3.2.1.62	D1711N	introduction of a glycosylation site, reduced transport rate to the plasma membrane	208744	
3.2.1.62	D1711N	introduction of potential N-glycosylation site, no enzymic activity, probably due to altered protein folding pattern and reduced dimerization efficiency	208744	
3.2.1.62	D311Y	the mutant enzyme is characterized by a lowered KM value for the hydrolysis of 2-chloro-4-nitrophenyl beta-cellobioside and increased transglycosylation when using aliphatic 1,3-diols or alcohols bearing a delta-hydroxy ketone function as acceptors. The transglycosylation/hydrolysis ratio in reactions catalyzed by the mutant is completely inversed and weak secondary hydrolysis is postponed, thus providing the basis for high transglycosylation yields (between 68 and 93%)	749451	
3.2.1.62	D311Y	the mutant shows increased catalytic efficiency for the hydrolysis of 2-chloro-4-nitrophenyl beta-cellobioside compared to the wild type enzyme. The transglycosylation ability of the mutant is improved in comparison to the wild type enzyme	749451	
3.2.1.62	E165D	reduced activity	680835	
3.2.1.62	E165Q	almost no activity	680835	
3.2.1.62	E233A	site directed mutagenesis	680770	
3.2.1.62	E254Q	inactive	-, 732073	
3.2.1.62	E351S	site directed mutagenesis	680770	
3.2.1.62	E373D	reduced activity	680835