Publication details
Dual reaction mechanism of glycosyltransferase GlfT2 from Mycobacterium Tuberculosis
| Authors | |
|---|---|
| Year of publication | 2018 |
| Type | Conference abstract |
| MU Faculty or unit | |
| 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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