A computational and experimental study of O-glycosylation. Catalysis by human UDP-GalNAc polypeptide:GalNAc transferase-T2
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Title
A computational and experimental study of O-glycosylation. Catalysis by human UDP-GalNAc polypeptide:GalNAc transferase-T2
Authors
Keywords
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Journal
ORGANIC & BIOMOLECULAR CHEMISTRY
Volume 12, Issue 17, Pages 2645-2655
Publisher
Royal Society of Chemistry (RSC)
Online
2014-02-19
DOI
10.1039/c3ob42569j
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Note: Only part of the references are listed.- Formation of a Covalent Glycosyl-Enzyme Species in a Retaining Glycosyltransferase
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- Geometric Attributes of Retaining Glycosyltransferase Enzymes Favor an Orthogonal Mechanism
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- Site-specific protein O-glycosylation modulates proprotein processing — Deciphering specific functions of the large polypeptide GalNAc-transferase gene family
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- Essential role of glutamate 317 in galactosyl transfer by α3GalT: a computational study
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- Retaining Glycosyltransferase Mechanism Studied by QM/MM Methods: Lipopolysaccharyl-α-1,4-galactosyltransferase C Transfers α-Galactose via an Oxocarbenium Ion-like Transition State
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- Mechanistic evidence for a front-side, SNi-type reaction in a retaining glycosyltransferase
- (2011) Seung Seo Lee et al. Nature Chemical Biology
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- (2010) James C. Errey et al. ANGEWANDTE CHEMIE-INTERNATIONAL EDITION
- Trapping and characterization of covalent intermediates of mutant retaining glycosyltransferases
- (2010) Naoto Soya et al. GLYCOBIOLOGY
- Evaluation of Density Functionals and Basis Sets for Carbohydrates
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- QM/MM simulations predict a covalent intermediate in the hen egg white lysozyme reaction with its natural substrate
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