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