D-aspartate oxidase

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D-aspartate oxidase
D-aspartate oxidase
Identifiers
EC no.	1.4.3.1
CAS no.	9029-20-3
Databases
BRENDA	enzyme data
ExPASy	NiceZyme view
KEGG	enzyme entry
MetaCyc	metabolic pathway
Rhea	reactions
PDB structures	RCSB PDB PDBe PDBsum
Gene Ontology	AmiGO / QuickGO
PMC
Search
PMC	articles
PubMed	articles
NCBI	proteins

DDO
Identifiers
Aliases	DDO, Ddo, 5330420D20Rik, 5730402C02Rik, AI467244, DASOX, DDO-1, DDO-2, D-aspartate oxidase
External IDs	OMIM: 124450; MGI: 1925528; GeneCards: DDO
Enzyme activity
Gene location (Human)
Chr.	Chromosome 6 (human)
End	110,415,562 bp
Gene location (Mouse)
Chr.	Chromosome 10 (mouse)
End	40,557,843 bp
RNA expression pattern
	Top expressed in
	left ventricle; ; apex of heart; ; right ventricle; ; myocardium; ; myocardium of left ventricle; ; right adrenal gland; ; right adrenal cortex; ; right auricle of heart; ; left adrenal gland; ; kidney tubule;
	Top expressed in
	Ependyma of ventricular system of brain; ; digastric muscle; ; sternocleidomastoid muscle; ; right kidney; ; temporal muscle; ; triceps brachii muscle; ; soleus muscle; ; parotid gland; ; Epithelium of choroid plexus; ; myocardium of ventricle;
	More reference expression data
	; ;
	More reference expression data
Gene ontology
Molecular function	oxidoreductase activity; FAD binding; signaling receptor binding; protein binding; D-amino-acid oxidase activity; D-aspartate oxidase activity;
Cellular component	peroxisome; peroxisomal matrix; cytosol; cytoplasm;
Biological process	insemination; grooming behavior; aspartate metabolic process; D-amino acid metabolic process; hormone metabolic process; aspartate catabolic process; D-amino acid catabolic process; cellular nitrogen compound metabolic process; protein targeting to peroxisome;
	Sources:Amigo / QuickGO
Orthologs
Databases	NCBI: entry; OMA: entry
	8528
	70503
	ENSG00000203797
	ENSMUSG00000063428
	Q99489
	Q922Z0
	NM_003649; NM_004032
	NM_027442; NM_001316716; NM_001316717; NM_001316718; NM_001316719
NP_004023; NP_001355099; NP_001355100; NP_001355101; NP_001355102;
	NP_001355103; NP_001355104; NP_001359037
	NP_001303645; NP_001303646; NP_001303647; NP_001303648; NP_081718
	Wikidata
View/Edit Human	View/Edit Mouse

D-aspartate oxidase (EC 1.4.3.1) is an enzyme that is encoded by the DDO gene.^[5]^[6] D-aspartate oxidase catalyzes the chemical reaction

2D representation of the chemical structure of Q27076990.

D-Aspartic acid

+ H₂O

O₂

H₂O₂

Reversible left-right reaction arrow with minor forward substrate(s) from top left, minor forward product(s) to top right, minor reverse substrate(s) from bottom right and minor reverse product(s) to bottom left

O₂

H₂O₂

oxaloacetic acid

+ NH₃

The three substrates of this enzyme are D-aspartic acid, water and oxygen. Its products are oxaloacetic acid, hydrogen peroxide, and ammonia.^[7]^[8]^[9]^[10]

This enzyme belongs to the FAD dependent oxidoreductase family, specifically those acting on the CH-NH₂ group of donors with oxygen as acceptor. The systematic name of this enzyme class is D-aspartate:oxygen oxidoreductase (deaminating). Other names in common use include aspartic oxidase, and D-aspartic oxidase. This enzyme participates in alanine and aspartate metabolism. It employs one cofactor, FAD.

D-aspartate oxidase 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.^[6]

References

1 2 3 GRCh38: Ensembl release 89: ENSG00000203797 – Ensembl, May 2017
1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000063428 – Ensembl, May 2017
↑ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ 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".
↑ Enzyme 1.4.3.1 at KEGG Pathway Database.
↑ Still JL, Buell MV, Knox WE, Green DE (1949). "Studies on the cyclophorase system. VII. D-Aspartic oxidase". J. Biol. Chem. 179 (2): 831–837. doi:10.1016/S0021-9258(19)51276-5.
↑ Still JL; Sperling E (1950). "On the prosthetic group of the D-aspartic oxidase". J. Biol. Chem. 182 (2): 585–589. doi:10.1016/S0021-9258(18)56492-9.
↑ Dixon M, Kenworthy P (1967). "D-aspartate oxidase of kidney". Biochim. Biophys. Acta. 146 (1): 54–76. doi:10.1016/0005-2744(67)90073-3. PMID 6060479.

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. S2CID 40488767.
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): 203–2048. 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): 729–735. doi:10.1042/bj3220729. 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): 367–371. 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): 272–282. doi:10.1002/cne.10320. PMID 12209855. S2CID 24459809.
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): 16899–16903. Bibcode:2002PNAS...9916899M. 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): 805–811. Bibcode:2003Natur.425..805M. 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): 2121–2127. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.

[refGRCh38Ensembl-1] 1 2 3 GRCh38: Ensembl release 89: ENSG00000203797 – Ensembl, May 2017

[refGRCm38Ensembl-2] 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000063428 – Ensembl, May 2017

[3] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[4] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[pmid9163533-5] 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.

[entrez-6] 1 2 "Entrez Gene: DDO D-aspartate oxidase".

[7] Enzyme 1.4.3.1 at KEGG Pathway Database.

[8] Still JL, Buell MV, Knox WE, Green DE (1949). "Studies on the cyclophorase system. VII. D-Aspartic oxidase". J. Biol. Chem. 179 (2): 831–837. doi:10.1016/S0021-9258(19)51276-5.

[9] Still JL; Sperling E (1950). "On the prosthetic group of the D-aspartic oxidase". J. Biol. Chem. 182 (2): 585–589. doi:10.1016/S0021-9258(18)56492-9.

[10] Dixon M, Kenworthy P (1967). "D-aspartate oxidase of kidney". Biochim. Biophys. Acta. 146 (1): 54–76. doi:10.1016/0005-2744(67)90073-3. PMID 6060479.

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CH−NH₂ oxidoreductases (EC 1.4) – primarily amino acid oxidoreductases
1.4.1: NAD/NADP acceptor	Glutamate dehydrogenase GLUD1 GLUD2 Glutamate synthase (NADPH)
1.4.3: oxygen acceptor	D-amino acid oxidase Amine oxidase (Copper-containing (Lysyl Diamine Primary-amine)) (Flavin-containing (Monoamine)))
1.4.4: disulfide acceptor	Glycine cleavage system
1.4.99: other acceptors	D-amino acid oxidase Amine dehydrogenase

Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Diffusion-limited enzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator
Classification	EC number Enzyme superfamily Enzyme family List of enzymes
Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics
Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list) EC7 Translocases (list)

D-aspartate oxidase

See also

References

Further reading