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	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	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	
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	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