D-amino acid oxidase
D-amino-acid oxidase | |||||||||
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File:Crystal structure of RgDAAO (PDB code 1c0p).png
3D structure of DAAO from yeast (monomer)
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Identifiers | |||||||||
EC number | 1.4.3.3 | ||||||||
CAS number | Template:CAS | ||||||||
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 / EGO | ||||||||
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D-amino-acid oxidase | |
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Identifiers | |
Symbol | DAO (DAAO) |
Entrez | 1610 |
HUGO | 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 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
External links
- D-Amino-Acid Oxidase at the US National Library of Medicine Medical Subject Headings (MeSH)
- http://www.calzyme.com/commerce/catalog/spcategory.jsp?category_id=1043
References
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- ↑ Gene Overview of All Published Schizophrenia-Association Studies for DAAO - SZGene database.
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