Glycosylation enzymology is the study of the enzymes and reaction mechanisms that construct, process, or remodel glycans and glycoconjugates. Glycosyltransferases and glycosidases collectively establish the carbohydrate structures attached to proteins and lipids [1]. Glycosyltransferases form glycosidic bonds by transferring a sugar group from an activated donor to an acceptor, with substrate recognition determining linkage position and stereochemical outcome [2]. For protein glycosylation, successive reactions are organized within cellular compartments and participate in both initial glycan assembly and later processing [3]. Catalytic mechanisms involve positioning of the donor and acceptor, stabilization of charged intermediates or transition states, and conformational changes in bound sugar residues. Kinetic and structural analysis connects these individual reactions to the enzyme networks producing a particular glycan population [4].
- glycosyltransferases
- glycosidic bonds
- glycan processing
- substrate specificity
References
- Kazuaki Ohtsubo; Jamey D. Marth; Glycosylation in Cellular Mechanisms of Health and Disease. Cell 2006, 126, 855-867, 10.1016/j.cell.2006.08.019.
- L.L. Lairson; B. Henrissat; G.J. Davies; S.G. Withers; Glycosyltransferases: Structures, Functions, and Mechanisms. Annu. Rev. Biochem. 2008, 77, 521-555, 10.1146/annurev.biochem.76.061005.092322.
- Kelley W. Moremen; Michael Tiemeyer; Alison V. Nairn; Vertebrate protein glycosylation: diversity, synthesis and function. Nat. Rev. Mol. Cell Biol. 2012, 13, 448-462, 10.1038/nrm3383.
- Albert Ardèvol; Carme Rovira; Reaction Mechanisms in Carbohydrate-Active Enzymes: Glycoside Hydrolases and Glycosyltransferases. Insights from ab Initio Quantum Mechanics/Molecular Mechanics Dynamic Simulations. J. Am. Chem. Soc. 2015, 137, 7528-7547, 10.1021/jacs.5b01156.