670

1.1.3.6

0.9

-

substrate trans-dehydroandrosterone, rate of H2O2 formation detected with o-dianisidine and horseradish peroxidase. 0.1 M potassium phosphate, 1% Triton X-100, 1.25% propan-2-ol, 25°C and pH 7.5

697914

1.1.3.6

1

-

in the presence and absence of undecanol

287653

1.1.3.6

1.2

-

-

287674

1.1.3.6

1.2

-

assay relies on spectroscopic detection of 4-cholesten-3-one formation

287670

1.1.3.6

1.2

-

substrate trans-dehydroandrosterone, detection of product formation at 240 nm. 0.1 M potassium phosphate, 1% Triton X-100, 1.25% propan-2-ol, 25°C and pH 7.5

697914

1.14.14.29

0.005

-

-

686694

1.14.14.29

0.014

-

pH 7.4, 37°C

657806

1.1.1.51

3 entries

1.1.1.62

3 entries

1.1.3.6

20 entries

1.14.14.29

2 entries

1.14.15.35

0.326

-

wild-type, pH 7.5, 37°C, S50 value, Hill coefficient 1.55

727300

2.4.1.173

0.04

-

activity is assayed radiometrically using UDP-[U-14C] glucose, at pH 8.0 and 37°C

671624

2.4.1.173

0.043

-

-

671624

2.4.1.173

0.119

-

for the cytosolic enzyme

672427

2.8.2.14

0.0014

-

isoform SULT2A1, in 50 mM Tris/HCl buffer, pH 7.4, 1 mM dithiothreitol, 5 mM MgCl2, and 1 mg/ml bovine serum albumin, at 37°C

702138

2.8.2.14

0.00383

-

apparent value, at pH 5.5 and 7.4, at 37°C

726539

2.8.2.14

0.00383

-

apparent value, in 50 mM NaH2PO4 buffer (pH 5.5), 2 mM MgCl2, at 37°C

726539

2.8.2.15

0.0006

-

truncated isoform SULT2B1b, in 50 mM Tris-HCl, pH 7.5, 10 mM MgCl2, at 37°C

673295

2.8.2.15

0.000788

-

pH 7.7, 37°C, 3-betaHST isoform

645736

2.8.2.15

0.0008

-

in 0.25 M potassium phosphate at pH 7.0, and 7.5 mM 2-mercaptoethanol, at 37°C

724741

2.8.2.15

0.0008

-

in 0.25 M potassium phosphate buffer (pH 7.0), at 37°C

724113

2.8.2.15

0.0016

-

pH 7.5, ?

645729

2.8.2.15

0.0019

-

pH 7.4, 37°C, isoenzyme DHEA-ST

645739

2.8.2.15

0.0031

-

pH 7.5, 37°C

662232

2.8.2.15

0.0038

-

full-length isoform SULT2B1b, in 50 mM Tris-HCl, pH 7.5, 10 mM MgCl2, at 37°C

673295

2.8.2.15

0.0044

-

pH 7.4, 37°C, isoenzyme His-SULT2B1a

645739

2.8.2.15

0.0051

-

isoform SULT2A1, in 50 mM Tris/HCl buffer, pH 7.4, 1 mM dithiothreitol, 5 mM MgCl2, and 1 mg/ml bovine serum albumin, at 37°C

702138

2.8.2.15

0.0093

-

pH 7.4, 37°C, isoenzyme SULT2B1a

645739

2.8.2.15

0.0109

-

pH 7.4, 37°C, isoenzyme His-SULT2B1b

645739

2.8.2.15

0.0185

-

pH 7.4, 37°C, isoenzyme SULT2B1b

645739

2.8.2.15

0.02

-

pH 7.5, 25°C, BNST4

663165

2.8.2.15

0.025

-

pH 7.0, 37°C, recombinant SULT1A2

673061

2.8.2.2

0.0006

-

pH 7.5, 37°C, recombinant truncated mutant SULT2B1

673295

2.8.2.2

0.0007

-

pH 7.0, 25°C, recombinant mutant Y238W

694259

2.8.2.2

0.0011

-

pH 7.0, 25°C, recombinant mutant Y238F

694259

2.8.2.2

0.001157

-

pH 7.7, 37°C

645781

2.8.2.2

0.0013

-

pH 7.0, 25°C, recombinant mutant M137I

694259

2.8.2.2

0.0013

-

pH 7.0, 25°C, recombinant mutant M137W

694259

2.8.2.2

0.0019

-

pH 7.0, 25°C, recombinant mutant M137V

694259

2.8.2.2

0.0019

-

pH 7.5, 37°C

645791

2.8.2.2

0.002

-

pH 7.4, 37°C

645798

2.8.2.2

0.0023

-

isoform SULT2B1a, pH and temperature not specified in the publication

738296

2.8.2.2

0.0025

-

isoform SULT2A1, pH and temperature not specified in the publication

738296

2.8.2.2

0.0025

-

pH 7.0, 25°C, recombinant wild-type enzyme

694259

2.8.2.2

0.0033

-

pH 7.0, 25°C, recombinant mutant Y238A

694259

2.8.2.2

0.0036

-

pH 7.0, 25°C, recombinant mutant M137I/Y238A

694259

2.8.2.2

0.0038

-

pH 7.5, 37°C, recombinant wild-type, full-length SULT2B1

673295

2.8.2.2

0.0042

-

pH 7.0, 25°C, recombinant mutant M137V/Y238A

694259

2.8.2.2

0.0044

-

isoform SULT2B1b, pH and temperature not specified in the publication

738296

2.8.2.2

0.006

-

pH 8.0, 37°C

645773

2.8.2.2

0.0065

-

pH 7.0, 25°C, recombinant mutant M137V/Y238A

694259

2.8.2.2

0.0086

-

pH 7.5, 37°C

645792

2.8.2.2

0.012

-

-

645774

2.8.2.2

0.012

-

pH 5.5, 37°C

645776

2.8.2.2

0.0179

-

pH 7.5, 37°C, recombinant isozyme SULT2B1a

661823

2.4.1.173

3 entries

2.8.2.14

3 entries

2.8.2.15

15 entries

2.8.2.2

23 entries

2.8.2.34

0.00072

-

pH 6.5, 37°C, 5 mM MgCl2

659656

2.8.2.4

0.00005

-

pH 7.0, 37°C, SULT1E1-K85A

645902

2.8.2.4

0.0002

-

pH 7.0, 37°C, SULT1E1-wild-type

645902

2.8.2.4

0.00085

-

pH 6.5, 37°C

645884

2.8.2.4

0.0607

-

pH 7.0, 37°C, SULT1E1-wild-type

645902

5.3.3.1

0.0175

-

mutant R240Q, isoform 2, 27°C, pH 7.4

662371

5.3.3.1

0.0279

-

wild-type, isoform 1, 27°C, pH 7.4

662371

5.3.3.1

0.033

-

mutant Q105M, isoform 1, 27°C, pH 7.4

662371

5.3.3.1

0.0623

-

mutant Q240R, isoform 1, 27°C, pH 7.4

662371

5.3.3.1

0.0808

-

mutant Q105M, isoform 2, 27°C, pH 7.4

662371

5.3.3.1

0.0884

-

wild-type, isoform 2, 27°C, pH 7.4

662371

2.8.2.4

4 entries

5.3.3.1

6 entries

K_i Value (18 results)

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Show KI Value (18 entries)

EC NUMBER

KI VALUE [MM]

KI VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

1.1.1.49

0.0011

-

in the presence of NADP+

696748

1.1.1.49

0.0017

-

in the presence of D-glucose 6-phosphate

696748

1.1.1.49

0.0215

-

substrate D-glucose 6-phosphate, pH 7.6, temperature not specified in the publication

711462

1.1.1.49

0.0223

-

substrate NADP+, pH 7.6, temperature not specified in the publication

711462

1.1.1.49

4 entries

1.14.14.29

0.024

-

-

686694

2.8.2.15

0.008

-

in 0.25 M potassium phosphate buffer (pH 7.0), at 37°C

724113

2.8.2.15

0.0106

-

pH 7.5, 37°C

662232

2.8.2.15

0.112

-

pH 7.0, 37°C, recombinant SULT1A2

673061

2.8.2.2

0.0061

-

pH 7.0, 25°C, recombinant wild-type enzyme

694259

2.8.2.2

0.0071

-

pH 7.0, 25°C, recombinant mutant M137W

694259

2.8.2.2

0.012

-

pH 7.0, 25°C, recombinant mutant Y238F

694259

2.8.2.2

0.015

-

pH 7.0, 25°C, recombinant mutant Y238W

694259

2.8.2.2

0.036

-

pH 7.0, 25°C, recombinant mutant M137I

694259

2.8.2.2

0.045

-

pH 7.0, 25°C, recombinant mutant Y238A

694259

2.8.2.2

0.053

-

pH 7.0, 25°C, recombinant mutant M137V

694259

2.8.2.2

0.17

-

pH 7.0, 25°C, recombinant mutant M137I/Y238A

694259

2.8.2.2

0.466

-

pH 7.0, 25°C, recombinant mutant M137V/Y238A

694259

2.8.2.15

3 entries

2.8.2.2

9 entries

2.8.2.4

0.17

-

pH 8.1, 37°C

645872

IC₅₀ Value (7 results)

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Show IC50 Value (7 entries)

EC NUMBER

IC50 VALUE

IC50 VALUE MAXIMUM

COMMENTARY

LITERATURE

1.1.1.21

0.0011

-

in 0.1 M potassium phosphate, pH 7.4, at 25°C

695881

1.1.1.49

0.0056

-

pH 7.6, temperature not specified in the publication

711462

1.3.1.22

0.000025

-

pH 6.5, 37°C

726491

1.4.1.3

0.0072

-

pH 8.0, temperature not specified in the publication

743356

1.4.1.3

0.0294

-

presence of 0.1 M ADP, pH 8.0, temperature not specified in the publication

743356

1.4.1.3

0.216

-

pH 8.0, temperature not specified in the publication

743356

1.4.1.3

0.396

-

presence of 0.1 M ADP, pH 8.0, temperature not specified in the publication

743356

1.4.1.3

4 entries

References & Links

Literature References (196)

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Show Reference (196 entries)

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1983

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Biochim. Biophys. Acta

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1979

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287670

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Characterization of cholesterol oxidase from Streptomyces hygroscopicus and Brevibacterium sterolicum

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287672

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Crystal structure determination of cholesterol oxidase from Streptomyces and structural characterization of key active site mutants

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10467115

Cholesterol oxidase from Streptomyces hycroscopicus and Brevibacterium sterolicum: effect of surfactants and organic solvents on activity

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Kinetic mechanisms of cholesterol oxidase from Streptomyces hygroscopicus and Brevibacterium sterolicum

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495965

Preparation of highly purified 3alpha- and 3beta-hydroxysteroid dehydrogenases from Pseudomonas sp

1979

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Affinity labeling of human placental 3beta-hydroxy-DELTA5-steroid dehydrogenase and steroid delta-isomerase: evidence for bifunctional catalysis by a different conformation of the same protein for each enzyme activity

1992

Thomas, J.L.; Strickler, R.C.; Myers, R.P.; Covey, D.F

Biochemistry

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389376

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Purification and properties of 3-beta-hydroxysteroid dehydrogenase and delta-5-3-ketosteroid isomerase from bovine corpora lutea

1966

Cheatum, S.G.; Warren, J.C.

Biochim. Biophys. Acta

122

1-13

389380

6603965

Differences in inhibition by various steroids of rat testis and Pseudomonas testosteroni DELTA5-3beta-hydroxysteroid dehydrogenase

1983

Spona, J.

Endocrinol. Exp.

17

107-118

389382

11070354

Kinetic properties of microsomal 3beta hydroxysteroid dehydrogenase-isomerase from the testis of Bufo arenarum H

2000

Pozzi, A.G.; Canosa, L.F.; Calvo, J.C.; Ceballos, N.R.

J. Steroid Biochem. Mol. Biol.

73

257-264

389383

8477648

Enzyme characteristics of two distinct forms of mouse 3beta-hydroxysteroid dehydrogenase/DELTA5-DELTA4-isomerase complementary deoxyribonucleic acids expressed in COS-1 cells

1993

Clarke, T.R.; Bain, P.A.; Sha, L.; Payne, A.H.

Endocrinology

132

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389384

9075693

Isolation of a new mouse 3beta-hydroxysteroid dehydrogenase isoform, 3beta-HSD VI, expressed during early pregnancy

1997

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Endocrinology

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389385

10686147

Membrane-bound human 3beta-hydroxysteroid dehydrogenase: overexpression with his-tag using a baculvirus system and single-step purification

2000

Huang, Y.W.; Lu, M.L.; Qi, H.; Lin, S.X.

Protein Expr. Purif.

18

169-174

389386

11463578

The engineered, cytosolic form of human type I 3beta-hydroxysteroid dehydrogenase/isomerase: purification, characterization and crystallization

2001

Thomas, J.L.; Mason, J.I.; Blanco, G.; Veisaga, M.L.

J. Mol. Endocrinol.

27

77-83

389389

11061520

3beta-Hydroxysteroid dehydrogenase/DELTA5---4-isomerase activity associated with the human 17beta-hydroxysteroid dehydrogenase type 2 isoform

2000

Suzuki, T.; Sasana, H.; Andersson, S.; Mason, J.I.

J. Clin. Endocrinol.

85

3669-3672

389390

10704908

Bovine adrenal 3beta-hydroxysteroid dehydrogenase (E.C. 1.1.1.145)/5-ene-4-ene isomerase (E.C. 5.3.3.1): characterization and its inhibition by isoflavones

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Wong, C.K.; Keung, W.M.

J. Steroid Biochem. Mol. Biol.

71

191-202

389391

8119176

Characterization of the 3beta-hydroxysteroid dehydrogenase activity associated with bovine adrenocortical mitochondria

1994

Cherradi, N.; Defaye, G.; Chambaz, E.M.

Endocrinology

134

1358-1364

389393

1388046

Kinetic evidence for separate 3beta-hydroxysteroid dehydrogenase-isomerases in androgen and 16-androstene biosynthetic pathways in the pig testis

1992

Hebert, P.; Cooke, G.M.

J. Steroid Biochem. Mol. Biol.

42

901-910

389394

7841933

Purification and characterization of 5alpha-dihydrotestosterone 3beta-hydroxysteroid dehydrogenase from mature pig testicular cytosol

1994

Nakajin, S.; Ishii, A.; Shinoda, M.

Biol. Pharm. Bull.

17

1155-1160

389396

1955079

3beta-Hydroxysteroid dehydrogenase/DELTA 5-4-isomerase expression in rat and characterization of the testis isoform

1991

Lorence, M.C.; Naville, D.; Graham-Lorence, S.E.; Mack, S.O.; Murry, B.A.; Trant, J.M.; Mason, J.I.

Mol. Cell. Endocrinol.

80

21-31

389400

8547173

Expression and characterization of isoforms of 3beta-hydroxysteroid dehydrogenase/delta 5->4-isomerase in the hamster

1995

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J. Steroid Biochem. Mol. Biol.

55

481-487

389401

7918109

Over-expression of human type I (placental) 3beta-hydroxy-5-ene-steroid dehydrogenase/isomerase in insect cells infected with recombinant baculovirus

1994

Nash, W.E.; Mercer, R.W.; Blanco, G.; Strickler, R.C.; Mason, J.I.; Thomas, J.L.

J. Steroid Biochem. Mol. Biol.

50

235-240

389402

10550629

DELTA5-3beta-Hydroxysteroid dehydrogenase from Digitalis lanata Ehrh. - a multifunctional enzyme in steroid metabolism?

1999

Finsterbusch, A.; Lindemann, P.; Grimm, R.; Eckerskorn, C.; Luckner, M.

Planta

209

478-486

390127

9115645

Characterization of the adrenal cytochrome P450C17 in the hamster, a small animal model for the study of adrenal dehydroepiandrosterone biosynthesis

1997

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DNA Cell Biol.

16

357-368

486679

7362263

Acyl CoA:cholesterol acyl transferase activity in human placental microsomes: inhibition by progesterone

1980

Simpson, E.R.; Burkhart, M.F.

Arch. Biochem. Biophys.

200

79-85

488871

-

Substrate specificity of partially purified UDP-glucose:nuatigenin glucosyltransferase from oat leaves

1988

Kalinowska, M.; Wojciechowski, Z.A.

Plant Sci.

55

239-245

645659

8117269

Human liver thermolabile phenol sulfotransferase: cDNA cloning, expression and characterization

1994

Wood, T.C.; Aksoy, I.A.; Aksoy, S.; Weinshilboum, R.M.

Biochem. Biophys. Res. Commun.

198

1119-1127

645711

6928376

Partial purification of a human liver sulphotransferase active towards bile salts

1980

Loeoef, L.; Hjerten, S.

Biochim. Biophys. Acta

617

192-204

645722

737567

Enzymatic sulfation of steroids. V. Partial purification and some properties of sulfotransferase III, the major glucocorticoid sulfotransferase of liver cytosol from male rats

1978

Singer, S.S.; Gebhart, J.; Hess, E.

Can. J. Biochem.

56

1028-1035

645724

6932974

Enzymic synthesis of steroid sulphates. XIII. Isolation and properties of dehydroepiandrosterone sulphotransferase from human foetal adrenals

1980

Adams, J.B.; McDonald, D.

Biochim. Biophys. Acta

615

275-278

645729

2764897

Purification and characterization of human liver dehydroepiandrosterone sulphotransferase

1989

Falany, C.N.; Vasquez, M.E.; Kalb, J.M.

Biochem. J.

260

641-646

645730

-

Purification and immunochemical charcterization of a male-specific rat liver oestrogen sulphotransferase

1993

Borthwick, E.B.; Burchell, A.; Coughtrie, M.W.H.

Biochem. J.

289

719-725

645731

8297382

Identification of a new adult human liver sulfotransferase with specificity for endogenous and xenobiotic estrogens

1994

Forbes-Bamforth, K.J.; Coughtrie, M.W.H.

Biochem. Biophys. Res. Commun.

198

707-711

645733

8943792

Steroid sulfotransferases

1996

Luu-The, V.; Bernier, F.; Dufort, I.

J. Endocrinol.

150

87-97

645735

9484797

Mouse steroid sulfotransferases. Substrate specificity and preliminary X-ray crystallographic analysis

1998

Kakuta, Y.; Pedersen, L.C.; Chae, K.; Song, W.C.; Leblanc, D.; London, R.; Carter, C.W.; Negishi, M.

Biochem. Pharmacol.

55

313-317

645736

10493595

Testosterone sulfotransferase: Evidence in the guinea pig that this reaction is carried out by 3alpha-hydroxysteroid sulfotransferase

1999

Park, B.C.; Lee, Y.C.; Strott, C.A.

Steroids

64

510-517

645739

11457664

Expression and characterization of the human 3b-hydroxysteroid sulfotransferases (SULT2B1alpha and SULT2B1beta)

2001

Meloche, C.A.; Falany, C.N.

J. Steroid Biochem. Mol. Biol.

77

261-269

645768

485156

Partial purification and some properties of rat liver sulfotransferase I, a glucocorticoid sulfotransferase usually restricted to female rats

1979

Singer, S.S.

Arch. Biochem. Biophys.

196

340-349

645769

6936065

Enzymatic sulfation of steroids. XI. The extensive purification and some properties of hepatic sulfotransferase III from female rats

1980

Singer, S.S.; Bruns, L.

Can. J. Biochem.

58

660-666

645773

4129

Studies on a 3beta-hydroxysteroid sulphotransferase from rat liver

1976

Ryan, R.A.; Carroll, J.

Biochim. Biophys. Acta

429

391-401

645774

6935986

The identity of alcohol sulfotransferases with hydroxysteroid sulfotransferases

1980

Lyon, E.S.; Jakoby, W.B.

Arch. Biochem. Biophys.

202

474-481

645776

6173569

Hydroxysteroid sulfotransferase

1981

Lyon, E.S.; Marcus, C.J.; Wang, J.L.; Jakoby, W.B.

Methods Enzymol.

77

206-213

645778

1355717

Sulfation of estrone and 17beta-estradiol in human liver. Catalysis by thermostable phenol sulfotransferase and by dehydroepiandrosterone sulfotransferase

1992

Hernandez, J.S.; Watson, R.W.G.; Wood, T.C.; Weinshilboum, R.M.

Drug Metab. Dispos.

20

413-422

645779

1520333

Molecular cloning of the alcohol/hydroxysteroid form (hSTa) of sulfotransferase from human liver

1992

Kong, A.N.T.; Yang, L.; Ma, M.; Tao, D.; Bjornsson, T.D.

Biochem. Biophys. Res. Commun.

187

448-454

645780

-

Cloning and expression of human liver dehydroepiandrosterone sulphotransferase

1993

Comer, K.A.; Falany, J.L.; Falany, C.N.

Biochem. J.

289

233-240

645781

8226877

Isolation of two distinct 3-hydroxysteroid sulfotransferases from the guinea pig adrenal. Evidence for 3alpha-hydroxy versus 3beta-hydroxy stereospecificity

1993

Driscoll, W.J.; Martin, B.M.; Chen, H.C.; Strott, C.A.

J. Biol. Chem.

268

23496-23503

645782

8299591

Dehydroepiandrosterone sulfotransferase in the developing human fetus: quantitative biochemical and immunological characterization of the hepatic, renal, and adrenal enzymes

1994

Barker, E.V.; Hume, R.; Hallas, A.; Coughtrie, W.H.

Endocrinology

134

982-989

645783

8597484

Human dehydroepiandrosterone sulfotransferase. Purification, molecular cloning, and characterization

1995

Falany, C.N.; Comer, K.A.; Dooley, T.P.; Glatt, H.

Ann. N. Y. Acad. Sci.

774

59-72

645784

8924618

Influence of substrate structure on the catalytic efficiency of hydroxysteroid sulfotransferase STa in the sulfation of alcohols

1996

Chen, G.; Banoglu, E.; Duffel, M.W.

Chem. Res. Toxicol.

9

67-74

645785

8969973

Steroid sulfotransferases

1996

Strott, C.A.

Endocr. Rev.

17

670-697

645786

9037254

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