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{{enzyme
| Name = 3-alpha(or 20-beta)-hydroxysteroid dehydrogenase
| EC_number = 1.1.1.53
| CAS_number = 9028-42-6
| IUBMB_EC_number = 1/1/1/53
| GO_code = 0047044
| image = 
| width = 
| caption = 
}}
In [[enzymology]], a '''3alpha(or 20beta)-hydroxysteroid dehydrogenase''' ({{EC number|1.1.1.53}}) is an [[enzyme]] that [[catalysis|catalyzes]] the [[chemical reaction]]

:[[Androstanediol|androstan-3alpha,17beta-diol]] + NAD<sup>+</sup> <math>\rightleftharpoons</math> 17beta-hydroxyandrostan-3-one + NADH + H<sup>+</sup>

Thus, the two [[substrate (biochemistry)|substrates]] of this enzyme are [[androstan-3alpha,17beta-diol]] and [[nicotinamide adenine dinucleotide|NAD<sup>+</sup>]], whereas its 3 [[product (chemistry)|products]] are [[17beta-hydroxyandrostan-3-one]], [[nicotinamide adenine dinucleotide|NADH]], and [[hydrogen ion|H<sup>+</sup>]].

This enzyme belongs to the family of [[oxidoreductase]]s, specifically those acting on the CH-OH group of donor with NAD<sup>+</sup> or NADP<sup>+</sup> as acceptor. The systematic name of this enzyme class is '''3alpha(or 20beta)-hydroxysteroid:NAD<sup>+</sup> 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<sup>+</sup>-oxidoreductase''', '''NADH-20beta-hydroxysteroid dehydrogenase''', and '''20beta-HSD'''. This enzyme participates in [[bile acid biosynthesis]] and [[c21-steroid hormone metabolism]].

==Structural studies==

As of late 2007, 6 [[tertiary structure|structures]] have been solved for this class of enzymes, with [[Protein Data Bank|PDB]] accession codes {{PDB link|1HDC}}, {{PDB link|1N5D}}, {{PDB link|1NFF}}, {{PDB link|1NFQ}}, {{PDB link|1NFR}}, and {{PDB link|2HSD}}.

==References==
{{reflist|1}}
* {{cite journal | author = Edwards CA, Orr JC | date = 1978 | title = Comparison of the 3''α''- and 20''β''-Hydroxysteroid Dehydrogenase Activities of the Cortisone Reductase of ''Streptomyces hydrogenans'' | journal = Biochemistry | volume = 17 | pages = 4370&ndash;6 | pmid = 718844 | doi = 10.1021/bi00614a003 | issue = 21 }}
* {{cite journal | author = Kung CC, Huang WN, Huang YC, Yeh KC | date = 2006 | title = Proteomic survey of copper-binding proteins in ''Arabidopsis'' roots by immobilized metal affinity chromatography and mass spectrometry | journal = Proteomics | volume = 6 | pages = 2746&ndash;58 | pmid = 16526091 | doi = 10.1002/pmic.200500108 | issue = 9 }}
* {{cite journal | author = Lynn WS Jr, Brown RH | date = 1958 | title = The conversion of progesterone to androgens by testes | journal = J. Biol. Chem. | volume = 232 | pages = 1015&ndash;30 | pmid = 13549484 | issue = 2 }}
* {{cite journal | author = Strickler RC, Covey DF, Tobias B | date = 1980 | title = Study of 3''α'',20''β''-Hydroxysteroid Dehydrogenase with an Enzyme-Generated Affinity Alkylator: Dual Enzyme Activity at a Single Active Site | journal = Biochemistry | volume = 19 | pages = 4950&ndash;4 | pmid = 6936053 | doi = 10.1021/bi00563a002 | issue = 22 }}
* {{cite journal | author = Sweet F, Samant BR | date = 1980 | title = Bifunctional Enzyme Activity at the Same Active Site: Study of 3''α'' and 20''β'' Activity by Affinity Alkylation of 3''α'',20''β''-Hydroxysteroid Dehydrogenase with 17-(Bromoacetoxy)steroids | journal = Biochemistry | volume = 19 | pages = 978&ndash;86 | pmid = 6928375 | doi = 10.1021/bi00546a023 | issue = 5 }}

[[Category:EC 1.1.1]]
[[Category:NADH-dependent enzymes]]
[[Category:Enzymes of known structure]]


{{1.1.1-enzyme-stub}}