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Literature summary extracted from

  • Andemson, S.; Davis, D.L.; Dahlback, H.; Jornvall, H.; Russell, D.W.
    Cloning, structure, and expression of the mitochondrial cytochrome P-450 sterol 26-hydroxylase, a bile acid biosynthetic enzyme (1989), J. Biol. Chem., 264, 8222-8229.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.14.15.15 DNA and amino acid sequence determinationa nd analysis, functional expression in COS-M6 cells, overview Oryctolagus cuniculus

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.14.15.15 mitochondrion
-
 Oryctolagus cuniculus 5739
-

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.14.15.15 56657
-
 x * 56657, amino acid sequence calculation Oryctolagus cuniculus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.14.15.15 5-cholestene-3beta,7alpha-diol + reduced adrenodoxin + O2 Oryctolagus cuniculus
-
 5-cholestene-3alpha,7alpha,26-triol + oxidized adrenodoxin + H2O
-
 ?
1.14.15.15 5beta-cholestane-3alpha,7alpha,12alpha-triol + reduced adrenodoxin + O2 Oryctolagus cuniculus
-
 5beta-cholestane-3alpha,7alpha,12alpha,26-tetraol + oxidized adrenodoxin + H2O
-
 ?
1.14.15.15 5beta-cholestane-3alpha,7alpha-diol + reduced adrenodoxin + O2 Oryctolagus cuniculus
-
 5beta-cholestane-3alpha,7alpha,26-triol + oxidized adrenodoxin + H2O
-
 ?
1.14.15.15 7alpha-hydroxy-4-cholesten-3-one + reduced adrenodoxin + O2 Oryctolagus cuniculus
-
 7alpha,26-dihydroxy-4-cholesten-3-one + oxidized adrenodoxin + H2O
-
 ?
1.14.15.15 cholesterol + reduced adrenodoxin + H+ + O2 Oryctolagus cuniculus
-
 26-hydroxycholesterol + oxidized adrenodoxin + H2O
-
 ?
1.14.15.15 additional information Oryctolagus cuniculus the enzyme catalyzes the first step in the oxidation of the side chain of sterol intermediates in the biosynthesis of bile acids ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.14.15.15 Oryctolagus cuniculus
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.14.15.15 native enzyme partially by mitochondria preparation Oryctolagus cuniculus

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.14.15.15 liver
-
 Oryctolagus cuniculus
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.14.15.15 5-cholestene-3beta,7alpha-diol + reduced adrenodoxin + O2
-
 Oryctolagus cuniculus 5-cholestene-3alpha,7alpha,26-triol + oxidized adrenodoxin + H2O
-
 ?
1.14.15.15 5beta-cholestane-3alpha,7alpha,12alpha-triol + reduced adrenodoxin + O2
-
 Oryctolagus cuniculus 5beta-cholestane-3alpha,7alpha,12alpha,26-tetraol + oxidized adrenodoxin + H2O
-
 ?
1.14.15.15 5beta-cholestane-3alpha,7alpha-diol + reduced adrenodoxin + O2
-
 Oryctolagus cuniculus 5beta-cholestane-3alpha,7alpha,26-triol + oxidized adrenodoxin + H2O
-
 ?
1.14.15.15 7alpha-hydroxy-4-cholesten-3-one + reduced adrenodoxin + O2
-
 Oryctolagus cuniculus 7alpha,26-dihydroxy-4-cholesten-3-one + oxidized adrenodoxin + H2O
-
 ?
1.14.15.15 cholesterol + reduced adrenodoxin + H+ + O2
-
 Oryctolagus cuniculus 26-hydroxycholesterol + oxidized adrenodoxin + H2O
-
 ?
1.14.15.15 additional information the enzyme catalyzes the first step in the oxidation of the side chain of sterol intermediates in the biosynthesis of bile acids Oryctolagus cuniculus ?
-
 ?

Subunits

EC Number Subunits Comment Organism
1.14.15.15 ? x * 56657, amino acid sequence calculation Oryctolagus cuniculus

Synonyms

EC Number Synonyms Comment Organism
1.14.15.15 cytochrome P-450 sterol 26-hydroxylase
-
 Oryctolagus cuniculus

Cofactor

EC Number Cofactor Comment Organism Structure
1.14.15.15 Ferredoxin
-
 Oryctolagus cuniculus
1.14.15.15 NADPH
-
 Oryctolagus cuniculus