EC Number |
Reaction |
Reference |
---|
3.2.1.20 | maltotetraose + 3 H2O = 4 alpha-D-glucose |
ping-pong mechanism |
393289 |
3.2.1.20 | maltotetraose + 3 H2O = 4 alpha-D-glucose |
the enzyme has both exo-alpha-1,4-glucosidase and oligo-alpha-1,6-glucosidase activities |
654988 |
3.2.1.20 | maltotetraose + 3 H2O = 4 alpha-D-glucose |
residues Asp198, Glu265, and Asp327 are involved in catalysis, His100 and His326 are involved in substrate binding |
-, 655933 |
3.2.1.20 | maltotetraose + 3 H2O = 4 alpha-D-glucose |
the enzyme prefers short substrates, e.g. maltose and maltotriose, to longer substrates, and hydrolyzes alpha-1,4-glucosidic linkages, but also acts on alpha-1,2-, alpha-1,3-, and alpha-1,6-glucosidic linkages, the catalytic site contains three subsites with different affinities |
661611 |
3.2.1.20 | maltotetraose + 3 H2O = 4 alpha-D-glucose |
Val216 determines the substrate specificity of the yeast enzyme, active site structure modelling |
664827 |
3.2.1.20 | maltotetraose + 3 H2O = 4 alpha-D-glucose |
substrate recognition and catalytic mechanism, active site structure, residues R400, D87, W284, M321, F327 are involved in formation of the +1 subsite in the GH31 alpha-glucosidase substrate binding |
666076 |