3alpha(or 20beta)-hydroxysteroid dehydrogenase

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

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

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. PMID 718844. doi:10.1021/bi00614a003.
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. PMID 16526091. doi:10.1002/pmic.200500108.
Lynn WS Jr, Brown RH (1958). "The conversion of progesterone to androgens by testes". J. Biol. Chem. 232 (2): 1015–30. 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. PMID 6936053. doi:10.1021/bi00563a002.
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. PMID 6928375. doi:10.1021/bi00546a023.

Oxidoreductases: alcohol oxidoreductases (EC 1.1)
1.1.1: NAD/NADP acceptor	3-hydroxyacyl-CoA dehydrogenase 3-hydroxybutyryl-CoA dehydrogenase Alcohol dehydrogenase Aldo-keto reductase 1A1 1B1 1B10 1C1 1C3 1C4 7A2 Aldose reductase Beta-Ketoacyl ACP reductase Carbohydrate dehydrogenases Carnitine dehydrogenase D-malate dehydrogenase (decarboxylating) DXP reductoisomerase Glucose-6-phosphate dehydrogenase Glycerol-3-phosphate dehydrogenase HMG-CoA reductase IMP dehydrogenase Isocitrate dehydrogenase Lactate dehydrogenase L-threonine dehydrogenase L-xylulose reductase Malate dehydrogenase Malate dehydrogenase (decarboxylating) Malate dehydrogenase (NADP+) Malate dehydrogenase (oxaloacetate-decarboxylating) Malate dehydrogenase (oxaloacetate-decarboxylating) (NADP+) Phosphogluconate dehydrogenase Sorbitol dehydrogenase Hydroxysteroid dehydrogenase: 3β 3β-HSD NSDHL 11β 11β-HSD1 11β-HSD2 17β
1.1.2: cytochrome acceptor	D-lactate dehydrogenase (cytochrome) D-lactate dehydrogenase (cytochrome c-553) Mannitol dehydrogenase (cytochrome)
1.1.3: oxygen acceptor	Glucose oxidase L-gulonolactone oxidase Xanthine oxidase
1.1.4: disulfide as acceptor	Vitamin K epoxide reductase Vitamin-K-epoxide reductase (warfarin-insensitive)
1.1.5: quinone/similar acceptor	Malate dehydrogenase (quinone) Quinoprotein glucose dehydrogenase
1.1.99: other acceptors	Choline dehydrogenase L2HGDH

Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Catalytically perfect enzyme Coenzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor
Classification	EC number Enzyme superfamily Enzyme family List of enzymes
Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics
Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list)

This article is issued from Wikipedia. The text is licensed under Creative Commons - Attribution - Sharealike. Additional terms may apply for the media files.