Dual reaction mechanism of glycosyltransferase GlfT2 from Mycobacterium Tuberculosis

Varování

Publikace nespadá pod Ekonomicko-správní fakultu, ale pod Středoevropský technologický institut. Oficiální stránka publikace je na webu muni.cz.

Autoři	JANOŠ Pavel KOZMON Stanislav TVAROŠKA Igor KOČA Jaroslav
Rok publikování	2018
Druh	Konferenční abstrakty
Fakulta / Pracoviště MU	Středoevropský technologický institut
Citace
Popis	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.
Související projekty:	CEITEC 2020