Dual reaction mechanism of glycosyltransferase GlfT2 from Mycobacterium Tuberculosis

Varování

Publikace nespadá pod Fakultu sportovních studií, 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