Carbohydrate-binding module 17 (CBM17)

Carbohydrate-binding module 17 (CBM17) is a non-catalytic protein domain found in various bacterial carbohydrate-active enzymes, particularly family 5 glycoside hydrolases such as endoglucanases [1, 2]. It belongs to the type-B CBM category, which is characterized by a shallow binding cleft that specifically recognizes and binds to the beta-1,4-glucan chains of non-crystalline (amorphous) cellulose and soluble cellooligosaccharides [3, 14]. Structurally, CBM17 adopts a beta-sandwich fold, often stabilized by calcium ions, and utilizes aromatic and polar amino acid residues to facilitate substrate interaction through CH-pi stacking and hydrogen bonding [14, 30]. Its primary biological function is to anchor the associated catalytic enzyme to the carbohydrate substrate, thereby increasing the local concentration of the enzyme and enhancing the efficiency of polysaccharide degradation [1, 35]. While CBM17 is not a direct therapeutic target for human diseases, it is extensively utilized in biotechnology as a molecular probe for visualizing cellulose accessibility in plant cell walls [18, 31]. Furthermore, it is a key component in the development of "designer" enzymes and multi-enzyme complexes for biomass conversion and biofuel production [20, 34]. Recent research has also explored its use as a targeting moiety in drug delivery systems for treating bacterial biofilms, although it does not currently interact with any approved pharmaceutical drugs [21]. It is primarily found in cellulolytic bacteria such as Clostridium cellulovorans and Bacillus species [6, 7].

Other names

Family 17 carbohydrate-binding moduleCBM family 17Cellulose-binding domain family XVIICBM17

Not applicable