D-amino acid oxidase
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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 spread from yeasts to human. It is not present in bacteria or in plants. Its function is to oxidize D-amino acids to the corresponding imino acids, producing ammonia and oxygen peroxide.
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.[1] DAAO is a candidate susceptibility gene[2] and together with G72 may play a role in the glutamatergic mechanisms of schizophrenia.[3]
[edit] See also
[edit] External links
[edit] References
- ^ 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:. PMID 18378121.
- ^ Gene Overview of All Published Schizophrenia-Association Studies for DAAO - SZGene database.
- ^ 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:. PMID 17250995.
- Pollegioni L. et al (2007). "Physiological functions of D-amino acid oxidases: from yeast to humans.". Cell Mol Life Sci 64 (11): 1373–94. doi:. PMID 17396222.
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