Biology:3alpha-hydroxysteroid dehydrogenase (A-specific)
| 3-alpha-hydroxysteroid dehydrogenase (A-specific) | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 1.1.1.213 | ||||||||
| 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 | ||||||||
| |||||||||
In enzymology, a 3alpha-hydroxysteroid dehydrogenase (A-specific) (EC 1.1.1.213) is an enzyme that catalyzes the chemical reaction
- androsterone + NAD(P)+ [math]\displaystyle{ \rightleftharpoons }[/math] 5alpha-androstane-3,17-dione + NAD(P)H + H+
The 3 substrates of this enzyme are androsterone, NAD+, and NADP+, whereas its 4 products are 5alpha-androstane-3,17-dione, NADH, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor, more specifically it is part of the group of hydroxysteroid dehydrogenases. The systematic name of this enzyme class is 3alpha-hydroxysteroid:NAD(P)+ oxidoreductase (A-specific).
Structural studies
As of late 2007, 11 structures have been solved for this class of enzymes, with PDB accession codes 1J96, 1LWI, 1S1P, 1S1R, 1S2A, 1S2C, 1XJB, 2F38, 2FGB, 2HDJ, and 2IPJ.
References
- "Stereochemistry of hydrogen transfer from pyridine nucleotides catalyzed by delta-4-3-oxosteroid 5-beta-reductase and 3-alpha-hydroxysteroid dehydrogenase from rat liver". Eur. J. Biochem. 12 (1): 80–4. 1970. doi:10.1111/j.1432-1033.1970.tb00823.x. PMID 4392180.
- Tomkins GM (1956). "A mammalian 3alpha-hydroxysteroid dehydrogenase". J. Biol. Chem. 218 (1): 437–447. PMID 13278351.
 |  |
