The complete conformational free energy landscape of β-xylose reveals a two-fold catalytic itinerary for β-xylanases.

ABSTRACT: Unraveling the conformational catalytic itinerary of glycoside hydrolases (GHs) is a growing topic of interest in glycobiology, with major impact in the design of GH inhibitors. β-xylanases are responsible for the hydrolysis of glycosidic bonds in β-xylans, a group of hemicelluloses of high biotechnological interest that are found in plant cell walls. The precise conformations followed by the substrate during catalysis in β-xylanases have not been unambiguously resolved, with three different pathways being proposed from structural analyses. In this work, we compute the conformational free energy landscape (FEL) of β-xylose to predict the most likely catalytic itineraries followed by β-xylanases. The calculations are performed by means of ab initio metadynamics, using the Cremer-Popl

SUBMITTER: Iglesias-Fernandez J 

PROVIDER: S-EPMC5811086 | biostudies-literature | 2015 Feb

REPOSITORIES: biostudies-literature