Chitinase ()

Chitinase Overview

Chitinase is an enzyme that catalyzes the hydrolytic cleavage of β-1,4-glycosidic bonds in chitin, a major structural polysaccharide found in the exoskeletons of arthropods (e.g., insects, crustaceans) and fungal cell walls. There are multiple chitinase enzyme families, notably family 18, 19, and 20 glycoside hydrolases, with family 18 found in bacteria, fungi, insects, and mammals, and family 19 mainly in plants[3][5][7][8]. Chitinases are structurally diverse but generally possess a modular architecture including a catalytic domain and, in some forms, a chitin-binding domain[4][5][7]. Their primary function is chitin degradation, involved in nutrient recycling in nature and defense against chitin-containing pathogens in plants and animals[2][5][9]. In humans, active chitinases such as chitotriosidase also play a role in immune responses and have been implicated in diseases such as asthma, allergies, and serve as biomarkers in Gaucher’s disease[3][7]. Drug modulation of chitinase activity is being explored for antifungal and anti-inflammatory therapies, though no approved drugs are currently available for direct chitinase inhibition.

Mechanism of Action

Chitinase inhibitors block chitinase enzymatic activity, thereby reducing the breakdown of chitin; proposed as antifungal, anti-allergic, or anti-asthmatic mechanisms[3]

Biological Functions

Safety Considerations

Interacting Drugs

Associated Biomarkers