EC Number   |
Protein Variants |
Reference |
|---|
   1.10.3.2 | A240P |
site-directed mutagenesis |
-, 724013 |
| 1.10.3.2 | D205R |
site-directed mutagenesis, the mutation in a highly conserved region perturbs the structural local environment in POXA1b, leading to a large rearrangement of the enzyme structure. The mutant shows highly reduced activity compared to the wild-type enzyme and is inactive with substrate syringaldazine |
697668 |
| 1.10.3.2 | D206A |
site-directed mutagenesis, the Asn mutation leads to a significant shift of pH optimum for activity with 2,6-dimethoxyphenol, the mutant shows several fold increased activity compared to the wild-type enzyme |
676943 |
| 1.10.3.2 | D206E |
site-directed mutagenesis, the Asn mutation leads to a significant shift of pH optimum for activity with 2,6-dimethoxyphenol, the mutant shows several fold increased activity compared to the wild-type enzyme |
676943 |
| 1.10.3.2 | D206N |
site-directed mutagenesis, the Asn mutation leads to a significant shift of pH optimum for activity with 2,6-dimethoxyphenol, the mutant shows several fold increased activity compared to the wild-type enzyme |
676943 |
| 1.10.3.2 | D341N |
site-directed mutagenesis the D3 domain coil, surface, the mutant shows H bonding with surrounding residue N340 in contrast to the wild-type enzyme |
-, 724013 |
| 1.10.3.2 | D360M |
mutation at sites Cu5 |
763429 |
| 1.10.3.2 | D394E |
mutant with the lower laccase activity displays a decreased decolorization efficiency as compared to the wild-type enzyme. Expressed in a lower level, about 50%, of the wild type enzyme. Optimum pH shifts towards the acidic value (0.5-1 units) relative to the wild type enzyme which has an optimal pH 6.0 |
-, 764221 |
| 1.10.3.2 | D394M |
mutant with the lower laccase activity displays a decreased decolorization efficiency as compared to the wild-type enzyme. Expressed in a lower level, about 50%, of the wild type enzyme. Optimum pH shifts towards the acidic value (0.5-1 units) relative to the wild type enzyme which has an optimal pH 6.0 |
-, 764221 |
| 1.10.3.2 | D394R |
mutant with the lower laccase activity displays a decreased decolorization efficiency as compared to the wild-type enzyme. Expressed in a lower level, about 16%, of the wild type enzyme. Optimum pH shifts towards the acidic value (0.5-1 units) relative to the wild type enzyme which has an optimal pH 6.0 |
-, 764221 |
