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Ribbon representation of the Streptomyces lividans β-1,4-endoglucanase catalytic domain - an example from the family 12 glycoside hydrolases [1]. Cellulase (EC 3.2.1.4; systematic name 4-β-D-glucan 4-glucanohydrolase) is any of several enzymes produced chiefly by fungi, bacteria, and protozoans that catalyze cellulolysis, the decomposition of cellulose and of some related polysaccharides:
Additionally, the KORRIGAN (KOR1) protein is thought to be a critical component of cellulose synthesis in that it acts as a cellulase at the plasma membrane-cell wall interface. KOR1 interacts with a two specific CesA proteins, possibly by proof-reading and relieving stress created by glucan chain synthesis, by hydrolyzing disordered amorphous ...
These enzymes were formerly known as cellulase family B. The 3D structure of the enzymatic core of cellobiohydrolase II (CBHII) from the fungus Trichoderma reesei reveals an alpha-beta protein with a fold similar to the ubiquitous barrel topology first seen in triose phosphate isomerase . [ 8 ]
Those found in aerobic bacteria bind cellulose (or other carbohydrates); but in anaerobic fungi they are protein binding domains, referred to as dockerin domains. The dockerin domains are believed to be responsible for the assembly of a multiprotein cellulase/hemicellulase complex, similar to the cellulosome found in certain anaerobic bacteria ...
Thus, degrading the biofilm may increase antibiotic efficacy, and potentiate host immune function and healing ability. For example, a combination of alpha-amylase and cellulase was shown to degrade polymicrobial bacterial biofilms from both in vitro and in vivo sources, and increase antibiotic effectiveness against them. [19]
In molecular biology, glycoside hydrolase family 5 is a family of glycoside hydrolases EC 3.2.1., which are a widespread group of enzymes that hydrolyse the glycosidic bond between two or more carbohydrates, or between a carbohydrate and a non-carbohydrate moiety.