Cloned (Comment) | Organism |
---|---|
mutant enzyme H290Q expressed in Escherichia coli | Mycolicibacterium smegmatis |
Protein Variants | Comment | Organism |
---|---|---|
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 | Mycolicibacterium smegmatis |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
D-lactate | competitive | Mycolicibacterium smegmatis |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Mycolicibacterium smegmatis | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
L-lactate + O2 | - |
Mycolicibacterium smegmatis | acetate + CO2 + H2O | - |
? |