EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
3.2.1.6 | N207D | increase in Tm-value to 75.3°C, compared to wild-type Tm-value of 71.4°C | Bacillus licheniformis |
3.2.1.73 | N207D | mutant displays better thermotolerance than the wild type but also reduced activity | Bacillus licheniformis |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
3.2.1.73 | Ca2+ | necessary for the activity of the enzyme | Bacillus licheniformis |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
3.2.1.6 | Bacillus licheniformis | - |
- |
- |
3.2.1.73 | Bacillus licheniformis | P27051 | - |
- |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
3.2.1.73 | 4-methylumbelliferyl 3-O-beta-cellobiosyl-beta-D-glucopyranoside + H2O | - |
Bacillus licheniformis | 4-methylumbelliferone + 3-O-beta-cellobiosyl-beta-D-glucopyranoside | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
3.2.1.73 | 1,3-1,4-beta-glucanase | - |
Bacillus licheniformis |
EC Number | Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|---|
3.2.1.6 | additional information | - |
hypothesis for thermal inactivation: the first phase in thermal denaturation could be produced when calcium interactions are disrupted and the main loop becomes free to rearrange. This phase yields a partially active intermediary during the first phase of inactivation and then the intermediary is slowly converted into a totally inactive enzyme in the second phase | Bacillus licheniformis |
3.2.1.6 | 71 | - |
Tm-value for wild-type enzyme is 71.4°C | Bacillus licheniformis |
3.2.1.6 | 75 | - |
Tm-value for mutant enzyme N207D is 75.3°C | Bacillus licheniformis |