Related Experiment Video
Updated: Jul 18, 2026

Identification and Characterization of Protein Glycosylation using Specific Endo- and Exoglycosidases
Published on: December 26, 2011
Comprehensive enzymatic characterization of glycosyltransferases with a beta3GT or beta4GT motif
Akira Togayachi1, Takashi Sato, Hisashi Narimatsu
1Glycogene Function Team of Research Center for Glycoscience, National Institute of Advanced Industrial Science and Technology (AIST), Ibaraki, Japan.
Abstract:
Bioinformatics is a very powerful tool in the field of glycoproteomics, as well as genomics and proteomics. The bioinformatics technique accelerates the comprehensive identification and in silico cloning of human glycogenes containing glycosyltransferases, glycolytic enzymes, sugar-nucleotide synthetases, sugar-nucleotide transporters, and so forth. Glycosyltransferase genes play central roles in carbohydrate chain biosynthesis and have been analyzed for their biological functions. At present, over 180 human glycosyltransferases were identified, cloned, and expressed in various expression systems to detect the activity for carbohydrate synthesis. The recombinant proteins for glycosyltransferase were successfully identified for their enzyme activities and substrate specificities. Their substrate specificities were determined using various donor substrates and acceptors. This section reviews the functions, substrate specificities, and enzymatic reactions of glycosyltransferases such as beta1,3-glycosyltransferase family and beta1,4-glycosyltransferase family.
Related Concept Videos
Oligosaccharide Assembly
Multiple sugar molecules that may or may...
Protein Glycosylation
Glycosylation occurs in...
Protein Folding Quality Check in the RER
