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ENZYME entry: EC 22.214.171.124
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- 17-alpha-hydroxyprogesterone + [reduced NADPH--hemoprotein reductase] + O(2) <=> androstenedione + acetate + [oxidized NADPH--hemoprotein reductase] + H(2)O
- 17-alpha-hydroxypregnenolone + [reduced NADPH--hemoprotein reductase] + O(2) <=> 3-beta-hydroxyandrost-5-en-17-one + acetate + [oxidized NADPH--hemoprotein reductase] + H(2)O
- A microsomal protein that catalyzes two independent reactions at the
same active site - the 17-hydroxylation of pregnenolone and
progesterone, which is part of glucocorticoid hormones biosynthesis
(EC 126.96.36.199), and the conversion of the 17-hydroxylated products
via a 17,20-lyase reaction to form androstenedione and 3-beta-
hydroxyandrost-5-en-17-one, leading to sex hormone biosynthesis.
- The activity of this reaction is dependent on the allosteric
interaction of the enzyme with cytochrome b5 without any transfer of
electrons from the cytochrome.
- The enzymes from different organisms differ in their substrate
specificity; while the enzymes from pig, hamster, and rat accept both
17-alpha-hydroxyprogesterone and 17-alpha-hydroxypregnenolone,
the enzymes from human, bovine, sheep, goat, and bison do not accept
the former, and the enzyme from guinea pig does not accept the
- Formerly EC 188.8.131.52.
|PRIAM enzyme-specific profiles||184.108.40.206|
|KEGG Ligand Database for Enzyme Nomenclature||220.127.116.11|
|IUBMB Enzyme Nomenclature||18.104.22.168|
|MEDLINE||Find literature relating to 22.214.171.124|
|Q9GMC7, CP17A_BISBI; ||P05185, CP17A_BOVIN; ||Q9N0U7, CP17A_CAPHI; |
|Q64410, CP17A_CAVPO; ||P12394, CP17A_CHICK; ||Q9GMC8, CP17A_FELCA; |
|Q95328, CP17A_HORSE; ||P05093, CP17A_HUMAN; ||O73853, CP17A_ICTPU; |
|Q2XVA1, CP17A_MACFA; ||Q8HYM9, CP17A_MACMU; ||P70687, CP17A_MESAU; |
|P27786, CP17A_MOUSE; ||P30437, CP17A_ONCMY; ||P70085, CP17A_ORYLA; |
|Q8HYN1, CP17A_PANTR; ||Q8HYN0, CP17A_PAPCY; ||Q9GLD2, CP17A_PAPHU; |
|Q91Z85, CP17A_PERLE; ||P19100, CP17A_PIG; ||O57525, CP17A_RANDY; |
|P11715, CP17A_RAT; ||Q29497, CP17A_SHEEP; ||Q92113, CP17A_SQUAC; |
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