4.1.2.40	K124A	strongly reduced aldolase activity	679492	
4.1.2.40	K204A	mutation results in more than 98% decrease in aldolase activity	679492	
4.1.2.40	L165E	the mutant shows enhanced substrate specificity toward fructose-1,6-bisphosphate	715040	
4.1.2.40	L165E/L275S	the mutant shows enhanced substrate specificity toward fructose-1,6-bisphosphate	715040	
4.1.2.40	L275S	the mutant shows enhanced substrate specificity toward fructose-1,6-bisphosphate	715040	
4.1.2.40	additional information	construction of chimeras of isoforms LacD.1 and LacD.2. The C-terminus of LacD.1 contributes to its differential enzymatic activity, as replacing of its C-terminal half with 162 amino acid residues from the C-terminus of LacD.2 leads to an enzyme very similarly to LacD.2 in the cleavage of tagatose bisphosphate but over 3 times more efficient than LacD.2 at cleaving fructose bisphosphate. In addition, loop 1 and turn 2 influence the differential enzymatic activity of LacD.1	-, 727768