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Enzyme Activity Measurement for N-Acylneuraminate Cytidylyltransferase

Creative Enzymes is an industrial biotech company specialized in enzyme activity assays. We partner with diverse and unique customers to support their needs in fundamental research to process optimization. By constantly striving for services of utmost quality, Creative Enzymes has earned the trust of many customers. We are one of the few companies that provide the highly accurate activity assay for N-acylneuraminate cytidylyltransferase.

Sialic acids are involved in a wide range of signaling, recognition, and cell-cell adhesion phenomena in mammalian cells and are over-expressed in some highly malignant tumors. It has been shown that the altered physiological levels of sialic acids can be closely related to some genetic disorders. Clearly, the mechanism of production of sialic acid-containing glycoconjugates is of clinical interests. N-acylneuraminate cytidylyltransferase (EC 2.7.7.43; CTP:N-acylneuraminate cytidylyltransferase; CMP-Neu5Ac synthetase) is an enzyme that catalyzes the penultimate step in the addition of sialic acids to the oligosaccharide component of glycoconjugates and is a required component of sialylation pathways. This enzyme catalyzes the reaction of N-acetylneuraminic acid (NeuAc) with cytidine-5-triphosphate (CTP) to produce a pyrophosphate (PPi) and CMP-N-acetylneuraminic acid (CMP-NeuAc), an “activated” sugar nucleotide monophosphate. This reaction is unique because sialic acid is directly coupled to cytosine monophosphate. N-acylneuraminate cytidylyltransferase has been isolated from both mammalian and bacterial sources. Although bacterial and eukaryotic N-acylneuraminate cytidylyltransferases share several common catalytic properties, many critical differences have been studied, including the substrate specificity, tertiary structure, inhibitor sensitivity, and cellular localization. Thus, bacterial N-acylneuraminate cytidylyltransferases can be targeted by rational drug design strategies.

Enzyme Activity Measurement for N-Acylneuraminate Cytidylyltransferase Figure 1: Enzymatic synthesis of CMP-NeuAc by N-acylneuraminate cytidylyltransferase (CMP-Neu5Ac synthetase).
Reference: Kittelmann M, Klein T, Kragl U, et al. Applied microbiology and biotechnology, 1995, 44(1-2): 59-67.

Additionally, N-acylneuraminate cytidylyltransferase also gains attentions in the field of biotechnology. Given the expense of chemically synthesizing CMP-NeuAc and its instability, N-acylneuraminate cytidylyltransferase in company with various sialyltransferases are vital for the enzymatic synthesis of biologically relevant, sialylated oligosaccharides. These sialylated oligosaccharides are used in clinical medicine and invaluable tools for the study of the various processes that require sialic acids. Therefore, it can be concluded that N-acylneuraminate cytidylyltransferase has a huge potential in the future discoveries in medicine and biotechnology.

Nonetheless, the activity assay of N-acylneuraminate cytidylyltransferase using chromatographic assay has not been well established on an industrial scale, although the chromatographic assay is considered to be the reliable and cost-effective method for activity quantification. Fortunately, as a globally recognized leader in the field of the enzyme activity measurement, Creative Enzymes has developed precise activity assays for N-acylneuraminate cytidylyltransferase. The quality of our results is assured with the most advanced chromatographic instruments. Ultimately, Creative Enzymes is your trustworthy partner who will certainly provide the best service experience in the global market.

Enzyme Activity Measurement for N-Acylneuraminate Cytidylyltransferase Figure 2: The crystal structure of murine N-acylneuraminate cytidylyltransferase.
PDB: 1QWJ



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Related Products
CatalogEXWM-3255
EC No.EC 2.7.7.43
CAS No.9067-82-7
Source
CatalogNATE-0023
EC No.EC 2.7.7.43
CAS No.9067-82-7
SourceE. coli BL21
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