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Ligand reduced adrenodoxin

Basic Ligand Information

Molecular Structure

Pathway Source

Pathways

BRENDA

androgen and estrogen metabolism, bile acid biosynthesis, neutral pathway

MetaCyc

11-oxyandrogens biosynthesis, bile acid biosynthesis, neutral pathway, ecdysone and 20-hydroxyecdysone biosynthesis, glucocorticoid biosynthesis, mineralocorticoid biosynthesis, pregnenolone biosynthesis, vitamin D3 biosynthesis more

Show all BRENDA pathways known for reduced adrenodoxin

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Roles as Enzyme Ligand

In Vivo Substrate in Enzyme-catalyzed Reactions (19 results)

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Show Natural Substrate (19 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.14.14.25

cholesterol + reduced adrenodoxin + O2 = 24-hydroxycholesterol + oxidized adrenodoxin + H2O

675535, 676852

-

1.14.15.15

(24S)-3beta-hydroxy-24-methyl-5alpha-cholesta-8(14),22-dien-15-one + reduced adrenodoxin + H+ + O2 = ?

702407

-

1.14.15.15

(25R)-5beta-cholestane-3alpha,7alpha,12alpha,27-tetraol + reduced adrenodoxin + O2 = 3alpha,7alpha,12alpha-trihydroxy-5beta-cholestanoic acid + oxidized adrenodoxin + H2O

674402

-

1.14.15.15

3beta-hydroxy-5alpha-cholest-8(14)-en-15-one + reduced adrenodoxin + H+ + O2 = ?

702407

-

1.14.15.15

5-cholestene-3beta,7alpha-diol + reduced adrenodoxin + O2 = 5-cholestene-3alpha,7alpha,26-triol + oxidized adrenodoxin + H2O

674399, 674400

-

1.14.15.15

5beta-cholestane-3alpha,7alpha,12alpha,26-tetraol + reduced adrenodoxin + O2 = 3alpha,7alpha,12alpha-trihydroxy-5beta-cholestan-26-al + oxidized adrenodoxin + H2O

389410, 288209, 288207

-

1.14.15.15

5beta-cholestane-3alpha,7alpha,12alpha-triol + reduced adrenodoxin + H+ + O2 = (25R)-5beta-cholestane-3alpha,7alpha,12alpha,26-tetraol + oxidized adrenodoxin + H2O

705935

-

1.14.15.15

5beta-cholestane-3alpha,7alpha,12alpha-triol + reduced adrenodoxin + O2 = (25R)-5beta-cholestane-3alpha,7alpha,12alpha,26-tetraol + oxidized adrenodoxin + H2O

671957, 671685, 674402

-

1.14.15.15

5beta-cholestane-3alpha,7alpha,12alpha-triol + reduced adrenodoxin + O2 = 3alpha,7alpha,12alpha-trihydroxy-5beta-cholestanoic acid + oxidzed adrenodoxin + H2O

674402

-

1.14.15.15

5beta-cholestane-3alpha,7alpha,12alpha-triol + reduced adrenodoxin + O2 = 5beta-cholestane-3alpha,7alpha,12alpha,26-tetraol + oxidized adrenodoxin + H2O

674399, 674400

-

1.14.15.15

5beta-cholestane-3alpha,7alpha,12alpha-triol + reduced adrenodoxin + O2 = ?

439024, 439023, 439031, 439026

-

1.14.15.15

5beta-cholestane-3alpha,7alpha-diol + reduced adrenodoxin + O2 = 5beta-cholestane-3alpha,7alpha,26-triol + oxidized adrenodoxin + H2O

674399, 674400

-

1.14.15.15

7alpha-hydroxy-4-cholesten-3-one + reduced adrenodoxin + O2 = 7alpha,26-dihydroxy-4-cholesten-3-one + oxidized adrenodoxin + H2O

674399, 674400

-

1.14.15.15

cholesterol + reduced adrenodoxin + H+ + O2 = 26-hydroxycholesterol + oxidized adrenodoxin + H2O

674399, 674400

-

1.14.15.15

cholesterol + reduced adrenodoxin + O2 = 27-hydroxycholesterol + oxidized adrenodoxin + H2O

671957, 736561, 736710

-

1.14.15.4

11-deoxycorticosterone + reduced adrenodoxin + O2 = corticosterone + oxidized adrenodoxin + H2O

725981, 725828

-

1.14.15.4

18-hydroxycorticosterone + reduced adrenodoxin + O2 = aldosterone + oxidized adrenodoxin + H2O

725828

-

1.14.15.4

corticosterone + reduced adrenodoxin + O2 = 18-hydroxycorticosterone + oxidized adrenodoxin + H2O

725981, 725828

-

1.14.15.15

14 entries

1.14.15.4

3 entries

1.18.1.6

reduced adrenodoxin + NADP+ + H+ = oxidized adrenodoxin + NADPH

744400, 746398, 744908, 744909, 745425, 746501, 745575

-

In Vivo Product in Enzyme-catalyzed Reactions (1 result)

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Show Natural Product (1 entry)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.18.1.6

oxidized adrenodoxin + NADPH + H+ = reduced adrenodoxin + NADP+

0

-

Substrate in Enzyme-catalyzed Reactions (82 results)

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Show Substrate (82 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.14.14.25

cholesterol + reduced adrenodoxin + O2 = 24-hydroxycholesterol + oxidized adrenodoxin + H2O

676852, 675535

-

1.14.15.15

(24S)-3beta-hydroxy-24-methyl-5alpha-cholesta-8(14),22-dien-15-one + reduced adrenodoxin + H+ + O2 = ?

702407

-

1.14.15.15

(25R)-5beta-cholestane-3alpha,7alpha,12alpha,27-tetraol + reduced adrenodoxin + O2 = 3alpha,7alpha,12alpha-trihydroxy-5beta-cholestanoic acid + oxidized adrenodoxin + H2O

674402

-

1.14.15.15

1alpha-hydroxyvitamin D3 + reduced adrenodoxin + O2 = 1alpha,25-dihydroxyvitamin D3 + oxidized adrenodoxin + H2O

439034, 439035, 439036

-

1.14.15.15

3alpha,7alpha,12alpha-trihydroxy-5beta-cholestan-27-al + reduced adrenodoxin + O2 = 3alpha,7alpha,12alpha-trihydroxy-5beta-cholestanoic acid + oxidized adrenodoxin + H2O

674402

-

1.14.15.15

3beta-hydroxy-5alpha-cholest-8(14)-en-15-one + reduced adrenodoxin + H+ + O2 = ?

702407

-

1.14.15.15

5-cholestene-3beta,7alpha-diol + reduced adrenodoxin + O2 = 5-cholestene-3alpha,7alpha,26-triol + oxidized adrenodoxin + H2O

674399, 674400

-

1.14.15.15

5beta-cholestane-3alpha,7alpha,12alpha,26-tetraol + reduced adrenodoxin + O2 = 3alpha,7alpha,12alpha-trihydroxy-5beta-cholestan-26-al + oxidized adrenodoxin + H2O

389410, 288209, 288207

-

1.14.15.15

5beta-cholestane-3alpha,7alpha,12alpha,27-tetraol + reduced adrenodoxin + O2 = 3alpha,7alpha,12alpha-trihydroxy-5beta-cholestane-27-oic acid + oxidized adrenodoxin + H2O

671685

-

1.14.15.15

5beta-cholestane-3alpha,7alpha,12alpha-triol + reduced adrenodoxin + H+ + O2 = (25R)-5beta-cholestane-3alpha,7alpha,12alpha,26-tetraol + oxidized adrenodoxin + H2O

705935

-

1.14.15.15

5beta-cholestane-3alpha,7alpha,12alpha-triol + reduced adrenodoxin + O2 = (25R)-5beta-cholestane-3alpha,7alpha,12alpha,26-tetraol + oxidized adrenodoxin + H2O

671957, 671685, 674402

-

1.14.15.15

5beta-cholestane-3alpha,7alpha,12alpha-triol + reduced adrenodoxin + O2 = (25R)-5beta-cholestane-3alpha,7alpha,12alpha,27-tetraol + oxidized adrenodoxin + H2O

671957

-

1.14.15.15

5beta-cholestane-3alpha,7alpha,12alpha-triol + reduced adrenodoxin + O2 = 3alpha,7alpha,12alpha-trihydroxy-5beta-cholestanoic acid + oxidzed adrenodoxin + H2O

674402

-

1.14.15.15

5beta-cholestane-3alpha,7alpha,12alpha-triol + reduced adrenodoxin + O2 = 5beta-cholestane-3alpha,7alpha,12alpha,26-tetraol + oxidized adrenodoxin + H2O

674399, 674400

-

1.14.15.15

5beta-cholestane-3alpha,7alpha,12alpha-triol + reduced adrenodoxin + O2 = 5beta-cholestane-3alpha,7alpha,12alpha,27-tetrol + oxidized adrenodoxin + H2O

439023, 439026, 439028, 439029, 439030, 439031, 439034, 439035, 439036, 439024, 439025, 439032

-

1.14.15.15

5beta-cholestane-3alpha,7alpha,12alpha-triol + reduced adrenodoxin + O2 = ?

439024, 439023, 439031, 439026

-

1.14.15.15

5beta-cholestane-3alpha,7alpha-diol + reduced adrenodoxin + O2 = 5beta-cholestane-3alpha,7alpha,26-triol + oxidized adrenodoxin + H2O

674399, 674400

-

1.14.15.15

5beta-cholestane-3alpha,7alpha-diol + reduced adrenodoxin + O2 = ?

439029, 439030, 439034

-

1.14.15.15

5beta-cholestane-3alpha-ol + reduced adrenodoxin + O2 = ?

439029

-

1.14.15.15

7alpha-hydroxy-4-cholesten-3-one + reduced adrenodoxin + O2 = 7alpha,26-dihydroxy-4-cholesten-3-one + oxidized adrenodoxin + H2O

674399, 674400

-

1.14.15.15

beta-sitosterol + reduced adrenodoxin + O2 = 26-hydroxy-beta-sitosterol + 29-hydroxy-beta-sitosterol + oxidized adrenodoxin + H2O

735739

-

1.14.15.15

cholesterol + reduced adrenodoxin + H+ + O2 = 26-hydroxycholesterol + oxidized adrenodoxin + H2O

674399, 674400

-

1.14.15.15

cholesterol + reduced adrenodoxin + O2 = 24-hydroxycholesterol + oxidized adrenodoxin + H2O

671685

-

1.14.15.15

cholesterol + reduced adrenodoxin + O2 = 25-hydroxycholesterol + oxidized adrenodoxin + H2O

671685

-

1.14.15.15

cholesterol + reduced adrenodoxin + O2 = 26-hydroxycholesterol + oxidized adrenodoxin + H2O

735739

-

1.14.15.15

cholesterol + reduced adrenodoxin + O2 = 27-hydroxycholesterol + oxidized adrenodoxin + H2O

671957, 671685, 736561, 736710

-

1.14.15.15

cholesterol + reduced adrenodoxin + O2 = ?

439030

-

1.14.15.15

ergosterol + reduced adrenodoxin + O2 = 24-hydroxyergosterol + 26-hydroxyergosterol + 28-hydroxyergosterol + oxidized adrenodoxin + H2O

735739

-

1.14.15.15

27 entries

1.14.15.18

24,25-dihydroxycholecalciferol + reduced adrenodoxin + O2 = 1alpha,24,25-trihydroxycholecalciferol + oxidized adrenodoxin + H2O

440127, 440131

-

1.14.15.4

11-deoxycorticosterone + reduced adrenodoxin + O2 = corticosterone + oxidized adrenodoxin + H2O

725981, 725828

-

1.14.15.4

11-deoxycortisol + reduced adrenodoxin + O2 = cortisol + oxidized adrenodoxin + H2O

725981

-

1.14.15.4

18-hydroxycorticosterone + reduced adrenodoxin + O2 = aldosterone + oxidized adrenodoxin + H2O

725828

-

1.14.15.4

a steroid + reduced adrenodoxin + O2 = an 11beta-hydroxysteroid + oxidized adrenodoxin + H2O

724701

-

1.14.15.4

androstendione + reduced adrenodoxin + O2 = ? + oxidized adrenodoxin + H2O

725981

-

1.14.15.4

corticosterone + reduced adrenodoxin + O2 = 18-hydroxycorticosterone + oxidized adrenodoxin + H2O

725981, 725828

-

1.14.15.4

progesterone + reduced adrenodoxin + O2 = 11beta-hydroxyprogesterone + oxidized adrenodoxin + H2O

725981

-

1.14.15.4

testosterone + reduced adrenodoxin + O2 = 11-hydroxytestosterone + oxidized adrenodoxin + H2O

725981

-

1.14.15.6

(20S)-22-thiacholesterol + reduced adrenodoxin + O2 = (20S,22R)-22-thiacholesterol S-oxide + (20S,22S)-22-thiacholesterol S-oxide

285428

-

1.14.15.6

17,20-dihydroxyvitamin D2 + reduced adrenodoxin + O2 = 17,20,24-trihydroxyvitamin D2 + oxidized adrenodoxin + O2

703418

-

1.14.15.6

20,23-dihydroxyvitamin D3 + reduced adrenodoxin + O2 = 17,20,23-trihydroxyvitamin D3 + oxidized adrenodoxin + H2O

704039

-

1.14.15.6

20,23-dihydroxyvitamin D3 + reduced adrenodoxin + O2 = 17alpha,20,23-trihydroxyvitamin D3 + oxidized adrenodoxin + H2O

703625

-

1.14.15.6

20-hydroxyvitamin D2 + reduced adrenodoxin + O2 = 17,20,24-trihydroxyvitamin D2 + oxidized adrenodoxin + O2

703418

-

1.14.15.6

20-hydroxyvitamin D3 + reduced adrenodoxin + O2 = 20,23-dihydroxyvitamin D3 + 17alpha,20,23-trihydroxyvitamin D3 + oxidized adrenodoxin + H2O

703625

-

1.14.15.6

20-hydroxyvitamin D3 + reduced adrenodoxin + O2 = 20,23-dihydroxyvitamin D3 + oxidized adrenodoxin + H2O

704039

-

1.14.15.6

20alpha, 22(R)-dihydroxycholesterol + reduced adrenodoxin + O2 = ? + oxidized adrenodoxin + H2O

657647

-

1.14.15.6

20alpha-hydroxycholesterol + reduced adrenodoxin + O2 = pregnenolone + 4-methylpentanal + oxidized adrenodoxin + H2O

285418, 657647

-

1.14.15.6

22(R)-hydroxycholesterol + reduced adrenodoxin + O2 = ? + oxidized adrenodoxin + H2O

657647, 702403

-

1.14.15.6

22(R)-hydroxycholesterol + reduced adrenodoxin + O2 = pregnenolone + oxidized adrenodoxin + H2O

658508

-

1.14.15.6

25-hydroxycholesterol + reduced adrenodoxin + O2 = pregnenolone + oxidized adrenodoxin + H2O

658811

-

1.14.15.6

cholesterol + reduced adrenodoxin + O2 + H+ = pregnenolone + 4-methylpentanal + oxidized adrenodoxin + H2O

285412, 285413

-

1.14.15.6

cholesterol + reduced adrenodoxin + O2 = ? + oxidized adrenodoxin + H2O

657647

-

1.14.15.6

cholesterol + reduced adrenodoxin + O2 = pregnenolone + 4-methylpentanal + oxidized adrenodoxin + H2O

659756, 285412, 285413, 285414, 285415, 285419, 285420, 285423, 285424, 285426, 285427, 285428, 285429, 285430, 285431, 285432, 285433, 703418, 703876, 704039, 703100, 702781, 285422, 285421, 285425, 285416, 285418, 285417

-

1.14.15.6

cholesterol sulfate + reduced adrenodoxin + O2 = pregnenolone sulfate + 17-hydroxy-pregnenolone + dehydroisoandrosterone sulfate + oxidized adrenodoxin + H2O

285426

-

1.14.15.6

vitamin D2 + reduced adrenodoxin + O2 = 17,20,24-trihydroxyvitamin D2 + oxidized adrenodoxin + H2O

703418

-

1.14.15.6

vitamin D3 + reduced adrenodoxin + O2 = 20-hydroxyvitamin D3 + oxidized adrenodoxin + H2O

703625, 704039

-

1.14.15.8

11-deoxycorticosterone + reduced adrenodoxin + O2 = 15beta-hydroxy-11-deoxycorticosterone + 7beta,15beta-dihydroxy-11-deoxycorticosterone + oxidized adrenodoxin + H2O

744148

-

1.14.15.8

11-deoxycorticosterone + reduced adrenodoxin + O2 = 15beta-hydroxy-11-deoxycorticosterone + oxidized adrenodoxin + H2O

725584, 697323, 695980

-

1.14.15.8

11-deoxycortisol + reduced adrenodoxin + O2 = 15beta-15,17,21-trihydroxypregn-4-ene-3,20-dione + oxidized adrenodoxin + H2O

693956

-

1.14.15.8

11-deoxycortisol + reduced adrenodoxin + O2 = 15beta-hydroxy-11-deoxycortisol + oxidized adrenodoxin + H2O

744148

-

1.14.15.8

11beta-hydroxy-4-androstene-3,17-dione + reduced adrenodoxin + O2 = ? + oxidized adrenodoxin + H2O

744148

-

1.14.15.8

17alpha-methyltestosterone + reduced adrenodoxin + O2 = ? + oxidized adrenodoxin + H2O

744148

-

1.14.15.8

19-nortestosterone + reduced adrenodoxin + O2 = ? + oxidized adrenodoxin + H2O

744148

-

1.14.15.8

4-androstene-3,17-dione + reduced adrenodoxin + O2 = 15beta-hydroxyandrostene-3,17-dione + oxidized adrenodoxin + H2O

744148

-

1.14.15.8

abietic acid + reduced adrenodoxin + O2 = 12-hydroxyabietic acid + oxidized adrenodoxin + H2O

725584

-

1.14.15.8

abietic acid + reduced adrenodoxin + O2 = ? + oxidized adrenodoxin + H2O

744706

-

1.14.15.8

corticosterone + reduced adrenodoxin + O2 = 15beta-hydroxycorticosterone + oxidized adrenodoxin + H2O

744148

-

1.14.15.8

cortisone + reduced adrenodoxin + O2 = 15beta-hydroxycortisone + oxidized adrenodoxin + H2O

744148

-

1.14.15.8

dehydroabietic acid + reduced adrenodoxin + O2 = ? + oxidized adrenodoxin + H2O

744706

-

1.14.15.8

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

745699

-

1.14.15.8

dexamethasone + reduced adrenodoxin + O2 = ? + oxidized adrenodoxin + H2O

744148, 745699

-

1.14.15.8

digitoxigenin + reduced adrenodoxin + O2 = ? + oxidized adrenodoxin + H2O

745699

-

1.14.15.8

imipramine + reduced adrenodoxin + O2 = desipramine + oxidized adrenodoxin + H2O

725584

-

1.14.15.8

isopimaric acid + reduced adrenodoxin + O2 = ? + oxidized adrenodoxin + H2O

744706

-

1.14.15.8

prednisolone + reduced adrenodoxin + O2 = ? + oxidized adrenodoxin + H2O

744148

-

1.14.15.8

prednisone + reduced adrenodoxin + O2 = ? + oxidized adrenodoxin + H2O

744148, 745699

-

1.14.15.8

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

745699

-

1.14.15.8

progesterone + reduced adrenodoxin + O2 = 15beta-hydroxy-progesterone + 11alpha-hydroxy-progesterone + oxidized adrenodoxin + H2O

746507

-

1.14.15.8

progesterone + reduced adrenodoxin + O2 = 15beta-hydroxy-progesterone + oxidized adrenodoxin + H2O

697323

-

1.14.15.8

progesterone + reduced adrenodoxin + O2 = 15beta-hydroxyprogesterone + oxidized adrenodoxin + H2O

693956, 695981

-

1.14.15.8

testosterone + reduced adrenodoxin + O2 = 15beta-hydroxytestosterone + oxidized adrenodoxin + H2O

744148, 696142

-

1.18.1.6

reduced adrenodoxin + NADP = oxidized adrenodoxin + NADPH + H+

719475

-

1.18.1.6

reduced adrenodoxin + NADP+ + H+ = oxidized adrenodoxin + NADPH

744400, 746398, 744908, 744909, 745425, 746501, 745575

-

1.14.15.4

8 entries

1.14.15.6

18 entries

1.14.15.8

25 entries

1.18.1.6

2 entries

Product in Enzyme-catalyzed Reactions (4 results)

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Show Product (4 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.14.15.4

11-deoxycortisol + oxidized adrenodoxin + H2O = cortisol + reduced adrenodoxin + O2

0

-

1.14.15.4

deoxycorticosterone + oxidized adrenodoxin + H2O = corticosterone + reduced adrenodoxin + O2

0

-

1.18.1.6

oxidized adrenodoxin + NADH + H+ = reduced adrenodoxin + NAD+

0

-

1.18.1.6

oxidized adrenodoxin + NADPH + H+ = reduced adrenodoxin + NADP+

0

-

1.14.15.4

2 entries

1.18.1.6

2 entries

Enzyme Kinetic Parameters

K_M Value (3 results)

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Show KM Value (3 entries)

EC NUMBER

KM VALUE [MM]

KM VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

1.14.15.6

0.0004

-

free

285412

1.14.15.6

0.00056

-

+/-0.00004, complex between adrenodoxin and adrenodoxin reductase

285412

1.14.15.6

0.0012

-

-

285413

1.14.15.6

3 entries

References & Links

Literature References (83)

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Show Reference (83 entries)

BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

PAGES

285412

6766943

Mitochondrial cytochrome P-450sec. Mechanism of electron transport by adrenodoxin

1980

Hanukoglu, I.; Jefcoate, C.R.

J. Biol. Chem.

255

3057-3061

285413

7217084

Adrenal mitochondrial cytochrome P-450scc. Cholesterol and adrenodoxin interactions at equilibrium and during turnover

1981

Hanukoglu, I.; Spitsberg, V.; Bumpus, J.A.; Dus, K.M.; Jefcoate, C.R.

J. Biol. Chem.

256

4321-4328

285414

6783659

Mechanisms of ionic activation of adrenal mitochondrial cytochromes P-450scc and P-45011beta

1981

Hanukoglu, I.; Privalle, C.T.; Jefcoate, C.R.

J. Biol. Chem.

256

4329-4335

285415

184090

Purification and characterization of adrenal cortex mitochondrial cytochrome P-450 specific for cholesterol side chain cleavage activity

1976

Wang, H.P.; Kimura, T.

J. Biol. Chem.

251

6068-6074

285416

444237

Binding of Triton X-100 to purified cytochrome P-450scc and enhancement of the cholesterol side chain cleavage activity

1979

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

Biochem. Biophys. Res. Commun.

87

524-531

285417

6723652

The catalytic cycle of cytochrome P-450scc and intermediates in the conversion of cholesterol to pregnenolone

1984

Hume, R.; Kelly, R.W.; Taylor, P.L.; Boyd, G.S.

Eur. J. Biochem.

140

583-591

285418

4723901

Cytochrome P-450 from bovine adrenocortical mitochondria: an enzyme for the side chain cleavage of cholesterol. I. Purification and properties

1973

Shikita, M.; Hall, P.F.

J. Biol. Chem.

248

5598-5604

285419

1131251

Purification of cytochrome P-450 from bovine adrenocortical mitochondria by an aniline-Sepharose and the properties

1975

Takemori, S.; Sukara, K.; Hashimoto, K.; Hashimoto, M.; Sato, H.; Gomi, T.; Katagiri, M.

Biochem. Biophys. Res. Commun.

63

588-593

285420

2605191

Cholesterol metabolism by purified cytochrome P-450scc is highly stimulated by octyl glucoside and stearic acid exclusively in large unilamellar phospholipid vesicles

1989

Dhariwal, M.S.; Jefcoate, C.R.

Biochemistry

28

8397-8402

285421

4019455

Cytochrome P-450scc-adrenodoxin interactions. Ionic effects on binding, and regulation of cytochrome reduction by bound steroid substrates

1985

Lambeth, J.D.; Kriengsiri, S.

J. Biol. Chem.

260

8810-8816

285422

3968069

Competitive inhibition of cytochrome P-450scc by (22R)- and (22S)-22-aminocholesterol. Side-chain stereochemical requirements for C-22 amine coordination to the active-site heme

1985

Nagahisa, A.; Foo, T.; Gut, M.; Orme-Johnson, W.H.

J. Biol. Chem.

260

846-851

285423

6244284

Purification and characterization of mitochondrial cytochrome P-450 associated with cholesterol side chain cleavage from bovine corpus luteum

1980

Kashiwagi, K.; Dafeldecker, W.P.; Salhanick, H.A.

J. Biol. Chem.

255

2606-2611

285424

6688621

Active site-directed inhibitors of cytochrome P-450scc. Structural and mechanistic implications of a side chain-substituted series of amino-steroids

1983

Sheets, J.J.; Vickery, L.E.

J. Biol. Chem.

258

11446-11452

285425

6822531

C-22-Substituted steroid derivatives as substrate analogues and inhibitors of cytochrome P-450scc

1983

Sheets, J.J.; Vickery, L.E.

J. Biol. Chem.

258

1720-1725

285426

6572949

Modulation of the kinetics of cholesterol side-chain cleavage by an activator and by an inhibitor isolated from the cytosol of the cortex of bovine adrenals

1983

Warne, P.A.; Greenfield, N.J.; Lieberman, S.

Proc. Natl. Acad. Sci. USA

80

1877-1881

285427

4723902

Cytochrome P-450 from bovine adrenocortical mitochondria: an enzyme for the side chain cleavage of cholesterol. II. Subunit structure

1973

Shikita, M.; Hall, P.F.

J. Biol. Chem.

248

5605-5609

285428

7599132

Cytochrome P-450scc-mediated oxidation of (20S)-22-thiacholesterol: Characterization of mechanism-based inhibition

1995

Miao, E.; Joardar, S.; Zuo, C.; Cloutier, N.J.; Nagahisa, A.; Byon, C.; Wilson, S.R.; Orme-Johnson, W.H.

Biochemistry

34

8415-8421

285429

8662703

alpha-Branched 1,2-diacyl phosphatidylcholines as effectors of activity of cytochrome P450SCC (CYP11A1). Modeling the structure of the fatty acyl chain region of cardiolipin

1996

Schwarz, D.; Kisselev, P.; Wessel, R.; Jueptner, O.; Schmid, R.D.

J. Biol. Chem.

271

12840-12846

285430

11173513

Site-directed mutagenesis of cytochrome P450scc (CYP11A1). Effect of lysine residue substitution on its structural and functional properties

2000

Lepesheva, G.I.; Azeva, T.N.; Strushkevich, N.V.; Gilep, A.A.; Usanov, S.A.

Biochemistry (Moscow)

65

1409-1418

285431

10924360

The use of the novel substrate-heme complex approach in the derivation of a representation of the active site of the enzyme cholesterol side chain cleavage

2000

Ahmed, S.

Biochem. Biophys. Res. Commun.

274

821-824

285432

8431464

Substrate-binding region of cytochrome P-450scc (P-450 XIA1). Identification and primary structure of the cholesterol binding region in cytochrome P-450scc

1993

Tsujita, M.; Ichikawa, Y.

Biochim. Biophys. Acta

1161

124-130

285433

12081479

Probing the interaction of bovine cytochrome P450scc (CYP11A1) with adrenodoxin: evaluating site-directed mutations by molecular modeling

2002

Usanov, S.A.; Graham, S.E.; Lepesheva, G.I.; Azeva, T.N.; Strushkevich, N.V.; Gilep, A.A.; Estabrook, R.W.; Peterson, J.

Biochemistry

41

8310-8320

288207

5914340

The oxidation of 5-beta-cholestane-3-alpha, 7-alpha, 12-alpha, 26-tetraol to 5-beta-cholestane-3-alpha, 7-alpha, 12-alpha-triol-26-oic acid via 5-beta-cholestane-3-alpha, 7-alpha, 12-alpha-triol-26-al by rat liver

1966

Masui, T.; Herman, R.; Staple, E.

Biochim. Biophys. Acta

117

266-268

288209

5723340

Separation of 5-beta-cholestane-3-alpha,7-alpha,12-alpha,26-tetrol oxidoreductase, and acetaldehyde-NAD oxidoreductase from the soluble fraction of rat liver by gel filtration

1968

Okuda, K.; Takigawa, N.

Biochem. Biophys. Res. Commun.

33

788-793

389410

6338006

Physiological function and kinetic mechanism of human liver alcohol dehydrogenase as 5beta-cholestane-3alpha,7alpha,12alpha,26-tetrol dehydrogenase

1983

Okuda, A.; Okuda, K.

J. Biol. Chem.

258

2899-2905

439023

4388637

Oxidation of 5-beta-cholestane-3alpha,7alpha, 12alpha-triol by rat-liver mitochondria

1968

Okuda, K.; Hoshita, N.

Biochim. Biophys. Acta

164

381-388

439024

4150013

Enzymatic characteristics of CO-sensitive 26-hydroxylase system for 5beta-cholestane-3alpha,7alpha 12alpha-triol in rat-liver mitochondria and its intramitochondrial localization

1973

Taniguchi, S.; Hoshita, N.; Okuda, K.

Eur. J. Biochem.

40

607-617

439025

843347

Photochemical action spectrum of the co-inhibited 5beta-cholestane-3alpha,7alpha,12alpha-triol 26-hydroxylase system

1977

Okuda, K.; Weber, P.; Ullrich, V.

Biochem. Biophys. Res. Commun.

74

1071-1076

439026

195887

Spectral evidence for a liver mitochondrial cytochrome P450 involved in bile acid metabolism

1977

Okuda, K.; Ruf, H.H.; Ullrich, V.

Hoppe-Seyler's Z. Physiol. Chem.

358

689-694

439028

271969

Hepatic mitochondrial cytochrome P-450: isolation and functional characterization

1977

Sato, R.; Atsuta, Y.; Imai, Y.; Taniguchi, S.; Okuda, K.

Proc. Natl. Acad. Sci. USA

74

5477-5481

439029

7077149

Partial purification and characterization of 5beta-cholestane-3alpha,7alpha,12alpha-triol and 5beta-cholestane-3alpha,7alpha-diol 27-monooxygenase

1982

Atsuta, Y.; Okuda, K.

J. Lipid Res.

23

345-351

439030

2848026

Purification and characterization of 5beta-cholestane-3alpha,7alpha,12alpha-triol 27-hydroxylase from female rat liver mitochondria

1988

Okuda, K.; Masumoto, O.; Ohyama, Y.

J. Biol. Chem.

263

18138-18142

439031

4026854

Evidence for peroxisomal hydroxylase activity in rat liver

1985

Thompson, S.L.; Krisans, S.K.

Biochem. Biophys. Res. Commun.

130

708-716

439032

6260795

25-Hydroxylation vitamin D3 and side chain hydroxylations of 5beta-cholestane-3alpha,7alpha,12 alpha-triol by purified rabbit and rat liver microsomal cytochromes P-450

1981

Hansson, R.; Holmberg, I.; Wikvall, K.

J. Biol. Chem.

256

4345-4349

439034

1880123

Multi-functional property of rat liver mitochondrial cytochrome P-450

1991

Ohyama, Y.; Masumoto, O.; Usui, E.; Okuda, K.

J. Biochem.

109

389-393

439035

2013339

Expression of rat liver vitamin D3 25-hydroxylase cDNA in Saccharomyces cerevisiae

1991

Akiyoshi-Shibata, M.; Usui, E.; Sakaki, T.; Yabusaki, Y.; Noshiro, M.; Okuda, K.; Ohkawa, H.

FEBS Lett.

280

367-370

439036

2253771

Unique property of liver mitochondrial P450 to catalyze the two physiologically important reactions involved in both cholesterol catabolism and vitamin D activation

1990

Usui, E.; Noshiro, M.; Ohyama, Y.; Okuda, K.

FEBS Lett.

274

175-177

440127

10092858

Enzymic properties of mouse 25-hydroxyvitamin D3 1alpha-hydroxylase expressed in Escherichia coli

1999

Sakaki, T.; Sawada, N.; Takeyama, K.i.; Kato, S.; Inouye, K.

Eur. J. Biochem.

259

731-738

440131

11686044

Enzymatic studies on the key enzymes of vitamin D metabolism; 1alpha-hydroxylase (CYP27B1) and 24-hydroxylase (CYP24)

2001

Inouye, K.; Sakaki, T.

Biotechnol. Annu. Rev.

7

179-194

657647

12392719

The effect of glycerol on cytochrome P450scc (CYP11A1) spin state, activity, and hydration

2002

Headlam, M.J.; Tuckey, R.C.

Arch. Biochem. Biophys.

407

95-102

658508

12823901

Formation and functioning of fused cholesterol side-chain cleavage enzymes

2003

Nazarov, P.A.; Drutsa, V.L.; Miller, W.L.; Shkumatov, V.M.; Luzikov, V.N.; Novikova, L.A.

DNA Cell Biol.

22

243-252

658811

12093115

The cDNA cloning and tissue expression of the cytochrome P450scc from Syrian hamster (Mesocricetus auratus)

2002

Vilchis, F.; Chavez, B.; Larrea, F.; Timossi, C.; Montiel, F.

Gen. Comp. Endocrinol.

126

279-286

659756

12911631

Cellular distribution and bioactivity of the key steroidogenic enzyme, cytochrome P450side chain cleavage, in sensory neural pathways

2003

Patte-Mensah, C.; Kappes, V.; Freund-Mercier, M.J.; Tsutsui, K.; Mensah-Nyagan, A.G.

J. Neurochem.

86

1233-1246

671685

10512735

Biochemical characterization of a truncated form of CYP27A purified from rabbit liver mitochondria

1999

Furster, C.; Bergman, T.; Wikvall, K.

Biochem. Biophys. Res. Commun.

263

663-666

671957

11412116

Putative helix F contributes to regioselectivity of hydroxylation in mitochondrial cytochrome P450 27A

2001

Pikuleva, I.A.; Puchkaev, A.; Bjoerkhem, I.

Biochemistry

40

7621-7629

674399

6423637

Hydroxylations in biosynthesis of bile acids. Isolation of a cytochrome P-450 from rabbit liver mitochondria catalyzing 26-hydroxylation of C27-steroids

1984

Wikvall, K.

J. Biol. Chem.

259

3800-3804

674400

2722778

Cloning, structure, and expression of the mitochondrial cytochrome P-450 sterol 26-hydroxylase, a bile acid biosynthetic enzyme

1989

Andemson, S.; Davis, D.L.; Dahlback, H.; Jornvall, H.; Russell, D.W.

J. Biol. Chem.

264

8222-8229

674402

-

Sterol 27-hydroxylase in bile acid biosynthesis. Mechanism of oxidation of 5beta-cholestane-3alpha,7alpha,12alpha,27-tetraol into 3alpha,7alpha,12alpha-trihydroxy-5beta-cholestanoic acid

1993

Holmberg-Betsholtz, I.; Lund, E.; Bjorkhem, I.; Wikvall, K.

J. Biol. Chem.

266

11079-11085

675535

16825952

Lovastatin modulates increased cholesterol and oxysterol levels and has a neuroprotective effect on rat hippocampal neurons after kainate injury

2006

He, X.; Jenner, A.M.; Ong, W.Y.; Farooqui, A.A.; Patel, S.C.

J. Neuropathol. Exp. Neurol.

65

652-663

676852

16505352

Brain cholesterol turnover required for geranylgeraniol production and learning in mice

2006

Kotti, T.J.; Ramirez, D.M.; Pfeiffer, B.E.; Huber, K.M.; Russell, D.W.

Proc. Natl. Acad. Sci. USA

103

3869-3874

693956

18830657

Molecular evolution of a steroid hydroxylating cytochrome P450 using a versatile steroid detection system for screening

2008

Virus, C.; Bernhardt, R.

Lipids

43

1133-1141

695980

10720486

Substrate binding to 15beta-hydroxylase (CYP106A2) probed by FT infrared spectroscopic studies of the iron ligand CO stretch vibration

2000

Simgen, B.; Contzen, J.; Schwarzer, R.; Bernhardt, R.; Jung, C.

Biochem. Biophys. Res. Commun.

269

737-742

695981

15178459

Identification of monohydroxy progesterones produced by CYP106A2 using comparative HPLC and electrospray ionisation collision-induced dissociation mass spectrometry

2004

Lisurek, M.; Kang, M.J.; Hartmann, R.W.; Bernhardt, R.

Biochem. Biophys. Res. Commun.

319

677-682

696142

17073788

Function and engineering of the 15beta-hydroxylase CYP106A2

2006

Virus, C.; Lisurek, M.; Simgen, B.; Hannemann, F.; Bernhardt, R.

Biochem. Soc. Trans.

34

1215-1218

697323

18481342

Theoretical and experimental evaluation of a CYP106A2 low homology model and production of mutants with changed activity and selectivity of hydroxylation

2008

Lisurek, M.; Simgen, B.; Antes, I.; Bernhardt, R.

Chembiochem

16

1439-1449

702403

18621100

Import of hybrid forms of CYP11A1 into yeast mitochondria

2008

Minenko, A.N.; Novikova, L.A.; Luzikov, V.N.; Kovaleva, I.E.

Biochim. Biophys. Acta

1780

1121-1130

702407

18603016

Metabolism of a novel side chain modified DELTA8(14)-15-ketosterol, a potential cholesterol lowering drug: 28-hydroxylation by CYP27A1

2008

Pettersson, H.; Norlin, M.; Andersson, U.; Pikuleva, I.; Bjoerkhem, I.; Misharin, A.; Wikvall, K.

Biochim. Biophys. Acta

1781

383-390

702781

18455917

Screen-printed electrodes based on carbon nanotubes and cytochrome P450scc for highly sensitive cholesterol biosensors

2008

Carrara, S.; Shumyantseva, V.V.; Archakov, A.I.; Samori, B.

Biosens. Bioelectron.

24

148-150

703100

18398688

Steroidogenic acute regulatory (StAR) protein and cholesterol side-chain cleavage (P450scc)-regulated steroidogenesis as an organ-specific molecular and cellular target for endocrine disrupting chemicals in fish

2008

Arukwe, A.

Cell Biol. Toxicol.

24

527-540

703418

19116262

Metabolism of vitamin d2 to 17,20,24-trihydroxyvitamin d2 by cytochrome p450scc (CYP11A1)

2009

Nguyen, M.N.; Slominski, A.; Li, W.; Ng, Y.R.; Tuckey, R.C.

Drug Metab. Dispos.

37

761-767

703625

18410379

Pathways and products for the metabolism of vitamin D3 by cytochrome P450scc

2008

Tuckey, R.C.; Li, W.; Zjawiony, J.K.; Zmijewski, M.A.; Nguyen, M.N.; Sweatman, T.; Miller, D.; Slominski, A.

FEBS J.

275

2585-2596

703876

19824542

Construction and characteristics of transgenic tobacco Nicotiana tabacum L. plants expressing CYP11A1 cDNA encoding cytochrome P450scc

2009

Spivak, S.; Berdichevets, I.; Iarmolinskiǐ, D.; Maneshina, T.; Shpakovskiǐ, G.; Kartel, N.

Genetika

45

1217-1224

704039

18573681

Kinetics of vitamin D3 metabolism by cytochrome P450scc (CYP11A1) in phospholipid vesicles and cyclodextrin

2008

Tuckey, R.C.; Nguyen, M.N.; Slominski, A.

Int. J. Biochem. Cell Biol.

40

2619-2626

705935

19665519

Expression of sterol 27-hydroxylase in glial cells and its regulation by liver X receptor signaling

2009

Gilardi, F.; Viviani, B.; Galmozzi, A.; Boraso, M.; Bartesaghi, S.; Torri, A.; Caruso, D.; Crestani, M.; Marinovich, M.; de Fabiani, E.

Neuroscience

164

530-540

719475

2294024

A negative cooperativity between NADPH and adrenodoxin on binding to NADPH:adrenodoxin reductase

1990

Cenas, N.; Marcinkeviciene, J.; Kulys, J.; Usanov, S.

FEBS Lett.

259

338-340

724701

22331364

Very-low-density lipoprotein mediates transcriptional regulation of aldosterone synthase in human adrenocortical cells through multiple signaling pathways

2012

Saha, S.; Bornstein, S.R.; Graessler, J.; Kopprasch, S.

Cell Tissue Res.

348

71-80

725584

22426093

Autodisplay of functional CYP106A2 in Escherichia coli

2012

Schumacher, S.D.; Hannemann, F.; Teese, M.G.; Bernhardt, R.; Jose, J.

J. Biotechnol.

161

104-112

725828

22446688

Human aldosterone synthase: recombinant expression in E. coli and purification enables a detailed biochemical analysis of the protein on the molecular level

2012

Hobler, A.; Kagawa, N.; Hutter, M.C.; Hartmann, M.F.; Wudy, S.A.; Hannemann, F.; Bernhardt, R.

J. Steroid Biochem. Mol. Biol.

132

57-65

725981

23322723

Structural insights into aldosterone synthase substrate specificity and targeted inhibition

2013

Strushkevich, N.; Gilep, A.A.; Shen, L.; Arrowsmith, C.H.; Edwards, A.M.; Usanov, S.A.; Park, H.W.

Mol. Endocrinol.

27

315-324

735739

26891232

Human CYP27A1 catalyzes hydroxylation of beta-sitosterol and ergosterol

2016

Ehrhardt, M.; Gerber, A.; Zapp, J.; Hannemann, F.; Bernhardt, R.

Biol. Chem.

397

513-518

736561

24096962

Evidence for a role of sterol 27-hydroxylase in glucocorticoid metabolism in vivo

2013

Voegeli, I.; Jung, H.H.; Dick, B.; Erickson, S.K.; Escher, R.; Funder, J.W.; Frey, F.J.; Escher, G.

J. Endocrinol.

219

119-129

736710

25649950

Identification and analysis of CYP7A1, CYP17A1, CYP20A1, CYP27A1 and CYP51A1 in cynomolgus macaques

2014

Uno, Y.; Hosaka, S.; Yamazaki, H.

J. Vet. Med. Sci.

76

1647-1650

744148

25904128

Comparison of CYP106A1 and CYP106A2 from Bacillus megaterium - identification of a novel 11-oxidase activity

2015

Kiss, F.M.; Schmitz, D.; Zapp, J.; Dier, T.K.; Volmer, D.A.; Bernhardt, R.

Appl. Microbiol. Biotechnol.

99

8495-8514

744400

25712867

Sensitivity to anti-Fas is independent of increased cathepsin D activity and adrenodoxin reductase expression occurring in NOS-3 overexpressing HepG2 cells

2015

Linares, C.I.; Ferrin, G.; Aguilar-Melero, P.; Gonzalez-Rubio, S.; Rodriguez-Peralvarez, M.; Sanchez-Arago, M.; Chicano-Galvez, E.; Cuezva, J.M.; Montero-Alvarez, J.L.; Muntane, J.; de la Mata, M.

Biochim. Biophys. Acta

1853

1182-1194

744706

26864272

Crystal structure of CYP106A2 in substrate-free and substrate-bound form

2016

Janocha, S.; Carius, Y.; Hutter, M.; Lancaster, C.R.; Bernhardt, R.

ChemBioChem

17

852-860

744908

27878817

Structural characterization of CYP260A1 from Sorangium cellulosum to investigate the 1alpha-hydroxylation of a mineralocorticoid

2016

Khatri, Y.; Carius, Y.; Ringle, M.; Lancaster, C.R.; Bernhardt, R.

FEBS Lett.

590

4638-4648

744909

28281299

Investigating the effect of available redox protein ratios for the conversion of a steroid by a myxobacterial CYP260A1

2017

Khatri, Y.; Schifrin, A.; Bernhardt, R.

FEBS Lett.

591

1126-1140

745425

28043840

Characterization of cytochrome P450 CYP109E1 from Bacillus megaterium as a novel vitamin D3 hydroxylase

2017

Abdulmughni, A.; Jozwik, I.K.; Putkaradze, N.; Brill, E.; Zapp, J.; Thunnissen, A.W.; Hannemann, F.; Bernhardt, R.

J. Biotechnol.

243

38-47

745575

29177972

Conservation of the enzyme-coenzyme interfaces in FAD and NADP binding adrenodoxin reductase - a ubiquitous enzyme

2017

Hanukoglu, I.

J. Mol. Evol.

85

205-218

745699

24903845

Steroid conversion with CYP106A2 - production of pharmaceutically interesting DHEA metabolites

2014

Schmitz, D.; Zapp, J.; Bernhardt, R.

Microb. Cell Fact.

13

81

746398

28905435

Isatin-induced increase in the affinity of human ferrochelatase and adrenodoxin reductase interaction

2017

Ershov, P.; Mezentsev, Y.; Gilep, A.; Usanov, S.; Buneeva, O.; Medvedev, A.; Ivanov, A.

Protein Sci.

26

2458-2462

746501

28458234

Raman and infrared spectroscopic evidence for the structural changes of the 2Fe2S cluster and its environment during the interaction of adrenodoxin and adrenodoxin reductase

2017

Khalil, M.; Bernhardt, R.; Hellwig, P.

Spectrochim. Acta A. Mol. Biomol. Spectrosc.

183

298-305

746507

28163026

Engineering of CYP106A2 for steroid 9alpha- and 6beta-hydroxylation

2017

Nikolaus, J.; Nguyen, K.T.; Virus, C.; Riehm, J.L.; Hutter, M.; Bernhardt, R.

Steroids

120

41-48

Links to other databases for reduced adrenodoxin

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