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Literature summary for 1.14.14.19 extracted from

  • Nakajin, S.; Shinoda, M.; Hall, P.F.
    Purification and properties of 17alpha-hydroxylase from microsomes of pig adrenal: a second C21 side-chain cleavage system (1983), Biochem. Biophys. Res. Commun., 111, 512-517.
    View publication on PubMed

Localization

Localization Comment Organism GeneOntology No. Textmining
microsome
-
Sus scrofa
-
-

Metals/Ions

Metals/Ions Comment Organism Structure
Fe3+ 11.1 nM heme per mg protein Sus scrofa

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
53000
-
SDS-PAGE Sus scrofa

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
progesterone + [reduced NADPH-hemoprotein reductase] + O2 Sus scrofa
-
17alpha-hydroxyprogesterone + [oxidized NADPH-hemoprotein reductase] + H2O product eliminates at C20,21 acetate to yield androstenedione ?

Organism

Organism UniProt Comment Textmining
Sus scrofa
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Sus scrofa

Source Tissue

Source Tissue Comment Organism Textmining
adrenal gland
-
Sus scrofa
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
progesterone + [reduced NADPH-hemoprotein reductase] + O2
-
Sus scrofa 17alpha-hydroxyprogesterone + [oxidized NADPH-hemoprotein reductase] + H2O product eliminates at C20,21 acetate to yield androstenedione ?