5fyd

Publication Abstract from PubMed

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 7beta-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 7alpha-hydroxysteroid dehydrogenase provides a rationale for the opposite stereoselectivity. The presence of a C-terminal extension reshapes the substrate site of the beta-selective enzyme, possibly leading to an inverted orientation of the bound substrate. This article is protected by copyright. All rights reserved.

Structural and biochemical insights into 7beta-hydroxysteroid dehydrogenase stereoselectivity.,Savino S, Ferrandi EE, Forneris F, Rovida S, Riva S, Monti D, Mattevi A Proteins. 2016 Mar 23. doi: 10.1002/prot.25036. PMID:27006087^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.