Cloned (Comment) | Organism |
---|---|
recombinant wild-type Fcb2 and its recombinant FDH domain (FMN-binding domain) are expressed in Escherichia coli | Saccharomyces cerevisiae |
Protein Variants | Comment | Organism |
---|---|---|
additional information | the separately engineered flavodehydrogenase domain produces superoxide anion in its slow reaction with oxygen. This reaction apparently also takes place in the holoenzyme when oxygen is the sole electron acceptor, because the heme domain autoxidation is also slow. This is not unexpected in view of the heme domain mobility relative to the tetrameric flavodehydrogenase core. Reaction is so slow that it cannot compete with the normal electron flow in the presence of monoelectronic acceptors, such as ferricyanide and cytochrome c | Saccharomyces cerevisiae |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Saccharomyces cerevisiae | P00175 | - |
- |
Storage Stability | Organism |
---|---|
-70°C, in 0.1 M phosphate buffer, 1 mM EDTA, pH 7, 10 mM DL-lactate is added to the Fcb2 preparations to keep the enzyme in the reduced state | Saccharomyces cerevisiae |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
L-lactate + ferricyanide | - |
Saccharomyces cerevisiae | pyruvate + ferrocyanide + H+ | - |
? | |
L-lactate + O2 | the FDH domain reacts slowly with oxygen with formation of superoxide anion when separated from its natural electron acceptor, whether isolated or included in the holoenzyme | Saccharomyces cerevisiae | ? + superoxide anion | - |
? |
Synonyms | Comment | Organism |
---|---|---|
Fcb2 | - |
Saccharomyces cerevisiae |
flavocytochrome b2 | - |
Saccharomyces cerevisiae |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
FMN | - |
Saccharomyces cerevisiae |