| FAD dependent oxidoreductase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| crystal structure of d-amino acid oxidase in complex with two anthranylate molecules | |||||||||
| Identifiers | |||||||||
| Symbol | DAO | ||||||||
| Pfam | PF01266 | ||||||||
| Pfam clan | CL0063 | ||||||||
| InterPro | IPR006076 | ||||||||
| PROSITE | PDOC00753 | ||||||||
| SCOP | 1kif | ||||||||
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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) [1] 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 [2] to be important for the enzyme's catalytic activity.
This article incorporates text from the public domain Pfam and InterPro IPR006076