3.2.1.21	celloheptaose + 6 H2O  = 7 beta-D-glucose	double replacement mechanism, retaining the configuration. A water molecule may be involved in the stabilization of transition states through a sugar 2-hydroxyl oxygen	696002	
3.2.1.21	celloheptaose + 6 H2O  = 7 beta-D-glucose	molecular basis of the catalytic mechanism involving the acid/base Glu167 and the nucleophilic Glu356, the structure of BglB shows that several polar residues narrow the active site pocket and contour additional subsites, detailed substrate-binding mode and oligosaccharide-enzyme recognition pattern of BglB, overview, oligomerization in BglA can assist in fine-tuning the specificity of the active centre by modulating the loops surrounding the cavity	681444	
3.2.1.21	celloheptaose + 6 H2O  = 7 beta-D-glucose	reaction and kinetic mechanisms	663625	
3.2.1.21	celloheptaose + 6 H2O  = 7 beta-D-glucose	residues E173 and E362 are essential for catalytic activity	664360	
3.2.1.21	celloheptaose + 6 H2O  = 7 beta-D-glucose	structural basis for substrate specificity, residues N259, F261, and S462 are important, substrate binding mode and structure	665542	
3.2.1.21	celloheptaose + 6 H2O  = 7 beta-D-glucose	substrate binding mode and structure	665542	
3.2.1.21	celloheptaose + 6 H2O  = 7 beta-D-glucose	the conserved Asp287 is the potential nucleophile in the catalytic center	-, 677741	
3.2.1.21	celloheptaose + 6 H2O  = 7 beta-D-glucose	the enzyme contains a His residue which is important for catalytic activity	663728	
3.2.1.21	celloheptaose + 6 H2O  = 7 beta-D-glucose	the putative acid/base catalyst is Glu170	678852	
3.2.1.21	celloheptaose + 6 H2O  = 7 beta-D-glucose	the two catalytic glutamate residues are located on strand 4, the acid/base Glu165, and on strand 7,the nucleophile Glu373	681442	
3.2.1.21	celloheptaose + 6 H2O  = 7 beta-D-glucose	the two glutamic acid residues Glu172 and Glu370 are essential for enzyme activity of CellG	681491	
3.2.1.21	celloheptaose + 6 H2O  = 7 beta-D-glucose	Trp49 is important for transglucosylation catalytic activity	677813	
3.2.1.21	celloheptaose + 6 H2O  = 7 beta-D-glucose	W293 of the SDW segment, which is the residue next to the nucleophile D292 in family 3 BGL, is very important for hydrolytic reaction as a binder to a substrate. G294 of the SDWG sequence might play an important role in catalysis, interaction between the sugar rings and aromatic ring of W293 at the entrance of the catalytic pocket enhances the substrate recognition of beta-glucosidase	677765	
3.2.1.21	celloheptaose + 6 H2O  = 7 beta-D-glucose	Wide specificity for beta-glucosides. Some examples also hydrolyse one or more of the following: beta-D-galactosides, alpha-L-arabinosides, beta-D-xylosides, beta-D-fucosides	-