| D-amino-acid oxidase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
.png) 3D structure of DAAO from yeast (monomer) | |||||||||
| Identifiers | |||||||||
| EC no. | 1.4.3.3 | ||||||||
| CAS no. | 9000-88-8 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
| D-amino-acid oxidase | |||||||
|---|---|---|---|---|---|---|---|
| Identifiers | |||||||
| Symbol | DAO (DAAO) | ||||||
| NCBI gene | 1610 | ||||||
| HGNC | 2671 | ||||||
| OMIM | 124050 | ||||||
| RefSeq | NM_001917 | ||||||
| UniProt | P14920 | ||||||
| Other data | |||||||
| EC number | 1.4.3.3 | ||||||
| Locus | Chr. 12 q24 | ||||||
| |||||||
D-amino acid oxidase (DAAO; also OXDA or DAMOX) is an enzyme with the function on a molecular level to oxidize D-amino acids to the corresponding α-keto acids, producing ammonia and hydrogen peroxide. This results in a number of physiological effects in various systems, most notably the brain. The enzyme is most active toward neutral D-amino acids, and not active toward acidic D-amino acids. One of its most important targets in mammals is D-Serine in the central nervous system. By targeting this and other D-amino acids in vertebrates, DAAO is important in detoxification. The role in microorganisms is slightly different, breaking down D-amino acids to generate energy.[1]
DAAO is expressed in a wide range of species from yeasts to human.[1] It is not present in plants or in bacteria which instead use D-amino acid dehydrogenase. DAAO in humans is a candidate susceptibility gene[2] and together with G72 may play a role in the glutamatergic mechanisms of schizophrenia.[3] DAAO also plays a role in both biotechnological and medical advancements. Risperidone and sodium benzoate are inhibitors of DAAO.
D-amino acid oxidase is different from diamine oxidase that are both sometimes referred to as DAO.
- ^ a b Pollegioni L, Piubelli L, Sacchi S, Pilone MS, Molla G (June 2007). "Physiological functions of D-amino acid oxidases: from yeast to humans". Cellular and Molecular Life Sciences. 64 (11): 1373–94. doi:10.1007/s00018-007-6558-4. PMC 11136250. PMID 17396222. S2CID 24070769.
- ^ SZGene database (28 August 2007). "Gene Overview of All Published Schizophrenia-Association Studies for DAAO". Schizophrenia Research Forum. Archived from the original on 2008-05-12.
- ^ Boks MP, Rietkerk T, van de Beek MH, Sommer IE, de Koning TJ, Kahn RS (September 2007). "Reviewing the role of the genes G72 and DAAO in glutamate neurotransmission in schizophrenia". European Neuropsychopharmacology. 17 (9): 567–72. doi:10.1016/j.euroneuro.2006.12.003. PMID 17250995. S2CID 24756346.