3.2.1.165	D139A	the mutation significantly decreases the hydrolytic activity compared to the wild type enzyme. The mutant enzyme exclusively exhibits glycosynthase activity using alpha-D-glucosaminyl fluoride and D-glucosamine as substrates	-, 749852	
3.2.1.165	D139E	compared with the wild type, the hydrolytic activity of the mutant is significantly suppressed (less than 0.1%), and the fluoride release activity also decreases to less than 3%	-, 749852	
3.2.1.165	D139S	the mutation significantly decreases the hydrolytic activity compared to the wild type enzyme	-, 749852	
3.2.1.165	D143A	the mutation significantly decreases the hydrolytic activity compared to the wild type enzyme	-, 749852	
3.2.1.165	D178N	inactive	751103	
3.2.1.165	D180N	inactive	751103	
3.2.1.165	D464A	specific acitivity is 0.44% compared to the activity of the wild-type enzyme	748421	
3.2.1.165	D464E	no activity	748421	
3.2.1.165	D464E/E539D	no activity	748421	
3.2.1.165	D464N	specific acitivity is 1.9% compared to the activity of the wild-type enzyme	748421