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