EC Number |
Protein Variants |
Reference |
---|
3.2.1.151 | D483A |
site-directed mutagenesis, a catalytic acid mutant, the mutation causes loss of the enzymatic activity by more than 10 000fold compared to the wild-type enzyme |
-, 753549 |
3.2.1.151 | D70A |
site-directed mutagenesis in the PoGH74cat module at the catalytic base |
-, 752723 |
3.2.1.151 | D70A |
site-directed mutagenesis, mutation of the catalytic base, the mutant turnover rate is similar to wild-type |
-, 752723 |
3.2.1.151 | D70A |
site-directed mutagenesis, the mutation causes loss of the enzymatic activity by more than 10 000fold compared to the wild-type enzyme |
-, 753549 |
3.2.1.151 | D74A |
crystallization data in complex with oligosaccharide substrate |
680677 |
3.2.1.151 | DELTAYNIIG |
loop deletion variant of isoform NXG1, structurally similar to the strict endo-transglycolase from Populus tremula x Populus tremuloides. Mutant has a greatly increased transglycosylation:hydrolysis ratio |
676433 |
3.2.1.151 | E155A |
the mutant acts as glucosynthase and can perform the condensation of xyloglucosyl fluorides, albeit at poor rates |
707647 |
3.2.1.151 | E358S |
nucleophile mutant |
715635 |
3.2.1.151 | E94A |
the GH16 xyloglucan hydrolase mutant of TmNXG1 acting as glycosynthase is capable of synthesizing XLLG-based xyloglucan oligosaccharides at rates feasible for preparative synthesis, thus providing an essential expansion of product ranges |
707647 |
3.2.1.151 | G476Y |
site-directed mutagenesis in the PoGH74cat module at the -1 subsite |
-, 752723 |