Cloned (Comment) | Organism |
---|---|
expression in Escherichia coli | Thermobaculum terrenum |
Protein Variants | Comment | Organism |
---|---|---|
K136T/Y137D/K138N/D139S | mutation resulted in improved trehalose yield compared to that of the wild-type enzyme | Thermobaculum terrenum |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Thermobaculum terrenum | D1CE96 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
alpha,alpha-trehalose | composition of the TtTreS active site is studied through computer calculation and enzyme analysis. The results are consistent with a two-step double-displacement mechanism. The data suggest that glucose rotation, following breakage of the alpha-1,4 glycosidic bond, is a key factor determining the reaction direction and conversion rate. The N246 residue plays an important role in glucose rotation | Thermobaculum terrenum | maltose | - |
r | |
maltose | composition of the TtTreS active site is studied through computer calculation and enzyme analysis. The results are consistent with a two-step double-displacement mechanism. The data suggest that glucose rotation, following breakage of the alpha-1,4 glycosidic bond, is a key factor determining the reaction direction and conversion rate. The N246 residue plays an important role in glucose rotation | Thermobaculum terrenum | alpha,alpha-trehalose | - |
r |
Synonyms | Comment | Organism |
---|---|---|
TreS | - |
Thermobaculum terrenum |