Comprehensive enzymatic characterization of glycosyltransferases with a beta3GT or beta4GT motif.
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.
Togayachi
Akira
A
Glycogene Function Team of Research Center for Glycoscience, National Institute of Advanced Industrial Science and Technology (AIST), Ibaraki, Japan.
Sato
Takashi
T
Narimatsu
Hisashi
H
D020816:Amino Acid Motifs; D019295:Computational Biology; D005700:Galactosyltransferases; D016695:Glycosyltransferases / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D006801:Humans; D013379:Substrate Specificity
D016695:Glycosyltransferases; C479886:B3GALT5 protein, human; D005700:Galactosyltransferases; C493310:beta1,4-galactosyltransferase, human