EC Number   |
Protein Variants |
Reference |
|---|
    3.2.1.8 | A54T |
when exposed to 80°C for 90 min the mutant displays a low stability and retains only 10% of its activity. It is extremely alkali tolerant. After 90 min at pH 10 it retains 93% of its activity. It has catalytic activity almost comparable to the wild-type |
697995 |
| 3.2.1.8 | A60D |
increase in thermostability and in optimum temperature |
738888 |
| 3.2.1.8 | biofuel production |
potential application in the field of biomass pretreatment and biofuel production |
-, 750334 |
| 3.2.1.8 | D101N |
site-directed mutagenesis, deleterious mutation |
709203 |
| 3.2.1.8 | D101N/G103F/R132A/R136A |
site-directed mutagenesis, the mutant is expressed in inclusion bodies |
709203 |
| 3.2.1.8 | D11F/R122D |
no inhibition by Triticum aestivum xylanase inhibitor-I |
680984 |
| 3.2.1.8 | D11F/R122D |
the mutant shows highly decreased sensitivity to inhibitor Triticum aestivum xylanase inhibitor compared to wild-type enzyme |
709202 |
| 3.2.1.8 | D144A |
crystallization data |
-, 664135 |
| 3.2.1.8 | D281N |
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme. The TtGH8 D281N-beta-1,4-xylohexaose complex structure reveals that, the -1 subsite sugar is in a completely ring-flipped, southern hemisphere 1C4 chair conformation. Although this allows access to a hexasaccharide complex structure, the ring-flipped -1 sugar is unlikely to be representative of a catalytically relevant conformation since its position neither allows protonation of the leaving group by Glu73 nor is there a potential reactive water. In the 1C4 chair conformation the now axial (and down) O2 occupies the position that should instead be occupied by the nucleophilic water |
-, 749504 |
| 3.2.1.8 | D48N/T64S |
shift in pH optimum from 2.0 to 5.0 |
-, 739002 |
