Structural and biochemical insights into 7β‐hydroxysteroid dehydrogenase stereoselectivity. Issue 6 (6th April 2016)

• Record Type: Journal Article
• Authors: Savino, Simone; Ferrandi, Erica Elisa; Forneris, Federico; Rovida, Stefano; Riva, Sergio; Monti, Daniela; Mattevi, Andrea
• Is Part Of: Proteins. Volume 84:Issue 6(2016)
• Page Start: 859
• Page End: 865
• Publication Date: 2016-04-06
• Subjects: biocatalysis -- short‐chain dehydrogenase -- steroid -- stereoselectivity -- NADP; Proteins -- Periodicals; Proteins -- Periodicals; 572.6
• DOI: 10.1002/prot.25036
• Languages: English
• ISSNs: 0887-3585

Abstract

ABSTRACT: Hydroxysteroid dehydrogenases are of great interest as biocatalysts for transformations involving steroid substrates. They feature a high degree of stereo‐ and regio‐selectivity, acting on a defined atom with a specific configuration of the steroid nucleus. The crystal structure of 7β‐hydroxysteroid dehydrogenase from Collinsella aerofaciens reveals a loop gating active‐site accessibility, the bases of the specificity for NADP +, and the general architecture of the steroid binding site. Comparison with 7α‐hydroxysteroid dehydrogenase provides a rationale for the opposite stereoselectivity. The presence of a C‐terminal extension reshapes the substrate site of the β‐selective enzyme, possibly leading to an inverted orientation of the bound substrate. Proteins 2016; 84:859–865. © 2016 Wiley Periodicals, Inc.