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