3alpha(or 20beta)-hydroxysteroid dehydrogenase

From Wikipedia, the free encyclopedia

In enzymology, a 3alpha(or 20beta)-hydroxysteroid dehydrogenase (EC 1.1.1.53) is an enzyme that catalyzes the chemical reaction

androstan-3alpha,17beta-diol + NAD⁺ $\rightleftharpoons$ 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.

1 Structural studies
2 References
3 External links
- 3.1 Gene Ontology (GO) codes

[edit] Structural studies

As of late 2007, 6 structures have been solved for this class of enzymes, with PDB accession codes 1HDC, 1N5D, 1NFF, 1NFQ, 1NFR, and 2HSD.

[edit] References

IUBMB entry for 1.1.1.53
BRENDA references for 1.1.1.53 (Recommended.)
PubMed references for 1.1.1.53
PubMed Central references for 1.1.1.53
Google Scholar references for 1.1.1.53
Edwards CA, Orr JC (1978). "Comparison of the 3alpha-and 20beta-hydroxysteroid dehydrogenase activities of the cortisone reductase of Streptomyces hydrogenans". Biochemistry. 17: 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: 2746–58. doi:10.1002/pmic.200500108. PMID 16526091.
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: 2746–58. doi:10.1002/pmic.200500108. PMID 16526091.
LYNN WS Jr, BROWN RH (1958). "The conversion of progesterone to androgens by testes". J. Biol. Chem. 232: 1015–30. PMID 13549484.
Strickler RC, Covey DF, Tobias B (1980). "Study of 3 alpha, 20 beta-hydroxysteroid dehydrogenase with an enzyme-generated affinity alkylator: dual enzyme activity at a single active site". Biochemistry. 19: 4950–4. doi:10.1021/bi00563a002. PMID 6936053.
Sweet F, Samant BR (1980). "Bifunctional enzyme activity at the same active site: study of 3 alpha and 20 beta activity by affinity alkylation of 3 alpha, 20 beta-hydroxysteroid dehydrogenase with 17-(bromoacetoxy)steroids". Biochemistry. 19: 978–86. doi:10.1021/bi00546a023. PMID 6928375.