1.13.12.4	G99A	(S)-lactate binds tighter to the G99A-mutant than to wild-type	440397	
1.13.12.4	H290Q	-	440424	
1.13.12.4	H290Q	the ability of L-lactate to reduce the enzyme flavin is abolished, whereas reoxidation of reduced enzyme with oxygen proceeds at a rate like that found in the wild type enzyme. Unlike the situation with wild type enzyme, where the transition state analog oxalate is bound tightly in a two-step reaction involving proton uptake from solution, the mutant enzyme binds oxalate weakly, in a single step reaction. Replacing the histidine has a significant effect on the ability of the enzyme to stabilize the flavin N(5)-sulfite adduct. Sulfite is bound at least 1000fold weaker than it is in the wild type enzyme	440400	
1.13.12.4	K266M	the rate of reduction with (S)-lactate is decreased compared with that of the wild-type enzyme, the mutant enzyme is virtually inactive	440399, 440424	
1.13.12.4	R293K	uncoupled reaction, no decarboxylation	440424	
1.13.12.4	Y152F	nearly as active as wild-type	440424	
1.13.12.4	Y44F	uncoupled reaction, no decarboxylation	440424