β-Glucoronidase Inhibitors

Chemical inhibitors of β-Glucuronidase can exert their inhibitory action through various mechanisms, primarily by mimicking the structure of the enzyme's natural substrates or by binding to its active site, thereby preventing the catalysis of reactions involving the hydrolysis of glucuronides. Saccharolactone is a prime example, as it competes with the natural substrates of β-Glucuronidase for the active site, effectively blocking it. Similarly, D-Saccharic acid 1,4-lactone engages in competitive inhibition with β-Glucuronidase, which prevents the enzyme from breaking down its usual substrates.

Further, Glycyrrhetinic acid and D-Glucuronic acid also function as competitive inhibitors due to their structural resemblance to the enzyme's substrates, which allows them to occupy the active site of β-Glucuronidase, reducing its activity. L-Ascorbic acid reduces the enzyme's activity by competing with natural substrates at the active site. On the other hand, flavonoids such as Hesperidin, Quercetin, Baicalein, and Chrysin inhibit β-Glucuronidase by directly binding to the enzyme. Their inhibitory action is rooted in their ability to prevent the interaction between β-Glucuronidase and its substrates, with Quercetin and Baicalein specifically known for their competitive binding at the enzyme's active site. Emodin inhibits β-Glucuronidase by a similar mechanism, interacting with the active site and thus preventing normal enzymatic function. These inhibitors collectively encompass a range of structures and origins, but all converge on the common outcome of inhibiting the function of β-Glucuronidase by preventing substrate processing through competitive and non-competitive mechanisms.