21β-hydroxylase
| Steroid 21-Hydroxylase | |||||||||
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| Identifiers | |||||||||
| EC number | 1.14.99.10 | ||||||||
| CAS number | 9029-68-9 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
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| Search | |
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| PMC | articles |
| PubMed | articles |
| NCBI | proteins |
Steroid 21-hydroxylase, also called steroid 21-monooxygenase, 21α-Hydroxylase, P450 21A2, and, less commonly 21β-Hydroxylase, is a enzyme that is involved with the biosynthesis of the steroid hormones aldosterone and cortisol. These syntheses take place in the adrenal cortex. Specifically, 21-hydroxylase converts progesterone and 17α-hydroxyprogesterone into 11-deoxycorticosterone and 11-deoxycortisol, respectively, by hydroxylating at the C21 position. The products of the conversions then continue through their appropriate pathways towards creation of aldosterone and cortisol. Like other cytochrome P450 enzymes, 21-hydroxylase participates in the , and engages in one-electron transfer with NADPH-. Its structure includes an essential iron heme group centered within the protein, also common to all P450 enzymes. Variations of the 21-hydroxylase enzyme can be found in all vertebrates. However, understanding of human 21-hydroxylase structure and function is of particular clinical value, as a failure of the enzyme to act appropriately results in congenital adrenal hyperplasia. The x-ray crystal structure for human 21-hydroxylase, with bound progesterone, was realized and published in 2015, providing opportunity for further study. The enzyme is notable for its substrate specificity and relatively high catalytic efficiency.
21-hydroxylase is a complex of three independent and identical enzyme subunits. Each subunit in the human enzyme consists of 13 ...
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