EC Number   |
Protein Variants |
Reference |
|---|
   3.2.1.182 | E191A |
crystals of the enzymatically inactive mutant E191A are soaked in a solution containing DIMBOA-Glc as substrate and 3.5M sodium formate as cryoprotectant, the structure is solved at a resolution of 2.2 A and the DIMBOA-Glc molecule is clearly defined. In the structure, the aglycone moiety is shown to be stabilized by interaction with the aromatic ring of W379 and by a hydrogen bond with T194 |
720762 |
| 3.2.1.182 | E191A |
mutant shows no activity |
682403 |
| 3.2.1.182 | E191D |
catalytically inactive mutant is used for crystal structure determination |
720952 |
| 3.2.1.182 | E407A |
mutant shows no activity |
682403 |
| 3.2.1.182 | E462A |
inactive mutant, E462 plays a crucial role in hydrolysis of the substrate |
720762 |
| 3.2.1.182 | F198A |
kcat/Km values of ScGlu-F198A for DIMBOA-glucoside and DIBOA-glucoside decrease by a factor of 24- to 28fold as compared to wild-type ScGlu due to an increased Km, whereas the kcat value increases |
682403 |
| 3.2.1.182 | F198A |
Km increased compared to wild-type, kcat decreased compared to wild-type |
682403 |
| 3.2.1.182 | F471Y |
kcat values for DIBOA-glucoside increased, Km (DIBOA-glucoside) increased, Km (DIMBOA-glucoside) decreased, kcat values for DIMBOA-glucoside increased |
682403 |
| 3.2.1.182 | F471Y |
Km increased compared to wild-type, kcat (DIBOA-glucoside) increased compared to wild-type, kcat (DIMBOA-glucoside or 4-nitrophenyl beta-D-glucoside) increased compared to wild-type |
682403 |
| 3.2.1.182 | G464F |
kcat values for DIMBOA-glucoside and DIBOA-glucoside decreased, Km values increased |
682403 |
