Cloned (Comment) | Organism |
---|---|
- |
Proteus vulgaris |
Crystallization (Comment) | Organism |
---|---|
in complex with flavin adenine dinucleotide. The overall fold is similar to D-amino acid oxidases with an additional hydrophobic insertion module on protein surface. The hydrophobic module serves as an extra membrane-binding site. Residues Q99 and R315 may interact with the carboxyl group of substrate amino acids, residues Q278 and L317 may be important for substrate selectivity | Proteus vulgaris |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
membrane | - |
Proteus vulgaris | 16020 | - |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Proteus vulgaris | Q9LCB2 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | purified enzyme can generate a significant amount of hydrogen peroxide in vitro, it may be able to use dioxygen to directly reoxidize FADH2 | Proteus vulgaris | ? | - |
? |