Title : The molecular basis of isolated 17,20 lyase deficiency.

Pub. Date : 1998 Aug-Nov

PMID : 9888582






4 Functional Relationships(s)
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Sentence
Compound Name
Protein Name
Organism
1 Human P450c17 catalyzes the 17alpha-hydroxylation of pregnenolone to 17OH pregnenolone and of progesterone to 17alpha-OH progesterone; the same P450c17 enzyme also catalyzes 17,20 lyase activity on the same active site, converting 17OH-pregnenolone to DHEA. Dehydroepiandrosterone cytochrome P450 family 17 subfamily A member 1 Homo sapiens
2 Human P450c17 catalyzes the 17alpha-hydroxylation of pregnenolone to 17OH pregnenolone and of progesterone to 17alpha-OH progesterone; the same P450c17 enzyme also catalyzes 17,20 lyase activity on the same active site, converting 17OH-pregnenolone to DHEA. Dehydroepiandrosterone cytochrome P450 family 17 subfamily A member 1 Homo sapiens
3 Rodent and porcine P450c17 also catalyze 17,20 lyase activity with delta4 substrates, converting 17OH-progesterone to delta4 androstenedione, but human P450c17 catalyzes this reaction very inefficiently, so that virtually all human C19 sex steroids are made via 17OH pregnenolone and DHEA. Dehydroepiandrosterone cytochrome P450 family 17 subfamily A member 1 Homo sapiens
4 Rodent and porcine P450c17 also catalyze 17,20 lyase activity with delta4 substrates, converting 17OH-progesterone to delta4 androstenedione, but human P450c17 catalyzes this reaction very inefficiently, so that virtually all human C19 sex steroids are made via 17OH pregnenolone and DHEA. Dehydroepiandrosterone cytochrome P450 family 17 subfamily A member 1 Homo sapiens