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Enzyme Activity Measurement for Beta-N-Acetylhexosaminidase

Creative Enzymes is proud to provide a variety of enzyme activity assays for customers from different industries. We are committed to the most reliable enzymatic measurement in the global market. Our quality and productivity is assured by advanced analytical instrument and standardized quality control. Among all of our accurate activity quantification services, analysis of beta-N-acetylhexosaminidase has been a widely welcomed one.

Beta-N-acetylhexosaminidase (EC 3.2.1.52; formerly EC 3.2.1.29 and EC 3.2.1.30; beta-N-acetyl-D-hexosaminide N-acetylhexosaminohydrolase) is an exo-type enzyme that hydrolyzes N-acetylhexosaminides at the non-reducing end, whereby an N-acetylhexosamine, usually N-acetylglucosamine (GlcNAc) or N-acetylgalactosamine (GalNAc), is released. The enzyme that catalyzes the cleavage of β-N-acetylglucosaminide is also known as β-N-acetylglucosaminidase, while an enzyme specifically for β-N-acetylgalactosaminide has not been detected or identified. In general, β-N-acetylhexosaminidases hydrolyze the β-glycosides of N-acetylglucosaminide and N-acetylgalactosaminide; they are not specific for the aglycone group, although they prefer aryl substituents. These enzymes are widely distributed in nature and have now been detected in animal tissues, microorganisms, and plants. β-N-acetylhexosaminidases are thought to involved in the processing and turnover of glycoproteins during germination in plants; they are considered to function in the metabolism of N-glycans during ripening in apple fruits. On the other hand, some plant β-N-acetylhexosaminidases also degrade chitin and chitin oligomers. Therefore, their participation in the defense system, against chitinous pathogens in plants, has been suggested. However, since the natural substrate of β-N-acetylhexosaminidase has not been identified in plants and substrate specificity has been examined only for a limited number of compounds, the physiological significance of the enzyme has yet to be elucidated.

In humans, there are two major β-N-acetylhexosaminidase isoforms: HexA is composed of a heterodimer of the α and β subunits, and HexB is composed of a homodimer of two β subunits. Note that, a genetic deficiency of β-N-acetylhexosaminidase can cause Tay-Sachs disease or Sandhoff disease. Therefore, it has clinical significance to further investigate the functions and action mechanisms of β-N-acetylhexosaminidase, which relies on accurately monitoring the enzyme activity.

Creative Enzymes is experienced in performing precise enzymatic assays for β-N-acetylhexosaminidases, which is determined by spectrophotometric assays. For details, the enzyme activity is assayed by measuring the release of p-nitrophenol from pNP-β-GlcNAc. The amount of liberated p-nitrophenol is determined ty tracking the absorbance at 405 nm. Our test results are the most trusted and proven, due to a superb expert team. Overall, Creative Enzymes is your best partner for virtually all enzyme analysis services.

The crystal structure of beta-N-acetylhexosaminidase from Arthrobacter aurescens. Figure: The crystal structure of beta-N-acetylhexosaminidase from Arthrobacter aurescens.
PDB: 3RCN



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