Sugar conformations that enhance cleavage of glycosidic bonds in carbohydrate-active enzymes

Document typeConference report
Defense date2015-05-05
PublisherBarcelona Supercomputing Center
Rights accessOpen Access
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is licensed under a Creative Commons license
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Attribution-NonCommercial-NoDerivs 3.0 Spain
Abstract
Carbohydrate-active enzymes select particular
conformations of one sugar of their carbohydrate substrates to
enhance catalysis. The evolution of this conformation during
catalysis, known as the catalytic itinerary, is of fundamental interest
in glycobiology. Here we calculate the free energy landscape of β-
xylose to predict the possible catalytic itineraries of β-xylan enzymes.
Our results discard one of the three catalytic itineraries proposed on
the basis of X-ray structures of mutant enzymes. Additional classical
and quantum mechanics/molecular mechanics (QM/MM)
calculations indicate that complexes obtained from modified enzymes
do not necessarily represent the structures that take place in the
reaction coordinate.
CitationRaich, Lluís; Rovira, Carme. Sugar conformations that enhance cleavage of glycosidic bonds in carbohydrate-active enzymes. A: "BSC Doctoral Symposium (2nd: 2015: Barcelona)". 2nd ed. Barcelona: Barcelona Supercomputing Center, 2015, p. 97-98.
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