EC Number   |
General Information |
Reference |
|---|
    1.14.14.32 | malfunction |
17alpha-hydroxylase/17,20-lyase deficiency can lead to complete lack of masculinization and to ambiguous genitalia |
703945 |
| 1.14.14.32 | malfunction |
Japanese girl having 17alpha-hydroxylase/17,20-lyase deficiency with a deletion of codon 53 or 54 encoding Phe (TTC) in exon 1 (DELTAF54) on a maternal allele and a missense mutation resulting in a substitution of Asn (AAC) for His (CAC) at codon 373 in exon 6 (H373N) on a paternal allele. These mutations inactivate both 17alpha-hydroxylase and 17,20-lyase activities |
705509 |
| 1.14.14.32 | malfunction |
ovarian androgen biosynthesis can be inhibited by silencing CYP17 expression |
706689 |
| 1.14.14.32 | physiological function |
17alpha-hydroxylase/C17,20-lyase, CYP17, a P450 enzyme, is responsible for catalyzing the final step in androgen biosynthesis |
715857 |
| 1.14.14.32 | physiological function |
critical role of P450c17-I during shift in steroidogenesis, important role during ovarian development |
703775 |
| 1.14.14.32 | physiological function |
enzyme is most directly responsible for androgen synthesis |
706819 |
| 1.14.14.32 | physiological function |
no detectable differences in cognitive spatial learning between CYP17 chimeric and wild-type mice. Serum testosterone levels are reduced by 65% in the chimeric mice. Adult mouse brain dehydroepiandrosterone is formed via a Fe2+-sensitive CYP17-independent pathway |
-, 705402 |
| 1.14.14.32 | physiological function |
seasonal changes in testicular weight and size are correlated with spermatogenesis and P450c17 and aromatase cytochrome P450 (P450arom) |
705389 |
| 1.14.14.32 | physiological function |
the MEK/ERK pathway functions to inhibit the production of CYP17, while enhance the production of CYP19 in granulosa cells, probably involving a mechanism depending on c-fos, a downstream target of mitogen and extracellular signal-regulated kinases (MEK/ERK) signaling |
738346 |
| 1.14.14.32 | physiological function |
within living cells there are close interactions between cytochrome P450c17 and cytochrome b5. Residues E48 and E49 in cytochrome b5 are essential for activity, specific protein-protein interactions take place in a lipid membrane. The wild type cytochrome b5, but not a mutated, E48G/E49G cyt b5, alters the kinetics of electron transfer between the electrode and the P450c17 |
739432 |
