3alpha(or 20beta)-hydroxysteroid dehydrogenase
In enzymology, a 3alpha(or 20beta)-hydroxysteroid dehydrogenase (EC 1.1.1.53) is an enzyme that catalyzes the chemical reaction
| 3-alpha(or 20-beta)-hydroxysteroid dehydrogenase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 3-alpha,20-beta-hydroxysteroid dehydrogenase tetramer, Streptomyces exfoliatus | |||||||||
| Identifiers | |||||||||
| EC no. | 1.1.1.53 | ||||||||
| CAS no. | 9028-42-6 | ||||||||
| 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 | ||||||||
| |||||||||
- androstan-3alpha,17beta-diol + NAD+ 17beta-hydroxyandrostan-3-one + NADH + H+
Thus, the two substrates of this enzyme are androstan-3alpha,17beta-diol and NAD+, whereas its 3 products are 17beta-hydroxyandrostan-3-one, NADH, 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. The systematic name of this enzyme class is 3alpha(or 20beta)-hydroxysteroid:NAD+ oxidoreductase. Other names in common use include cortisone reductase, (R)-20-hydroxysteroid dehydrogenase, dehydrogenase, 20beta-hydroxy steroid, Delta4-3-ketosteroid hydrogenase, 20beta-hydroxysteroid dehydrogenase, 3alpha,20beta-hydroxysteroid:NAD+-oxidoreductase, NADH-20beta-hydroxysteroid dehydrogenase, and 20beta-HSD. This enzyme participates in bile acid biosynthesis and c21-steroid hormone metabolism.
Structural studies
editAs of late 2007, 6 structures have been solved for this class of enzymes, with PDB accession codes 1HDC, 1N5D, 1NFF, 1NFQ, 1NFR, and 2HSD.
References
edit- Edwards CA, Orr JC (1978). "Comparison of the 3α- and 20β-Hydroxysteroid Dehydrogenase Activities of the Cortisone Reductase of Streptomyces hydrogenans". Biochemistry. 17 (21): 4370–6. doi:10.1021/bi00614a003. PMID 718844.
- Kung CC, Huang WN, Huang YC, Yeh KC (2006). "Proteomic survey of copper-binding proteins in Arabidopsis roots by immobilized metal affinity chromatography and mass spectrometry". Proteomics. 6 (9): 2746–58. doi:10.1002/pmic.200500108. PMID 16526091. S2CID 25896917.
- Lynn WS Jr, Brown RH (1958). "The conversion of progesterone to androgens by testes". J. Biol. Chem. 232 (2): 1015–30. doi:10.1016/S0021-9258(19)77419-5. PMID 13549484.
- Strickler RC, Covey DF, Tobias B (1980). "Study of 3α,20β-Hydroxysteroid Dehydrogenase with an Enzyme-Generated Affinity Alkylator: Dual Enzyme Activity at a Single Active Site". Biochemistry. 19 (22): 4950–4. doi:10.1021/bi00563a002. PMID 6936053.
- Sweet F, Samant BR (1980). "Bifunctional Enzyme Activity at the Same Active Site: Study of 3α and 20β Activity by Affinity Alkylation of 3α,20β-Hydroxysteroid Dehydrogenase with 17-(Bromoacetoxy)steroids". Biochemistry. 19 (5): 978–86. doi:10.1021/bi00546a023. PMID 6928375.
