D-amino acid oxidase

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D-amino-acid oxidase
Crystal structure of RgDAAO (PDB code 1c0p).png
3D structure of DAAO from yeast (monomer)
EC number
CAS number 9000-88-8
IntEnz IntEnz view
ExPASy NiceZyme view
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum
Gene Ontology AmiGO / EGO
D-amino-acid oxidase
Symbol DAO (DAAO)
Entrez 1610
HUGO 2671
OMIM 124050
RefSeq NM_001917
UniProt P14920
Other data
EC number
Locus Chr. 12 q24

D-amino acid oxidase (DAAO; also DAO, OXDA, DAMOX) is a peroxisomal enzyme containing FAD as cofactor that 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. Its function is to oxidize D-amino acids to the corresponding imino acids, producing ammonia and hydrogen peroxide.

This enzyme belongs to the FAD dependent oxidoreductase family, and acts on the CH-NH2 group of D-amino acid donors with oxygen as acceptor. The enzyme is most active toward neutral D-amino acids, and not active toward acidic D-amino acids.

Recently, mammalian D-amino acid oxidase has been connected to the brain D-serine metabolism and to the regulation of the glutamatergic neurotransmission. In a postmortem study, the activity of DAAO was found to be two-fold higher in schizophrenia.[2]

DAAO is a candidate susceptibility gene[3] and together with G72 may play a role in the glutamatergic mechanisms of schizophrenia.[4] Risperidone and sodium benzoate are inhibitors of DAAO.

DAAO is used as a biocatalyst in several biotechnological applications, such as the oxidation of cephalosporin C, the deracemition of racemic D-amino acid solutions and as the biological component in several biosensors for the determination of the content in D-amino acids of biological fluids.

This protein may use the morpheein model of allosteric regulation. [5]

See also[edit]

External links[edit]


  1. ^ Pollegioni L, Piubelli L, Sacchi S, Pilone MS, Molla G (June 2007). "Physiological functions of D-amino acid oxidases: from yeast to humans". Cell. Mol. Life Sci. 64 (11): 1373–94. doi:10.1007/s00018-007-6558-4. PMID 17396222. 
  2. ^ Madeira C, Freitas ME, Vargas-Lopes C, Wolosker H, Panizzutti R (April 2008). "Increased brain d-amino acid oxidase (DAAO) activity in schizophrenia". Schizophr. Res. 101 (1–3): 76–83. doi:10.1016/j.schres.2008.02.002. PMID 18378121. 
  3. ^ Gene Overview of All Published Schizophrenia-Association Studies for DAAO - SZGene database.
  4. ^ 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". Eur Neuropsychopharmacol 17 (9): 567–72. doi:10.1016/j.euroneuro.2006.12.003. PMID 17250995. 
  5. ^ T. Selwood; E. K. Jaffe. (2011). "Dynamic dissociating homo-oligomers and the control of protein function.". Arch. Biochem. Biophys. 519 (2): 131–43. doi:10.1016/j.abb.2011.11.020. PMC 3298769. PMID 22182754.