EC Number   |
Protein Variants |
Reference |
|---|
   1.1.3.41 | E154P |
site-directed mutagenesis, the mutant shows increased thermolability compared to the wild-type enzyme |
-, 724072 |
| 1.1.3.41 | E50P |
site-directed mutagenesis, the mutant shows increased thermolability compared to the wild-type enzyme |
-, 724072 |
| 1.1.3.41 | K18R/E19R |
site-directed mutagenesis, the mutant shows increased thermolability compared to the wild-type enzyme |
-, 724072 |
| 1.1.3.41 | L234R/D235P |
site-directed mutagenesis, the mutant shows increased thermolability compared to the wild-type enzyme |
724072 |
| 1.1.3.41 | more |
construction of an AldO mutant synthetic bifunctional enzyme, the enzyme from Streptomyces coelicolor A3(2) is endowed with an extra catalytic functionality by fusing it to a microperoxidase. The mutant is functional and a both fully covalently flavinylated and heminylated: an oxiperoxidase. Replacement of portions of the wild-type AldO sequence with the bacterial cytochrome c CXXCH heme-binding motif, domain structure, overview |
-, 724756 |
| 1.1.3.41 | R232A/P233G |
site-directed mutagenesis, the mutant shows increased thermolability compared to the wild-type enzyme |
724072 |
| 1.1.3.41 | R232A/P233G/L234R/D235P |
site-directed mutagenesis, the mutant shows increased thermolability compared to the wild-type enzyme |
724072 |
| 1.1.3.41 | synthesis |
synthesis of rare sugars using Escherichia coli whole cells. The donor substrate dihydroxyacetone phosphate (DHAP) is generated from glycerol by glycerol kinase (GK) and glycerol phosphate oxidase (GPO). The acceptor D-glyceraldehyde is directly produced from glycerol by alditol oxidase. The aldol reaction between DHAP and D-glyceraldehyde is performed by L-rhamnulose-1-phosphate aldolase (RhaD) to generate the corresponding sugar-1-phosphate. Finally, the phosphate group is removed by fructose-1-phosphatase (YqaB) to obtain the rare sugars D-sorbose and D-psicose. Under the optimized conditions, the cascade produces 7.9 g/l of D-sorbose and D-psicose with a total conversion rate of 17.7% from glycerol |
-, 762798 |
| 1.1.3.41 | T16R/A17P |
site-directed mutagenesis, the mutant shows increased thermolability compared to the wild-type enzyme |
-, 724072 |
| 1.1.3.41 | T16R/A17P/K18R/G19R |
site-directed mutagenesis, the mutant shows increased thermolability compared to the wild-type enzyme |
-, 724072 |
