EC Number   |
Reaction |
Reference |
|---|
    3.2.1.54 | cyclomaltodextrin + H2O = linear maltodextrin |
- |
- |
| 3.2.1.54 | cyclomaltodextrin + H2O = linear maltodextrin |
active site structure |
655458 |
| 3.2.1.54 | cyclomaltodextrin + H2O = linear maltodextrin |
also hydrolyses linear maltodextrin, model of coupled hydrolysis and transglycosylation catalyzed by cyclodextrin-degrading enzymes, catalytic mechanism of double-displacement reaction, active site cleft structure, conserved Glu332 plays an important role in the binding of oligosaccharide acceptors |
646818 |
| 3.2.1.54 | cyclomaltodextrin + H2O = linear maltodextrin |
model of coupled hydrolysis and transglycosylation catalyzed by cyclodextrin-degrading enzymes, catalytic mechanism of double-displacement reaction, active site cleft structure, catalytically important residues are Asp325, Glu354, and Asp421, conserved Glu332 plays an important role in the binding of oligosaccharide acceptors |
-, 646818 |
| 3.2.1.54 | cyclomaltodextrin + H2O = linear maltodextrin |
model of coupled hydrolysis and transglycosylation catalyzed by cyclodextrin-degrading enzymes, catalytic mechanism of double-displacement reaction, active site cleft structure, conserved Glu332 plays an important role in the binding of oligosaccharide acceptors |
-, 646818 |
| 3.2.1.54 | cyclomaltodextrin + H2O = linear maltodextrin |
PFTA is a bifunctional enzyme showing alpha-amylase as well as cyclodextrin-hydrolyzing activity |
663700 |
| 3.2.1.54 | cyclomaltodextrin + H2O = linear maltodextrin |
TVA II is a bifunctional enzyme showing alpha-amylase as well as cyclodextrin-hydrolyzing activity, the enzyme hydrolyzes alpha-1,4-glucosidic linkages and alpha-1,6-glucosidic linkages, active site structure and substrate binding structure, Trp356 is involved in substrate binding, and Tyr374 is involved in substrate orientation for catalysis |
-, 664823 |
