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Literature summary for 1.14.15.18 extracted from

  • Postlind, H.
    Separation of the cytochromes P-450 in pig kidney mitochondria catalyzing 1 alpha-, 24- and 26-hydroxylations of 25-hydroxyvitamin D3 (1990), Biochem. Biophys. Res. Commun., 168, 261-266.
    View publication on PubMed

Localization

Localization Comment Organism GeneOntology No. Textmining
mitochondrion
-
Sus scrofa 5739
-

Organism

Organism UniProt Comment Textmining
Sus scrofa
-
-
-

Purification (Commentary)

Purification (Comment) Organism
purification of 1alpha-hydroxylating cytochrome P-450 Sus scrofa

Reaction

Reaction Comment Organism Reaction ID
calcidiol + 2 reduced adrenodoxin + 2 H+ + O2 = calcitriol + 2 oxidized adrenodoxin + H2O cytochrome P-450 type is specific for hydroxylation site of 25-hydroxyvitamin D3 Sus scrofa
calcidiol + 2 reduced adrenodoxin + 2 H+ + O2 = calcitriol + 2 oxidized adrenodoxin + H2O ferredoxin, ferredoxin reductase and cytochrome P-450 Sus scrofa

Source Tissue

Source Tissue Comment Organism Textmining
kidney
-
Sus scrofa
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
calcidiol + NADPH + O2 highly specific for calcidiol, calcidiol is identical with 25-hydroxycholecalciferol Sus scrofa calcitriol + NADP+ + H2O calcitriol is identical with 1,25-dihydroxycholecalciferol ?

Cofactor

Cofactor Comment Organism Structure
NADPH
-
Sus scrofa