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

Pub. Date : 2021 Nov 2

PMID : 34662099






2 Functional Relationships(s)
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1 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. Androstenedione cytochrome P450 family 17 subfamily A member 1 Homo sapiens
2 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. Androstenedione cytochrome P450 family 17 subfamily A member 1 Homo sapiens