Publication details

Dual reaction mechanism of glycosyltransferase GlfT2 from Mycobacterium Tuberculosis

Authors

JANOŠ Pavel KOZMON Stanislav TVAROŠKA Igor KOČA Jaroslav

Year of publication 2018
Type Conference abstract
MU Faculty or unit

Central European Institute of Technology

Citation
Description Glycosyltransferases are enzymes that catalyze the transfer of saccharide units and the formation of glycosidic bonds. Galactofuranosyltransferase 2 (GlfT2) is a key glycosyltransferase from Mycobacterium Tuberculosis. It catalyzes the transfer of galactofuranosyl (Galf) unit from donor substrate UDP-Galf onto a growing polysaccharide chain in alternating beta-(1-5) or beta-(1-6) linkages. The resulting galactan is a key part of the mycobacterial cell wall. GlfT2 is an interesting glycosyltransferase from a mechanistic point of view as well. It has a dual activity and works in processive manner switching the beta-(1-5) or beta-(1-6) mechanisms between steps. In order to study the two mechanisms of GlfT2 we have employed QM/MM Ab Initio MD using CPMD. Metadynamics is used to provide overview of the free energy landscape of the beta-(1-6) reaction and string method is used to obtain a minimum free energy paths for both beta-(1-6) and beta-(1-5) reactions. We show that both reactions proceed very similarly and feature similar transition-state structures.
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