EC Number |
Protein Variants |
Reference |
---|
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 |