Title : Mechanism of the Clinically Relevant E305G Mutation in Human P450 CYP17A1.

Pub. Date : 2021 Nov 2

PMID : 34662099






4 Functional Relationships(s)
Download
Sentence
Compound Name
Protein Name
Organism
1 An important branch point in human androgen production is catalyzed by cytochrome P450 CYP17A1 and involves an initial Compound I-mediated hydroxylation at the 17-position of either progesterone (PROG) or pregnenolone (PREG) to form 17-hydroxy derivatives, 17OH-PROG and 17OH-PREG, with approximately similar efficiencies. Progesterone cytochrome P450 family 17 subfamily A member 1 Homo sapiens
2 An important branch point in human androgen production is catalyzed by cytochrome P450 CYP17A1 and involves an initial Compound I-mediated hydroxylation at the 17-position of either progesterone (PROG) or pregnenolone (PREG) to form 17-hydroxy derivatives, 17OH-PROG and 17OH-PREG, with approximately similar efficiencies. Progesterone cytochrome P450 family 17 subfamily A member 1 Homo sapiens
3 For example, the replacement of the glutamic acid side with a glycine chain at position 305 in the CYP17A1 structure causes a clinically relevant steroidopathy; E305G CYP17A1 displays a dramatic decrease in the production of dehydroepiandrosterone from pregnenolone but surprisingly increases the activity of the enzyme toward the formation of androstenedione from progesterone. Progesterone cytochrome P450 family 17 subfamily A member 1 Homo sapiens
4 For example, the replacement of the glutamic acid side with a glycine chain at position 305 in the CYP17A1 structure causes a clinically relevant steroidopathy; E305G CYP17A1 displays a dramatic decrease in the production of dehydroepiandrosterone from pregnenolone but surprisingly increases the activity of the enzyme toward the formation of androstenedione from progesterone. Progesterone cytochrome P450 family 17 subfamily A member 1 Homo sapiens