Work

Protein flexibility drives sugar rotation and high substrate promiscuity in a GDP-sugar 4-epimerase

Year: 2025

Type: article

Abstract: UDP-galactose 4-epimerases (Gal4Es) catalyze the inversion of the 4-hydroxyl configuration of a sugar moiety from an NDP-sugar through a three-step process: oxidation, rotation and reduction. Despite extensive biochemical and structural studies, the role of protein dynamics on substrate specificity remains poorly understood. The recently identified subgroup of GDP-sugar 4-epimerases, notable for its exceptional substrate promiscuity, provides an intriguing model to investigate the role of dynamics in the Gal4E catalytic mechanism and the unique promiscuity of the subgroup.

Source: Computational and Structural Biotechnology Journal

DOI: 10.1016/j.csbj.2025.05.037

Authors: Carlos Josué Alvarez Quispe, Koen Beerens, Andy-Mark W.H. Thunnissen, Xevi Biarnés, Antoni Planas, Tom Desmet

Institutions: Ghent University, University of Groningen, Institut Químic de Sarrià, Universitat Ramon Llull

Language: English

Topic: Protein Structure and Dynamics

Subfield: Molecular Biology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: gold

Estimated APC paid: $3,230