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Information on EC - 17alpha-hydroxyprogesterone deacetylase

for references in articles please use BRENDA:EC1.14.14.32
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IUBMB Comments
A microsomal cytochrome P-450 (heme-thiolate) protein that catalyses two independent reactions at the same active site - the 17-hydroxylation of pregnenolone and progesterone, which is part of glucocorticoid hormones biosynthesis (EC, and the conversion of the 17-hydroxylated products via a 17,20-lyase reaction to form androstenedione and 3beta-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 [2,4]. The enzymes from different organisms differ in their substrate specificity. While the enzymes from pig, hamster, and rat accept both 17alpha-hydroxyprogesterone and 17alpha-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 latter .
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The enzyme appears in viruses and cellular organisms
cyp17, cyp17a1, p450c17, 17alpha-hydroxylase, cytochrome p450c17, 17,20 lyase, c17,20-lyase, 17alpha-hydroxylase/17,20-lyase, cytochrome p450 17a1, cytochrome p450 17, more
17alpha-hydroxypregnenolone + [reduced NADPH-hemoprotein reductase] + O2 = 3beta-hydroxyandrost-5-en-17-one + acetate + [oxidized NADPH-hemoprotein reductase] + H2O
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17alpha-hydroxyprogesterone + [reduced NADPH-hemoprotein reductase] + O2 = androstenedione + acetate + [oxidized NADPH-hemoprotein reductase] + H2O
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