4.1.2.52	D42A	inactive, the mutation leads to a concomitant loss of the metal ion	725493	
4.1.2.52	H45A	by site-directed mutagenesis, mutant enzyme has 24fold higher dissociation constant for Co2+ compared to the wild-type enzyme, apparent Km value for Co2+ increases by about 800fold compared to the wild-type enzyme, different kcat and km values	722258	
4.1.2.52	H45A	the mutation leads to a decrease in kcat of the enzyme by 78fold	725493	
4.1.2.52	H45Q	by site-directed mutagenesis, mutant enzyme has 69fold higher dissociation constant for Co2+ compared to the wild-type enzyme, apparent Km value for Co2+ increases by about 800fold compared to the wild-type enzyme, different kcat and km values	722258	
4.1.2.52	H45Q	the mutation leads to a decrease in kcat of the enzyme by 2059fold	725493	
4.1.2.52	R70A	almost inactive	725493	
4.1.2.52	R70A	replacement by site-specific mutagenesis results in an enzyme that lacks both aldolase and decarboxylase activities. The mutant enzyme is also unable to catalyze pyruvate proton exchange	721601	
4.1.2.52	R70K	the mutation reduces catalytic efficiency by 270fold	725493