D-amino acid oxidase
| D-amino-acid oxidase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| File:Crystal structure of RgDAAO (PDB code 1c0p).png 3D structure of DAAO from yeast (monomer) | |||||||||
| Identifiers | |||||||||
| EC number | 1.4.3.3 | ||||||||
| CAS number | 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 | ||||||||
| |||||||||
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| D-amino-acid oxidase | |
|---|---|
| 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.
DAAO is a candidate susceptibility gene[2] and together with G72 may play a role in the glutamatergic mechanisms of schizophrenia.[3] Risperidone and sodium benzoate are inhibitors of DAAO.
D-amino acid oxidase should not be confused with diamine oxidase as they are both sometimes referred to as DAO.
History
"The enzyme D-amino acid oxidase(DAO, DAAO) was discovered in the porcine kidney almost 75 years ago, and has since been extensively studied as a model flavin-dependent oxidase." [4]
Neurobiology of DAO
"The human DAO gene is located at chromosome 12q24 and comprises eleven exons."[5]
Actions of DAO in the Brain
"DAO oxidases D-amino acids through concomitent reduction of its prosthetic group, flavin adenine dinucleotide(FAD), producing the corresponding imino acids; this is then hydrolysed to yield ammonia and the corresponding a-keto acid." [6]
Regulation
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.[7]
This protein may use the morpheein model of allosteric regulation.[8]
Applications
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.
See also
- DAO
- DAOA-AS1
- D-amino acid dehydrogenase
- D-amino acid oxidase activator
- D-aspartate oxidase
- Diamine oxidase
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
- ↑ 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. PMID 17396222.
- ↑ Gene Overview of All Published Schizophrenia-Association Studies for DAAO Archived 2008-05-12 at the Wayback Machine. - 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". European Neuropsychopharmacology. 17 (9): 567–72. doi:10.1016/j.euroneuro.2006.12.003. PMID 17250995.
- ↑ [1]
- ↑ [2]
- ↑ [3]
- ↑ Madeira C, Freitas ME, Vargas-Lopes C, Wolosker H, Panizzutti R (April 2008). "Increased brain D-amino acid oxidase (DAAO) activity in schizophrenia". Schizophrenia Research. 101 (1–3): 76–83. doi:10.1016/j.schres.2008.02.002. PMID 18378121.
- ↑ Selwood T, Jaffe EK (March 2012). "Dynamic dissociating homo-oligomers and the control of protein function". Archives of Biochemistry and Biophysics. 519 (2): 131–43. doi:10.1016/j.abb.2011.11.020. PMC 3298769. PMID 22182754.
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- ↑ Verrall, L; Burnet, PWJ; Betts, J F; Harrison, PJ. "The neurobiology of D-amino acid oxidase (DAO) and its involvement in Schizophrenia". U.S. National Library of Medicine National Institutes of Health. NCBI. Retrieved 29 September 2017.