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Literature summary for 1.14.14.19 extracted from

  • Yoshimoto, F.K.; Peng, H.M.; Zhang, H.; Anderson, S.M.; Auchus, R.J.
    Epoxidation activities of human cytochromes P450c17 and P450c21 (2014), Biochemistry, 53, 7531-7540 .
    View publication on PubMedView publication on EuropePMC

Protein Variants

Protein Variants Comment Organism
A105L mutant has reduced progesterone 16alpha-hydroxylase activity. Catalyzes the 16alpha,17-epoxidation and the ordinarily minor 21-hydroxylation of 16,17-dehydroprogesterone in a 1:5 ratio of epoxide:21-hydroxylated products Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens P05093
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
16,17-dehydropregnenolone + [reduced NADPH-hemoprotein reductase] + O2
-
Homo sapiens ? + [oxidized NADPH-hemoprotein reductase] + H2O
-
?
16,17-dehydroprogesterone + [reduced NADPH-hemoprotein reductase] + O2
-
Homo sapiens ? + [oxidized NADPH-hemoprotein reductase] + H2O
-
?
additional information CYP17A1 wild-type and mutation A105L do not hydroxylate pregnenolone in 21- or 16alpha-position Homo sapiens ?
-
?

Synonyms

Synonyms Comment Organism
P450c17
-
Homo sapiens