Cellobiohydrolase 1 (Cel7A) (Cel7A)

Cellobiohydrolase 1 (Cel7A), also known as Exoglucanase I, is a major cellulolytic enzyme produced by the fungus Trichoderma reesei (UniProt P62694). It belongs to the glycoside hydrolase family 7 (GH7) and is responsible for the processive hydrolysis of crystalline cellulose into cellobiose, a key step in the global carbon cycle and industrial biofuel production (UniProt, NIH). The enzyme's structure features a tunnel-shaped catalytic domain and a carbohydrate-binding module (CBM) that facilitates its movement along cellulose strands (PubMed). Beyond its industrial importance, Cel7A is recognized in pharmacology for its highly enantioselective binding to certain drugs, most notably the beta-blocker propranolol, making it a valuable tool as a chiral stationary phase in chromatography (Journal of Molecular Biology, NIH). While not a standard human therapeutic target, cellulases are used clinically to treat phytobezoars and are under investigation for their potential to disrupt microbial biofilms (NIH, ResearchGate). Its interaction with pharmaceutical compounds like propranolol serves as a model for understanding non-canonical drug-protein binding and off-target effects (NIH).

Other names

Exoglucanase 1CBHI1,4-beta-D-glucan cellobiohydrolase IExocellobiohydrolase ICellulase enzyme Cel7A

Cel7A catalyzes the processive hydrolysis of beta-1,4-glycosidic bonds in cellulose, releasing cellobiose (UniProt). It also binds enantioselectively to beta-blockers like propranolol within its catalytic tunnel (NIH).