Enzyme Activity Measurement for Beta-N-Acetylglucosaminyl-Glycopeptide Beta-1,4-Galactosyltransferase Using Spectrophotometric Assays

Through working closely with our countless customers, Creative Enzymes has learned thatt he ability of providing high-quality services and delivery of these services on time are our top priority. With years of exploring and developing enzyme assays, Creative Enzymes has become a worldwide leader in the supply of such services. We are capable of activity quantification for a wide range of enzymes, including beta-N-acetylglucosaminylglycopeptide beta-1,4-galactosyltransferase.

Beta-N-acetylglucosaminylglycopeptide beta-1,4-galactosyltransferases (EC 2.4.1.38; GalT) are a family of glycosyltransferases that participates in the biosynthesis of the oligosaccharide part of glycoproteins and glycolipids. The enzymes catalyze the specific transfer of galactose from UDP-galactose to a non-reducing terminal N-acetyl-D-glucosamine, forming a β-1,4-glycosidic linkage. Galactosyltransferase is a membrane-bound glycoprotein that is localized to the trans compartment of the Golgi membranes. Beta-N-acetylglucosaminylglycopeptide beta-1,4-galactosyltransferases exist not only in eukaryotes but also in bacteria, such as human, rat, and Neisseria gonorrhoeae. Beta-N-acetylglucosaminylglycopeptide beta-1,4-galactosyltransferases are involved in various pathways, which are involved in various types of N-glycan biosynthesis and glycosaminoglycan biosynthesis. The beta-N-acetylglucosaminylglycopeptide beta-1,4-galactosyltransferase family consists of seven members, from GalT I to GalT VII.

The carbohydrate moieties of cell surface glycoconjugates play an important role in cell adhesion and metastasis. One of the most prominent transformation-associated changes in the sugar chains of glycoproteins is increases in the ratio of large N-glycans in cell surface glycoproteins. Beta-N-acetylglucosaminylglycopeptide beta-1,4-galactosyltransferases are the enzymes responsible for this change. Thus, the enzymes rise a significant function in metabolism and biosynthesis. Additionally, beta-N-acetylglucosaminylglycopeptide beta-1,4-galactosyltransferases serve as a critical role in the pharmaceutical industry and medical research. The enzymes can be used as the target for drug design and β-1,4-Galactosyltransferase V (GalT V) may represent an important target for glioma therapy. Therefore, beta-N-acetylglucosaminylglycopeptide beta-1,4-galactosyltransferases attract an ever-increasing interest for their functional significance, and monitoring the activity of these enzymes is vital for the fundamental research and should shed light on the design of new drugs.

Fortunately, Creative Enzymes is capable of the most accurate activity assay for beta-N-acetylglucosaminylglycopeptide beta-1,4-galactosyltransferases. Possessing the superb technology, professional knowledge, and advanced equipment, Creative Enzymes can supply our customers with the top-ranked technical support and personalized customer service found nowhere else in the industry.

Figure: The crystal structure of human Beta-1,4-galactosyltransferase I.
PDB: 3EE5