5.3.2.6	H6M	the mutant has about 3fold increased specific activity compared with that of wild type enzyme	748742	
5.3.2.6	H6M/A33E/F50V	the mutation strongly enhances the activity for the Michael-type addition of butanal to trans-beta nitrostyrene, compared to the wild type enzyme	748742	
5.3.2.6	M45Y/F50A	the mutant enzyme displays low Michael-type addition activity compared to the wild type enzyme	748742	
5.3.2.6	P1A	inactive	-, 749336	
5.3.2.6	P1A	site-directed mutagenesis, inactive mutant	718847	
5.3.2.6	P1A	the mutation results in 430fold decreases in kcat/Km compared to the wild type enzyme	726964	
5.3.2.6	R11A	site-directed mutagenesis, inactive mutant	718847	
5.3.2.6	R11A	site-directed mutagenesis, no kinetic effects of the R11A mutation, the stereoselectivity of the R11A-catalyzed protonation at C-5 of the dicarboxylate substrate decreases, while the stereoselectivity of protonation at C-3 of the monocarboxylate substrate increases in comparison with wild-type 4-OT	-, 718830	
5.3.2.6	R11A	the mutation results in 280fold decreases in kcat/Km compared to the wild type enzyme	726964	
5.3.2.6	R11A/R39A	site-directed mutagenesis, inactive mutant	-, 718830