Organism | UniProt | Comment | Textmining |
---|---|---|---|
Alkalihalobacillus lehensis | X5CPN2 | - |
- |
Alkalihalobacillus lehensis G1 | X5CPN2 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
beta-cyclodextrin + H2O | the main subsites for substrate stabilization in the active site are -2, -1, +1 and +2. A bulky residue, Trp359 at the +2 subsite is identified to cause steric interference to the bound linear malto-oligosaccharides thus prevented it to occupy subsite +3, which can only be reached by a highly bent glucose molecule such as beta-cyclodextrin | Alkalihalobacillus lehensis | maltose + ? | - |
? | |
beta-cyclodextrin + H2O | the main subsites for substrate stabilization in the active site are -2, -1, +1 and +2. A bulky residue, Trp359 at the +2 subsite is identified to cause steric interference to the bound linear malto-oligosaccharides thus prevented it to occupy subsite +3, which can only be reached by a highly bent glucose molecule such as beta-cyclodextrin | Alkalihalobacillus lehensis G1 | maltose + ? | - |
? | |
additional information | the enzyme exhibits high transglycosylation activity on maltooligosaccharides with polymerization degree of three and above | Alkalihalobacillus lehensis | ? | - |
? | |
additional information | the enzyme exhibits high transglycosylation activity on maltooligosaccharides with polymerization degree of three and above | Alkalihalobacillus lehensis G1 | ? | - |
? |
Synonyms | Comment | Organism |
---|---|---|
MAG1 | - |
Alkalihalobacillus lehensis |