Protein Variants | Comment | Organism |
---|---|---|
E172A | catalytic site mutant, no hydrolytic activity, no rescue of activity by 2 M azide | Bacillus cereus |
E172A/E367A | catalytic site double mutant, no hydrolytic activity, no rescue of activity by 2 M azide | Bacillus cereus |
E367A | catalytic site mutant, no hydrolytic activity in the absence of azide, in the presence of 2 M azide the mutant enzyme hydrolyzes maltopentaose at pH 7 and 25°C producing maltose, mechanism | Bacillus cereus |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Bacillus cereus | - |
var. mycoides | - |
Purification (Comment) | Organism |
---|---|
E172A, E367A and E172A/E367A mutant enzymes | Bacillus cereus |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
(alpha-D-glucopyranosyl-(1-4))n-alpha-D-glucopyranose + H2O = (alpha-D-glucopyranosyl-(1-4))n-2-alpha-D-glucopyranose + alpha-D-glucopyranosyl-(1-4)-beta-D-glucopyranose | catalytic mechanism, reaction mechanism | Bacillus cereus |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
maltopentaose + H2O | beta-amylase is an inverting enzyme that hydrolyzes the alpha-1,4-glucosidic linkage of the substrate liberating beta-maltose from the non-reducing end, catalytic mechanism, Glu-172 acts as general acid, Glu-367 acts as general base | Bacillus cereus | ? | - |
? | |
starch + H2O | beta-amylase is an inverting enzyme that hydrolyzes the alpha-1,4-glucosidic linkage of the substrate liberating beta-maltose from the non-reducing end, catalytic mechanism, Glu-172 acts as general acid, Glu-367 acts as general base | Bacillus cereus | ? | - |
? |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
25 | - |
assay at | Bacillus cereus |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7 | - |
assay at | Bacillus cereus |