Elucidating the functional significance of catalytic and chitin-binding domains for the anti-cancer property of a bacterial endochitinase.

ABSTRACT: Chitinases are enzymes that facilitate the breakdown of chitin and also interact with carbohydrate moieties such as heparin sulphate due to structural similarity with chitin, thereby influencing cell adherence and migration. Bacterial endo-chitinase contains several domains, such as a catalytic domain, an FNIII domain, and a chitin-binding domain. Recent studies have demonstrated the anti-cancer property of catalytically active chitinases; however, the mechanism and targets have not yet been explored. Therefore, this study investigates the importance of the catalytic and chitin-binding domains of a bacterial endo-chitinase (ChiC) for the anti-cancer property by creating domain-specific mutants. Initially, an in silico study identified an evolutionarily conserved tryptophan (W300) within th

SUBMITTER: Shrivastava A 

PROVIDER: S-EPMC12550298 | biostudies-literature | 2025 Dec

REPOSITORIES: biostudies-literature