CATH Classification
Level | CATH Code | Description |
---|---|---|
1 | Mainly Alpha | |
1.10 | Orthogonal Bundle | |
1.10.630 | Cytochrome p450 | |
1.10.630.10 | Cytochrome P450 |
Domain Context
CATH Clusters
Superfamily | Cytochrome P450 |
Functional Family | Cytochrome P450 1A1 |
Enzyme Information
1.14.14.19 |
Steroid 17-alpha-monooxygenase.
based on mapping to UniProt P05093
A C(21)-steroid + [reduced NADPH--hemoprotein reductase] + O(2) = a 17-alpha-hydroxy-C(21)-steroid + [oxidized NADPH--hemoprotein reductase] + H(2)O.
-!- Requires NADPH and EC 1.6.2.4. -!- Catalyzes two independent reactions at the same active site - the 17-alpha-hydroxylation of pregnenolone and progesterone, which is part of glucocorticoid hormones biosynthesis, and the conversion of the 17-alpha-hydroxylated products via a 17,20-lyase reaction to form androstenedione and dehydroepiandrosterone, leading to sex hormone biosynthesis (EC 1.14.14.32). -!- The ratio of the 17-alpha-hydroxylase and 17,20-lyase activities is an important factor in determining the directions of steroid hormone biosynthesis toward biosynthesis of glucocorticoid or sex hormones. -!- Formerly EC 1.14.1.7, EC 1.14.99.9 and EC 1.99.1.9.
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1.14.14.32 |
17-alpha-hydroxyprogesterone deacetylase.
based on mapping to UniProt P05093
(1) 17-alpha-hydroxyprogesterone + [reduced NADPH--hemoprotein reductase] + O(2) = androstenedione + acetate + [oxidized NADPH--hemoprotein reductase] + H(2)O. (2) 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 1.14.14.19), 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 latter. -!- Formerly EC 4.1.2.30.
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UniProtKB Entries (1)
P05093 |
CP17A_HUMAN
Homo sapiens
Steroid 17-alpha-hydroxylase/17,20 lyase
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PDB Structure
PDB | 6CIZ |
External Links | |
Method | X-RAY DIFFRACTION |
Organism | |
Primary Citation |
Structure-Based Design of Inhibitors with Improved Selectivity for Steroidogenic Cytochrome P450 17A1 over Cytochrome P450 21A2.
J. Med. Chem.
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