Enzyme Activity Measurement for Beta-Galactoside Alpha-2,3-Sialyltransferase

Creative Enzymes is an industrial biotech company providing high-quality bioanalytical services and contract research specialized in enzyme activity assays. We partner with diverse and unique customers to support their process optimization needs. All the activity assays are performed in a professional and timely manner, controlled by standardized processes. Herein, Creative Enzymes offers the accurate and reproducible enzymatic activity assay for beta-galactoside alpha-2,3-sialyltransferase.

Beta-galactoside alpha-2,3-sialyltransferase (EC 2.4.99.4) is an enzyme that catalyzes the transfer of CMP-N-acetylneuraminate to the β-D-galactosyl-1,4-N-acetyl-D-glucosaminyl termini on glycoproteins. This enzyme was found in viruses and cellular organisms. And this enzyme belongs to the family of transferases, specifically those glycosyltransferases that do not transfer hexosyl or pentosyl groups. The enzyme is one of the four sialyltranaferases that catalyze the biosynthesis of sialylated glycoconjugates. Although all sialyltransferases share cytidine monophosphate N-acetylneuraminic acid (CMP-Neu5Ac) as the common donor substrate, they are classified into four families according to the carbohydrate linkages they synthesize: beta-galactoside alpha-2,3-sialyltransferase (EC 2.4.99.4), beta-galactoside alpha-2,6-sialyltransferases (EC 2.4.99.1), GalNAc alpha 2,6-sialyltransferase (EC 2.4.99.3), and alpha 2,8-sialyltransferase (EC 2.4.99.8).

Sialic acids are vital components of carbohydrate chains and are linked to terminal positions of the carbohydrate moiety of glycoconjugates, including glycoproteins and glycolipids. Studies on the structure-function relationship of sialic acids have revealed that N-acetylneuraminic acid (Neu5Ac) is a major sialic acid component of glycoconjugates, and that the sialylated carbohydrate chains of glycoconjugates play significant roles in many biological processes, including immunological responses, viral infections, cell–cell recognition, and inflammation. Thefore, sialyltransferases, which control the production of sialylated glycoconjugates, are critical to regular biological activities. Beta-galactoside alpha-2,3-sialyltransferase has already gained a pivotal role in pharmaceutical industry. For instance, this enzyme can serve as a therapeutic target of taxol therapy. This enzyme is also a drug target for modulating leukocyte trafficking in human disorders, including autoimmune diseases and cancer. Besides, this enzyme was shown to be related to prostate cancer. Thus, beta-galactoside alpha-2,3-sialyltransferase is attracting an ever-increasing interest for its critical functions in medical research.

Creative Enzymes has engaged in the service of enzyme activity measurement for many years. We are fully competent to perform the activity assay for beta-galactoside alpha-2,3-sialyltransferase. For details, the enzymatic activity assays of the enzyme could be conducted in 100mM Tris-HCl buffer, pH 8.0, containing CMP-Neu5Ac (1mM) and Lac-b-O-MU (1mM). The content of the substrate is analyzed using high-performance liquid chromatography (HPLC) with a fluorescence detector (excitation at 325nm and emission at 372nm).

Equipped with the most advanced instruments, Creative Enzymes is well known for the rapid and accurate activity measurement services. We offer the technical support and personalized customer service of the best level in the industry.

Figure: The crystal structure of beta-galactoside alpha-2,3-ialyltransferase from a luminous marine bacterium, Photobacterium phosphoreum.
PDB: 2ZWI