Structural Snapshots of α-1,3-Galactosyltransferase with Native Substrates: Insight into the Catalytic Mechanism of Retaining Glycosyltransferases.

@article{AlbesaJov2017StructuralSO,
  title={Structural Snapshots of α-1,3-Galactosyltransferase with Native Substrates: Insight into the Catalytic Mechanism of Retaining Glycosyltransferases.},
  author={David Albesa-Jov{\'e} and Mar{\'i}a {\'A}ngela Sainz-Polo and Alberto Marina and Marcelo E Guerin},
  journal={Angewandte Chemie},
  year={2017},
  volume={56 47},
  pages={14853-14857}
}
Glycosyltransferases (GTs) are a key family of enzymes that catalyze the synthesis of glycosidic bonds in all living organisms. The reaction involves the transfer of a glycosyl moiety and can proceed with retention or inversion of the anomeric configuration. To date, the catalytic mechanism of retaining GTs is a topic of great controversy, particularly for those enzymes containing a putative nucleophilic residue in the active site, for which the occurrence of a double-displacement mechanism has… CONTINUE READING

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