3alpha-hydroxysteroid dehydrogenase (A-specific)
| 3-alpha-hydroxysteroid dehydrogenase (A-specific) | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 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)+ 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
[edit]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
[edit]- Bjorkhem I, Danielsson H (1970). "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. 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. doi:10.1016/S0021-9258(18)65907-1. PMID 13278351.
