DDO (gene)

D-aspartate oxidase

Identifiers

DDO ; DASOX; DDO-1; DDO-2

External IDs

OMIM: 124450 MGI: 1925528 HomoloGene: 101531 ChEMBL: 5887 GeneCards: DDO Gene

Gene ontology
Molecular function	• receptor binding • protein binding • D-aspartate oxidase activity • cofactor binding
Cellular component	• peroxisome
Biological process	• aspartate metabolic process • aspartate catabolic process • insemination • grooming behavior • D-amino acid catabolic process • hormone metabolic process • oxidation-reduction process
Sources: Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

ENSG00000203797

ENSMUSG00000063428

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 6:
110.71 – 110.74 Mb

Chr 10:
40.63 – 40.65 Mb

PubMed search

D-aspartate oxidase is an enzyme that is encoded by the DDO gene.^[1]^[2]

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.^[2]

References

↑ 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.
↑ 2.0 2.1 "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. 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.