DDO (gene)

DDO
Identifiers
Aliases	DDO, Ddo, 5330420D20Rik, 5730402C02Rik, AI467244, DASOX, DDO-1, DDO-2, D-aspartate oxidase
External IDs	MGI: 1925528 HomoloGene: 101531 GeneCards: DDO
Gene ontology Molecular function • oxidoreductase activity • FAD binding • receptor binding • protein binding • D-amino-acid oxidase activity • cofactor binding • D-aspartate oxidase activity Cellular component • peroxisome • peroxisomal matrix Biological process • insemination • grooming behavior • aspartate metabolic process • D-amino acid metabolic process • hormone metabolic process • aspartate catabolic process • D-amino acid catabolic process • oxidation-reduction process • glyoxylate metabolic process Sources:Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	8528	70503
Ensembl	ENSG00000203797	ENSMUSG00000063428
UniProt	Q99489	Q922Z0
RefSeq (mRNA)	NM_003649 NM_004032	NM_027442 NM_001316716 NM_001316717 NM_001316718 NM_001316719
RefSeq (protein)	NP_003640.2 NP_004023.2	NP_001303645.1 NP_001303646.1 NP_001303647.1 NP_001303648.1 NP_081718.2
Location (UCSC)	Chr 6: 110.39 – 110.42 Mb	Chr 10: 40.63 – 40.65 Mb
PubMed search	[1]	[2]
Wikidata

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D-aspartate oxidase is an enzyme that is encoded by the DDO gene.^[3][4]

The protein encoded by this gene is a peroxisomal flavoprotein that catalyzes the oxidative deamination of D-aspartate and N-methyl D-aspartate. Flavin adenine dinucleotide or 6-hydroxyflavin adenine dinucleotide can serve as the cofactor in this reaction. Two (or four, according to Q99489) transcript variants encoding different isoforms have been found for this gene.^[4]

References

1. "Human PubMed Reference:".
2. "Mouse PubMed Reference:".
3. Setoyama C, Miura R (Jul 1997). "Structural and functional characterization of the human brain D-aspartate oxidase". J Biochem. 121 (4): 798–803. doi:10.1093/oxfordjournals.jbchem.a021655. PMID 9163533.
4. "Entrez Gene: DDO D-aspartate oxidase".

Further reading

• Barker RF, Hopkinson DA (1977). "The genetic and biochemical properties of the D-amino acid oxidases in human tissues". Ann. Hum. Genet. 41 (1): 27–42. doi:10.1111/j.1469-1809.1977.tb01959.x. PMID 21608.
• Van Veldhoven PP, Brees C, Mannaerts GP (1991). "D-aspartate oxidase, a peroxisomal enzyme in liver of rat and man". Biochim. Biophys. Acta. 1073 (1): 203–8. doi:10.1016/0304-4165(91)90203-S. PMID 1991137.
• Nagasaki H (1994). "Gender-related differences of mouse liver D-aspartate oxidase in the activity and response to administration of D-aspartate and peroxisome proliferators". Int. J. Biochem. 26 (3): 415–23. doi:10.1016/0020-711X(94)90062-0. PMID 8187937.
• Simonic T, Duga S, Negri A, et al. (1997). "cDNA cloning and expression of the flavoprotein D-aspartate oxidase from bovine kidney cortex". Biochem. J. 322 (3): 729–35. PMC 1218248. PMID 9148742.
• Amery L, Brees C, Baes M, et al. (1999). "C-terminal tripeptide Ser-Asn-Leu (SNL) of human D-aspartate oxidase is a functional peroxisome-targeting signal". Biochem. J. 336 (2): 367–71. doi:10.1042/bj3360367. PMC 1219880. PMID 9820813.
• Zaar K, Köst HP, Schad A, et al. (2002). "Cellular and subcellular distribution of D-aspartate oxidase in human and rat brain". J. Comp. Neurol. 450 (3): 272–82. doi:10.1002/cne.10320. PMID 12209855.
• Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
• Mungall AJ, Palmer SA, Sims SK, et al. (2003). "The DNA sequence and analysis of human chromosome 6". Nature. 425 (6960): 805–11. doi:10.1038/nature02055. PMID 14574404.
• Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.