Creative Enzymes is proud to be one of the few international companies specifically developing and performing enzyme activity assays. Our research center stands out with the most advanced equipment, rich experiences, and a superb expert team, which assure high reproducibility and accuracy for the activity measurement. Herein, we are fully prepared to provide the accurate enzyme activity assay for thioglucosidases.

Thioglucosidases (also known as myrosinases or thioglucoside glucohydrolases, EC 3.2.1.147, formerly EC 3.2.3.1) are a group of enzymes that catalyze the hydrolysis of glucosinolates, the secondary plant metabolites, yielding D-glucose and an unstable aglycone intermediate. The aglycone intermediate will further react enzymatically or non-enzymatically to form several different products. A variety of products can be formed depending on the local environment, including isothiocyanates, thiocyanates, epithionitriles, and nitriles. These degradation products may have various biological effects such as toxicity. They are demonstrated to serve as a defense system against insect herbivore attack but can also act as attractants for specialist insects for feeding and oviposition on the plant. Thioglucosidases are stored physically separate from the glucosinolates in the plant. Upon tissue disruption, by mastication or pest attack, thioglucosidases get in contact with glucosinolates and hydrolysis occurs. It is noted that the myrosinase/glucosinolate system is characteristic of all members of the Brassicaceae family. As a critical part of the defense system of plants, the enzyme is present in multiple forms. About thirty isoforms of thioglucosidases have been predicted in oilseed rape, and classified into three subfamilies: MA, MB, and MC, based on their sequence homology.

Thioglucosidases belong to family 1 of the glycoside hydrolase (GH) superfamily and are the only known S-glycosidases. The active sites of thioglucosidases are very similar to that of O-glycosidases, operating via the overall retention mechanism. The common mechanism and unique catalytic activity arouse the interest of many researchers, aiming at understanding the activity determining structures and engineering for other specific catalytic activities. These studies significantly promote a strong demand for efficiently and accurately monitoring the activity of thioglucosidases.

Creative Enzymes provides the most precise enzymatic activity quantitation for thioglucosidases. For example, the enzyme activity can be assayed spectrophotometrically using our highly pure substrate, which has been demonstrated to contribute to the accuracy of the activity assay. Overall, Creative Enzymes has been always chasing the highest level of customers satisfaction through constant improvement in serve quality and customer care.

Figure: The crystal structure of thioglucosidase from Sinapis alba.
PDB: 1E4M