EC Number   |
Reaction |
Reference |
|---|
    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 |
