Chitinase B (Serratia marcescens) (ChiB)

Chitinase B from *Serratia marcescens* (ChiB) is an extracellular bacterial enzyme that catalyzes the hydrolysis of chitin, one of the most abundant natural polysaccharides[1][3][6][7]. The enzyme consists of a catalytic domain with a TIM-barrel fold, a flexible linker region, and a C-terminal chitin-binding domain required for efficient substrate interaction[1]. It is classified as a family 18 glycoside hydrolase and demonstrates exochitinase activity, cleaving chitin from the nonreducing end to generate oligomeric products[1][3][7]. Chitinase B acts synergistically with other chitinases (such as ChiA and ChiC) to enhance chitin degradation, a key process for nutrient acquisition in the environment and biotechnological applications such as the conversion of chitinous waste[1][3][5][6][7]. Berberine has been structurally observed in complex with ChiB[4], but there are no known approved inhibitors or drugs that specifically target this enzyme for therapeutic purposes. Caveats: - The enzyme is not a recognized therapeutic target or biomarker in clinical practice. - While it interacts with some small molecules (e.g., berberine in structural studies), their biological or clinical relevance remains investigational. - No human safety concerns are present, as this enzyme arises from bacteria and is mainly of biotechnological and microbiological interest.

Other names

SmChiBExochitinase BChitinase II

Endo- and exo-hydrolytic cleavage of β-1,4-glycosidic bonds in chitin chains, releasing chitooligosaccharides