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David Albesa‐Jov Fernanda Mendoza Ane Rodrigo‐Unzueta Fernando Gomolln‐Bel Javier O. Cifuente Saioa Urresti Natalia Comino Hansel Gmez Javier Romero‐García Jos M. Lluch Enea Sancho‐Vaello Xevi Biarns Antoni Planas Pedro Merino Laura Masgrau Marcelo E. Guerin 《Angewandte Chemie (Weinheim an der Bergstrasse, Germany)》2015,127(34):10036-10040
Glycosyltransferases (GTs) comprise a prominent family of enzymes that play critical roles in a variety of cellular processes, including cell signaling, cell development, and host–pathogen interactions. Glycosyl transfer can proceed with either inversion or retention of the anomeric configuration with respect to the reaction substrates and products. The elucidation of the catalytic mechanism of retaining GTs remains a major challenge. A native ternary complex of a GT in a productive mode for catalysis is reported, that of the retaining glucosyl‐3‐phosphoglycerate synthase GpgS from M. tuberculosis in the presence of the sugar donor UDP‐Glc, the acceptor substrate phosphoglycerate, and the divalent cation cofactor. Through a combination of structural, chemical, enzymatic, molecular dynamics, and quantum‐mechanics/molecular‐mechanics (QM/MM) calculations, the catalytic mechanism was unraveled, thereby providing a strong experimental support for a front–side substrate‐assisted SNi‐type reaction. 相似文献