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Results 1 - 6 of 6
EC Number Reaction Commentary Reference
Show all pathways known for 3.2.1.20Display the word mapDisplay the reaction diagram Show all sequences 3.2.1.20maltotetraose + 3 H2O = 4 alpha-D-glucose ping-pong mechanism 393289
Show all pathways known for 3.2.1.20Display the word mapDisplay the reaction diagram Show all sequences 3.2.1.20maltotetraose + 3 H2O = 4 alpha-D-glucose residues Asp198, Glu265, and Asp327 are involved in catalysis, His100 and His326 are involved in substrate binding -, 655933
Show all pathways known for 3.2.1.20Display the word mapDisplay the reaction diagram Show all sequences 3.2.1.20maltotetraose + 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
Show all pathways known for 3.2.1.20Display the word mapDisplay the reaction diagram Show all sequences 3.2.1.20maltotetraose + 3 H2O = 4 alpha-D-glucose the enzyme has both exo-alpha-1,4-glucosidase and oligo-alpha-1,6-glucosidase activities 654988
Show all pathways known for 3.2.1.20Display the word mapDisplay the reaction diagram Show all sequences 3.2.1.20maltotetraose + 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
Show all pathways known for 3.2.1.20Display the word mapDisplay the reaction diagram Show all sequences 3.2.1.20maltotetraose + 3 H2O = 4 alpha-D-glucose Val216 determines the substrate specificity of the yeast enzyme, active site structure modelling 664827
Results 1 - 6 of 6