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Enzyme Activity Measurement for 3-Galactosyl-N-Acetylglucosaminide 4-Alpha-L-Fucosyltransferase Using Chromatographic Assays

Creative Enzymes is an industrial biotech company specialized in enzyme activity assays. We partner with our diverse and unique customers to support them for processes and optimization. True to our company tradition, we firmly believe that the quality of services and products is the basic requirement for our corporate success. Here, Creative Enzymes is proud to provide chromatographic activity assays for 3-galactosyl-N-acetylglucosaminide 4-alpha-L-fucosyltransferase.

3-Galactosyl-N-acetylglucosaminide 4-alpha-L-fucosyltransferase (EC, a type II transmembrane glycoprotein, is a glycosyltransferase that catalyzes the transfer of fucose (Fuc) onto type 1 and type 2 carbohydrate determinants in α-1,4- and α-1,3- linkages, therefore participating in the synthesis of the carbohydrate adhesion structures, the Lewis (Le) determinants: Lea, sialyl-Lea, Leb, Lex, sialyl-Lex, and Ley. The enzyme functions in vitro to fucosylate oligosaccharides, glycolipids, glycopeptides, and glycoproteins. Importantly, this enzyme plays a pivotal role in three metabolic pathways, the glycosphingolipid biosynthesis - lacto series, glycosphingolipid biosynthesis - neo lacto series, and glycan structures biosynthesis 2 pathway.

Figure 1: Enzyme Activity Measurement for Glycosyl, Hexosyl, and Pentosyl Transferases Figure 1: The reaction catalyzed by 3-galactosyl-N-acetylglucosaminide 4-alpha-L-fucosyltransferase. (From MetaCyc)

Fucosylated glycans of the Lewis type mediate important processes, such as cell recognition and adhesion occurring in inflammation and metastases formation. 3-Galactosyl-N-acetylglucosaminide 4-alpha-L-fucosyltransferase can be used for the in vitro synthesis of glycomimetics that inhibit these processes. Furthermore, the valuable information on the catalytic mechanism of the enzyme would build a base for the design of specific fucosyltransferase inhibitors. Additionally, the enzyme from Helicobacter pylori possesses a broad tolerance toward nonnatural type I acceptor substrate analogs and therefore it represents a value for the chemoenzymatic synthesis of Lewis A, sialyl Lewis A, as well as mimetics. Thus, 3-galactosyl-N-acetylglucosaminide 4-alpha-L-fucosyltransferase is attracting researchers’ interests as a catalyst in biosynthesis. That is to say, it is very important to first be able to monitor the activity of 3-galactosyl-N-acetylglucosaminide 4-alpha-L-fucosyltransferase.

Fortunately, Creative Enzymes offers reliable and rapid activity measurement for 3-galactosyl-N-acetylglucosaminide 4-alpha-L-fucosyltransferase using the chromatographic assay. Creative Enzymes is a leading company of high-quality bioanalytical services and contract research specialized in enzyme activity analysis. We have served countless clients from all over the world. Our prompt service, good customer care, and dedicated resources have made us the most preferred vendor to our competitors. We believe that working closely with our customers is integral to our workflow due to the technical nature of enzymes.

Figure 2: The  crystal structure of human 3-galactosyl-N-acetylglucosaminide  4-alpha-L-fucosyltransferase Figure 2: The crystal structure of human 3-galactosyl-N-acetylglucosaminide 4-alpha-L-fucosyltransferase.
Uniport: P21217

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SourceE. coli
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