EC Number   |
Protein Variants |
Reference |
|---|
   3.2.1.25 | D206N |
catalytically active mutant enzyme, similar temperature optimum like wild-type enzyme. The high-catalytic turn-over rate by D206N for beta-glucosidase activity makes it a useful enzyme in cellulose degradation at high temperatures |
750443 |
| 3.2.1.25 | E206G |
complete loss of activity |
695664 |
| 3.2.1.25 | E314G |
complete loss of activity |
695664 |
| 3.2.1.25 | N461A |
crystallization data. Involved either in hydrogen bonding to the ligands or in the maintenance of the hydrophilic sheath around the ligand |
700352 |
| 3.2.1.25 | Q646A |
crystallization data. Involved either in hydrogen bonding to the ligands or in the maintenance of the hydrophilic sheath around the ligand |
700352 |
| 3.2.1.25 | W198G |
crystallization data. Involved either in hydrogen bonding to the ligands or in the maintenance of the hydrophilic sheath around the ligand |
700352 |
| 3.2.1.25 | W345A |
crystallization data. Involved either in hydrogen bonding to the ligands or in the maintenance of the hydrophilic sheath around the ligand |
700352 |
| 3.2.1.25 | W645A |
crystallization data. Involved either in hydrogen bonding to the ligands or in the maintenance of the hydrophilic sheath around the ligand |
700352 |
| 3.2.1.25 | Y537A |
crystallization data. Involved either in hydrogen bonding to the ligands or in the maintenance of the hydrophilic sheath around the ligand |
700352 |
| 3.2.1.25 | D206N |
in contrast to the wild-type enzyme which shows a catalytic efficiency for 4-nitrophenyl beta-D-mannopyranoside that is 5fold higher than that for 4-nitrophenyl beta-D-galactopyranoside and 4fold higher than that for 4-nitrophenyl beta-D-glucopyranoside, the mutant enzyme shows highest catalytic efficiency towards 4-nitrophenyl beta-D-glucopyranoside, 11fold higher than that for 4-nitrophenyl beta-D-galactopyranoside and 60fold higher than that for 4-nitrophenyl beta-D-mannopyranoside |
-, 654641 |
