Cloned (Comment) | Organism |
---|---|
expression of wild-type and mutant enzymes in Escherichia coli strain BL21(DE3) | Bacillus licheniformis |
Protein Variants | Comment | Organism |
---|---|---|
I157S/W193R | random mutagenesis, the mutant shows an altered pH profile compared to the wild-type enzyme | Bacillus licheniformis |
additional information | repeated cycles of random mutagenesis of a region comprising residues from the position 34-281, mutant library construction. Mutant TP8H5 shows an altered pH profile as compared to the wild-type. The sequencing of variant TP8H5 indicated 2 amino acid changes, Ile157Ser and Trp193Arg, which are located in the solvent accessible flexible loop region in domain B | Bacillus licheniformis |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Bacillus licheniformis | - |
- |
- |
Bacillus licheniformis MTCC 6598 | - |
- |
- |
Synonyms | Comment | Organism |
---|---|---|
AmyL | - |
Bacillus licheniformis |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
50 | - |
assay at | Bacillus licheniformis |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
6 | - |
wild-type and mutant I157S/W193R enzymes | Bacillus licheniformis |
pH Minimum | pH Maximum | Comment | Organism |
---|---|---|---|
3 | 10 | activity range, mutant I157S/W193R enzyme | Bacillus licheniformis |
4 | 10 | activity range, wild-type enzyme | Bacillus licheniformis |
General Information | Comment | Organism |
---|---|---|
physiological function | alpha-amylases catalyze the hydrolysis of internal alpha-D-(1,4)-glucosidic linkages in starch, glycogen, and related oligo- and polysaccharides to produce maltodextrins, maltooligosaccharides, and glucose | Bacillus licheniformis |