DDO (gene)
| D-aspartate oxidase | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||||||
| Symbols | DDO ; DASOX; DDO-1; DDO-2 | ||||||||||||
| External IDs | OMIM: 124450 MGI: 1925528 HomoloGene: 101531 ChEMBL: 5887 GeneCards: DDO Gene | ||||||||||||
| EC number | 1.4.3.1 | ||||||||||||
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| RNA expression pattern | |||||||||||||
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| More reference expression data | |||||||||||||
| Orthologs | |||||||||||||
| Species | Human | Mouse | |||||||||||
| Entrez | 8528 | 70503 | |||||||||||
| Ensembl | ENSG00000203797 | ENSMUSG00000063428 | |||||||||||
| UniProt | Q99489 | Q922Z0 | |||||||||||
| RefSeq (mRNA) | NM_003649 | NM_027442 | |||||||||||
| RefSeq (protein) | NP_003640 | NP_081718 | |||||||||||
| Location (UCSC) |
Chr 6: 110.39 – 110.42 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.
- 1 2 "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. replacement character in
|last4=at position 2 (help) - 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.
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