EC Number   |
Reaction |
Reference |
|---|
    3.2.1.1 | (alpha-D-glucopyranosyl-(1-4))n-alpha-D-glucopyranose + H2O = (alpha-D-glucopyranosyl-(1-4))n-m-alpha-D-glucopyranose + (alpha-D-glucopyranosyl-(1-4))m-alpha-D-glucopyranose |
- |
- |
| 3.2.1.1 | (alpha-D-glucopyranosyl-(1-4))n-alpha-D-glucopyranose + H2O = (alpha-D-glucopyranosyl-(1-4))n-m-alpha-D-glucopyranose + (alpha-D-glucopyranosyl-(1-4))m-alpha-D-glucopyranose |
active site mobility and structure of the psychrophilic alpha-amylase, ligand binding mechanism and conformational changes, side chains involved in substrate binding are strictly conserved, overview |
666079 |
| 3.2.1.1 | (alpha-D-glucopyranosyl-(1-4))n-alpha-D-glucopyranose + H2O = (alpha-D-glucopyranosyl-(1-4))n-m-alpha-D-glucopyranose + (alpha-D-glucopyranosyl-(1-4))m-alpha-D-glucopyranose |
endo mode of action |
-, 666829 |
| 3.2.1.1 | (alpha-D-glucopyranosyl-(1-4))n-alpha-D-glucopyranose + H2O = (alpha-D-glucopyranosyl-(1-4))n-m-alpha-D-glucopyranose + (alpha-D-glucopyranosyl-(1-4))m-alpha-D-glucopyranose |
isozyme Amyl III acts on the alpha-1,4-glycosidic linkage of the inner granule and releases oligosaccharides, decomposition of granules into G2 and G3 |
-, 665438 |
| 3.2.1.1 | (alpha-D-glucopyranosyl-(1-4))n-alpha-D-glucopyranose + H2O = (alpha-D-glucopyranosyl-(1-4))n-m-alpha-D-glucopyranose + (alpha-D-glucopyranosyl-(1-4))m-alpha-D-glucopyranose |
mode of action |
664782 |
| 3.2.1.1 | (alpha-D-glucopyranosyl-(1-4))n-alpha-D-glucopyranose + H2O = (alpha-D-glucopyranosyl-(1-4))n-m-alpha-D-glucopyranose + (alpha-D-glucopyranosyl-(1-4))m-alpha-D-glucopyranose |
PFTA is a bifunctional enzyme showing alpha-amylase as well as cyclodextrin-hydrolyzing activity |
663700 |
| 3.2.1.1 | (alpha-D-glucopyranosyl-(1-4))n-alpha-D-glucopyranose + H2O = (alpha-D-glucopyranosyl-(1-4))n-m-alpha-D-glucopyranose + (alpha-D-glucopyranosyl-(1-4))m-alpha-D-glucopyranose |
reaction mechanism and kinetic mechanism |
664440 |
| 3.2.1.1 | (alpha-D-glucopyranosyl-(1-4))n-alpha-D-glucopyranose + H2O = (alpha-D-glucopyranosyl-(1-4))n-m-alpha-D-glucopyranose + (alpha-D-glucopyranosyl-(1-4))m-alpha-D-glucopyranose |
residues Asp204, Glu240, and Asp305 are involved in catalysis, residues His118, Ala206, Lys207, and His304 are important for starch binding |
663786 |
| 3.2.1.1 | (alpha-D-glucopyranosyl-(1-4))n-alpha-D-glucopyranose + H2O = (alpha-D-glucopyranosyl-(1-4))n-m-alpha-D-glucopyranose + (alpha-D-glucopyranosyl-(1-4))m-alpha-D-glucopyranose |
the active site structure involves the catalytic residues D197, E233, and D300, reaction mechanism |
664094 |
| 3.2.1.1 | (alpha-D-glucopyranosyl-(1-4))n-alpha-D-glucopyranose + H2O = (alpha-D-glucopyranosyl-(1-4))n-m-alpha-D-glucopyranose + (alpha-D-glucopyranosyl-(1-4))m-alpha-D-glucopyranose |
the reaction mechanism involves no typical conformational change of the flexible loop, residues 303-309, that constitutes the surface edge of the substrate binding cleft, but only a small movement of the segment from residues 304/305, conformational change of catalytic residue Asp300 upon substrate binding, flexibility of the active site depends on the substrate aglycon bound, overview |
666839 |
