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2p5n

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Template:STRUCTURE 2p5n

Contents

Crystal structure of mouse 17-alpha hydroxysteroid dehydrogenase in complex with coenzyme NADPH

Template:ABSTRACT PUBMED 17909281

Function

[AK1CL_MOUSE] NADP-dependent 17-alpha-hydroxysteroid dehydrogenase that converts 5-alpha-androstane-3,17-dione into androsterone. Has lower 3-alpha-hydroxysteroid dehydrogenase activity. Has broad substrate specificity and acts on various 17-alpha-hydroxysteroids, 17-ketosteroids, 3-alpha hydroxysteroids and 3-ketosteroids. Reduction of keto groups is strictly stereoselective. Reduction of 17-ketosteroids yields only 17-alpha-hydroxysteroids. Likewise, reduction of 3-ketosteroids yields only 3-alpha-hydroxysteroids.[1] [2] [3]

About this Structure

2p5n is a 2 chain structure with sequence from Lk3 transgenic mice. Full crystallographic information is available from OCA.

See Also

Reference

  • Dhagat U, Carbone V, Chung RP, Schulze-Briese C, Endo S, Hara A, El-Kabbani O. Structure of 3(17)alpha-hydroxysteroid dehydrogenase (AKR1C21) holoenzyme from an orthorhombic crystal form: an insight into the bifunctionality of the enzyme. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2007 Oct 1;63(Pt, 10):825-30. Epub 2007 Sep 19. PMID:17909281 doi:S1744309107040985
  1. ↑ Ishikura S, Usami N, Nakajima S, Kameyama A, Shiraishi H, Carbone V, El-Kabbani O, Hara A. Characterization of two isoforms of mouse 3(17)alpha-hydroxysteroid dehydrogenases of the aldo-keto reductase family. Biol Pharm Bull. 2004 Dec;27(12):1939-45. PMID:15577209
  2. ↑ Bellemare V, Faucher F, Breton R, Luu-The V. Characterization of 17alpha-hydroxysteroid dehydrogenase activity (17alpha-HSD) and its involvement in the biosynthesis of epitestosterone. BMC Biochem. 2005 Jul 14;6:12. PMID:16018803 doi:http://dx.doi.org/1471-2091-6-12
  3. ↑ Faucher F, Pereira de Jesus-Tran K, Cantin L, Luu-The V, Labrie F, Breton R. Crystal structures of mouse 17alpha-hydroxysteroid dehydrogenase (apoenzyme and enzyme-NADP(H) binary complex): identification of molecular determinants responsible for the unique 17alpha-reductive activity of this enzyme. J Mol Biol. 2006 Dec 8;364(4):747-63. Epub 2006 Sep 16. PMID:17034817 doi:http://dx.doi.org/10.1016/j.jmb.2006.09.030

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