FAD dependent oxidoreductase family
| FAD dependent oxidoreductase | |||||||||
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crystal structure of d-amino acid oxidase in complex with two anthranylate molecules
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| Identifiers | |||||||||
| Symbol | DAO | ||||||||
| Pfam | PF01266 | ||||||||
| Pfam clan | CL0063 | ||||||||
| InterPro | IPR006076 | ||||||||
| PROSITE | PDOC00753 | ||||||||
| SCOP | 1kif | ||||||||
| SUPERFAMILY | 1kif | ||||||||
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| Available protein structures: | |
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| Pfam | structures |
| PDB | RCSB PDB; PDBe; PDBj |
| PDBsum | structure summary |
In molecular biology, the FAD dependent oxidoreductase family of proteins is a family of FAD dependent oxidoreductases. Members of this family include Glycerol-3-phosphate dehydrogenase EC 1.1.99.5, Sarcosine oxidase beta subunit EC 1.5.3.1, D-amino-acid dehydrogenase EC 1.4.99.1, D-aspartate oxidase EC 1.4.3.1.
D-amino acid oxidase EC 1.4.3.3 (DAMOX or DAO) is an FAD flavoenzyme that catalyses the oxidation of neutral and basic D-amino acids into their corresponding keto acids. DAOs have been characterised and sequenced in fungi and vertebrates where they are known to be located in the peroxisomes.
D-aspartate oxidase EC 1.4.3.1 (DASOX) is an enzyme, structurally related to DAO, which catalyses the same reaction but is active only toward dicarboxylic D-amino acids. In DAO, a conserved histidine has been shown to be important for the enzyme's catalytic activity.
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