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Ligand 5beta-cholestane-3alpha,7alpha-diol

Basic Ligand Information

Molecular Structure

Show all BRENDA pathways known for 5beta-cholestane-3alpha,7alpha-diol

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Roles as Enzyme Ligand

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

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Show Natural Substrate (1 entry)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.14.15.15

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

674399, 674400

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Substrate in Enzyme-catalyzed Reactions (3 results)

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Show Substrate (3 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.14.14.139

5beta-cholestane-3alpha,7alpha-diol + [reduced NADPH-hemoprotein reductase] + O2 = 5beta-cholestane-3alpha,7alpha,12alpha-triol + [oxidized NADPH-hemoprotein reductase] + H2O

659115

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1.14.15.15

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

674399, 674400

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1.14.15.15

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

439029, 439030, 439034

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1.14.15.15

2 entries

Product in Enzyme-catalyzed Reactions (1 result)

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Show Product (1 entry)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.1.1.213

7alpha-hydroxy-5beta-cholestan-3-one + NADPH + H+ = 5beta-cholestane-3alpha,7alpha-diol + NADP+

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Inhibitor in Enzyme-catalyzed Reactions (2 results)

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Show Inhibitors (2 entries)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

1.14.14.139

0.066 mM, 30% inhibition

659116

-

1.14.15.15

inhibits 5beta-cholestane-3alpha,7alpha,12alpha-triol 27-monooxygenase activity only slightly

439029

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Enzyme Kinetic Parameters

k_cat Value (Turnover Number) (1 result)

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Show Turnover Number (1 entry)

EC NUMBER

TURNOVER NUMBER [1/S]

TURNOVER NUMBER MAXIMUM [1/S]

COMMENTARY

LITERATURE

1.14.15.15

0.217

-

-

439030, 439034

K_M Value (1 result)

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Show KM Value (1 entry)

EC NUMBER

KM VALUE [MM]

KM VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

1.14.15.15

0.01

-

-

439029

References & Links

Literature References (7)

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Show Reference (7 entries)

BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

PAGES

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

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

659115

6766451

Hydroxylations in biosynthesis and metabolism of bile acids. Catalytic properties of different cytochrome P-450

1980

Hansson, R.; Wikvall, K.

J. Biol. Chem.

255

1643-1649

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

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

Links to other databases for 5beta-cholestane-3alpha,7alpha-diol

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Show Links (1 entry)

ChEBI

PubChem

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