EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
1.4.3.3 | additional information | immobilization of the enzyme, interaction of D-amino acid oxidase with single-walled carbon nanotubes, analysis by spectroscopic ellipsometry. DAAO can adopt multiple orientations on the surface, which are ultimately responsible for significant differences in catalytic activity, highest enzymatic activity by adsorbing the protein at pH 5.7 and 0.1 mg/ml, adsorption kinetics at different pH values, overview | Sus scrofa |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.4.3.3 | Sus scrofa | - |
- |
- |
EC Number | Posttranslational Modification | Comment | Organism |
---|---|---|---|
1.4.3.3 | flavoprotein | - |
Sus scrofa |
EC Number | Source Tissue | Comment | Organism | Textmining |
---|---|---|---|---|
1.4.3.3 | commercial preparation | from kidney | Sus scrofa | - |
1.4.3.3 | kidney | - |
Sus scrofa | - |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.4.3.3 | additional information | DAAO is a flavoprotein that catalyzes the dehydrogenation of different D-amino acids to their imino counterparts via a reduced flavin product complex. The reduced flavin is then reoxidized by O2 to yield H2O2, whereas the imino acid spontaneously hydrolyzes to the corresponding keto acid and NH4+. DAAO is strictly stereospecific and oxidizes a variety of D-amino acids, with a preference for those having small hydrophobic side chains, followed by those bearing polar, aromatic, and basic groups | Sus scrofa | ? | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
1.4.3.3 | DAAO | - |
Sus scrofa |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
1.4.3.3 | flavin | flavoenzyme | Sus scrofa |
EC Number | Organism | Comment | pI Value Maximum | pI Value |
---|---|---|---|---|
1.4.3.3 | Sus scrofa | - |
- |
6.37 |