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3alpha(or 20beta)-hydroxysteroid dehydrogenase

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(Redirected from 20β-HSD)
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
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
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PMCarticles
PubMedarticles
NCBIproteins

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+ 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

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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.

References

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  • 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.