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Ligand 7alpha-hydroxycholest-4-en-3-one

Basic Ligand Information

Molecular Structure

Show all BRENDA pathways known for 7alpha-hydroxycholest-4-en-3-one

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Roles as Enzyme Ligand

In Vivo Substrate in Enzyme-catalyzed Reactions (3 results)

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Show Natural Substrate (3 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.14.14.139

7alpha-hydroxycholest-4-en-3-one + NADPH + H+ + O2 = 7alpha,12alpha-dihydroxycholest-4-en-3-one + NADP+ + H2O

658237, 659123

-

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

-

1.3.1.3

DELTA4-cholesten-7alpha-ol-3-one + NADPH + H+ = 5beta-cholestan-7alpha-ol-3-one + NADP+

724713

-

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

1.1.1.181

cholest-5-ene-3beta,7alpha-diol + NAD+ = 7alpha-hydroxycholest-4-en-3-one + NADH

286129

-

Substrate in Enzyme-catalyzed Reactions (9 results)

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Show Substrate (9 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.14.14.139

7alpha-hydroxycholest-4-en-3-one + NADH + H+ + O2 = 7alpha,12alpha-dihydroxycholest-4-en-3-one + NAD+ + H2O

660512

-

1.14.14.139

7alpha-hydroxycholest-4-en-3-one + NADPH + H+ + O2 = 7alpha,12alpha-dihydroxycholest-4-en-3-one + NADP+ + H2O

659131, 658237, 658153, 659116, 659123, 660512

-

1.14.14.139

2 entries

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

-

1.14.15.29

7alpha-hydroxycholest-4-en-3-one + 6 reduced ferredoxin [iron-sulfur] cluster + 6 H+ + 3 O2 = (25S)-7alphahydroxy-3-oxocholest-4-en-26-oate + 6 oxidized ferredoxin [iron-sulfur] cluster + 4 H2O

744344

-

1.3.1.3

4-cholesten-7alpha-ol-3-one + NADPH + H+ = ?

726492

-

1.3.1.3

7alpha-hydroxy-4-cholesten-3-one + NADPH + H+ = 7alpha-hydroxy-5beta-cholestan-3-one + NADP+

390591

-

1.3.1.3

7alpha-hydroxy-4-cholesten-3-one + NADPH + H+ = ?

702225

-

1.3.1.3

7alpha-hydroxy-4-cholesten-3-one + NADPH = (5beta,7alpha)-7-hydroxycholestan-3-one + NADP+

685271

-

1.3.1.3

DELTA4-cholesten-7alpha-ol-3-one + NADPH + H+ = 5beta-cholestan-7alpha-ol-3-one + NADP+

724713

-

1.3.1.3

5 entries

Product in Enzyme-catalyzed Reactions (3 results)

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Show Product (3 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.1.1.145

7alpha-hydroxycholesterol + NAD+ = 7alpha-hydroxy-4-cholesten-3-one + NADH

0

-

1.1.1.181

cholest-5-ene-3beta,7alpha-diol + NAD+ = 7alpha-hydroxycholest-4-en-3-one + NADH

286129

-

1.1.3.6

7alpha-hydroxy-cholesterol + O2 = 7alpha-hydroxy-cholest-4-en-3-one + H2O2

0

-

Enzyme Kinetic Parameters

k_cat Value (Turnover Number) (2 results)

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Show Turnover Number (2 entries)

EC NUMBER

TURNOVER NUMBER [1/S]

TURNOVER NUMBER MAXIMUM [1/S]

COMMENTARY

LITERATURE

1.3.1.3

0.01

-

-

390591

1.3.1.3

0.033

-

pH 6.0, 37°C

726492

1.3.1.3

2 entries

K_M Value (5 results)

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Show KM Value (5 entries)

EC NUMBER

KM VALUE [MM]

KM VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

1.14.14.139

0.027

-

-

659116

1.14.15.29

0.0041

-

wild-type, pH 7.4, temperature not specified in the publication

744344

1.14.15.29

0.0051

-

mutant Y87W, pH 7.4, temperature not specified in the publication

744344

1.3.1.3

0.0008

-

pH 6.0, 37°C

726492

1.3.1.3

0.0091

-

-

390591

1.14.15.29

2 entries

1.3.1.3

2 entries

References & Links

Literature References (15)

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Show Reference (15 entries)

BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

PAGES

286129

6937465

Purification and properties of a 3beta-hydroxy-DELTA5-C27-steroid oxidoreductase from rabbit liver microsomes

1981

Wikvall, K.

J. Biol. Chem.

256

3376-3380

390591

6736016

Purification and characterization of DELTA 4-3-ketosteroid 5beta-reductase

1984

Okuda, A.; Okuda, K.

J. Biol. Chem.

259

7519-7524

658153

9461256

Rabbit liver contains one major sterol 12alpha-hydroxylase with broad substrate specificity

1998

Andersson, U.; Eggertsen, G.; Bjorkhem, I.

Biochim. Biophys. Acta

1389

150-154

658237

3149485

Effect of streptozotocin-induced diabetes on the activity of 7alpha-hydroxy-4-cholesten-3-one-specific 12alpha-hydroxylase in rats

1988

Kimura, K.; Ogura, M.

Biol. Chem. Hoppe-Seyler

369

1117-1120

659116

6806291

Purification and characterization of 7alpha-hydroxy-4-cholesten-3-one 12alpha-monooxygenase

1982

Murakami, K.; Okada, Y.; Okuda, K.

J. Biol. Chem.

257

8030-8035

659123

1400444

Purification and characterization of 7alpha-hydroxy-4-cholesten-3-one 12alpha-hydroxylase

1992

Ishida, H.; Noshiro, M.; Okuda, K.; Coon, M.J.

J. Biol. Chem.

267

21319-21323

659131

8943286

Molecular cloning and expression of rabbit sterol 12alpha-hydroxylase

1996

Eggertsen, G.; Olin, M.; Andersson, U.; Ishida, H.; Kubota, S.; Hellman, U.; Okuda, K.I.; Bjorkhem, I.

J. Biol. Chem.

271

32269-32275

660512

3939046

Assays for cholesterol 7alpha-hydroxylase and 12alpha-hydroxylase using high performance liquid chromatography

1985

Noshiro, M.; Ishida, H.; Hayashi, S.; Okuda, K.

Steroids

45

539-550

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

685271

18624455

The crystal structure of human DELTA4-3-ketosteroid 5beta-reductase defines the functional role of the residues of the catalytic tetrad in the steroid double bond reduction mechanism

2008

Faucher, F.; Cantin, L.; Luu-The, V.; Labrie, F.; Breton, R.

Biochemistry

47

8261-8270

702225

19075558

Crystal structures of human Delta4-3-ketosteroid 5beta-reductase (AKR1D1) reveal the presence of an alternative binding site responsible for substrate inhibition

2008

Faucher, F.; Cantin, L.; Luu-The, V.; Labrie, F.; Breton, R.

Biochemistry

47

13537-13546

724713

21185810

The effect of disease associated point mutations on 5beta-reductase (AKR1D1) enzyme function

2011

Mindnich, R.; Drury, J.E.; Penning, T.M.

Chem. Biol. Interact.

191

250-254

726492

21255593

Substrate specificity and inhibitor analyses of human steroid 5beta-reductase (AKR1D1)

2011

Chen, M.; Drury, J.E.; Penning, T.M.

Steroids

76

484-490

744344

26522442

Cytochrome P450 125A4, the third cholesterol C-26 hydroxylase from Mycobacterium smegmatis

2015

Frank, D.J.; Waddling, C.A.; La, M.; Ortiz de Montellano, P.R.

Biochemistry

54

6909-6916

Links to other databases for 7alpha-hydroxycholest-4-en-3-one

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Show Links (1 entry)

ChEBI

PubChem