DDO

Official Full Name

D-aspartate oxidase

Organism

Homo sapiens

Gene ID

8528

Background

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. Several transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Jan 2019]

Synonyms

DASOX; DASPO; DDO-1; DDO-2

Cat.No.	Product Name	Price
CSC-DC004127	Panoply™ Human DDO Knockdown Stable Cell Line	Inquiry
CSC-SC004127	Panoply™ Human DDO Over-expressing Stable Cell Line	Inquiry

Cat.No.	Product Name	Price
AD04681Z	Human DDO adenoviral particles	Inquiry
LV10463L	human DDO (NM_004032) lentivirus particles	Inquiry
LV10464L	human DDO (NM_003649) lentivirus particles	Inquiry

Cat.No.	Product Name	Price
SHG226475	shRNA set against Mouse Ddo(NM_027442.5)	Inquiry
SHG226357	shRNA set against Human DDO(NM_004032.2)	Inquiry
SHG226385	shRNA set against Human DDO(NM_003649.2)	Inquiry
SHH275701	shRNA set against Human DDO (NM_003649.2)	Inquiry
SHH275705	shRNA set against Mouse DDO (NM_027442.5)	Inquiry
SHH275709	shRNA set against Rat DDO (NM_001109465.2)	Inquiry

Cat.No.	Product Name	Price
CDCR286123	Human DDO ORF Clone(NM_003649.2)	Inquiry
CDCR376047	Rat Ddo ORF Clone(NM_001109465.2)	Inquiry
CDFH004883	Human DDO cDNA Clone(NM_003649.2)	Inquiry
CDFH004884	Human DDO cDNA Clone(NM_004032.2)	Inquiry
CDFR009000	Rat Ddo cDNA Clone(NM_001109465.2)	Inquiry
MiUTR1H-02712	DDO miRNA 3'UTR clone	Inquiry
MiUTR1H-02713	DDO miRNA 3'UTR clone	Inquiry
MiUTR1M-03741	DDO miRNA 3'UTR clone	Inquiry
CDCB188219	Rabbit DDO ORF clone (XM_008263368.1)	Inquiry
CDCR054242	Human DDO ORF clone (NM_004032.2)	Inquiry
CDCS411389	Human DDO ORF Clone (BC032786)	Inquiry

Detailed Information

Ddo (D-aspartate oxidase) gene, a member of the aspartate oxidase family, has been widely studied for its significant role in various biological processes. In eukaryotes, acidic D-amino acids are primarily being degraded by D-aspartate oxidase (DDO or DASPO, EC:1.4.3.1), but in the mouse heart, D-glutamate is metabolized mainly by D-glutamate cyclase (EC4.2.1.48), a flavonase that catalyzes the oxidative deamination of acidic D-amino acids to form the corresponding α-keto acids and ammonia. The reduced FAD is re-oxidized by molecular oxygen to produce hydrogen peroxide. DDO and DAAO are thought to have originated from the same ancestor due to the high degree of similarity in their amino acid sequences. 70 years ago, researchers first detected DDO in rabbit kidneys and livers, and it is now known to be present in eukaryotic organisms ranging from fungi to humans. it has not yet been detected in prokaryotic organisms or plants. in fungi, DDO is responsible for the toxicity of the D-Asp for cell growth and the elimination of the D-Asp. In fungi, DDO is required for cell growth on D-Asp and eliminates the toxicity of D-Asp. In mammals, DDO plays a key role in D-Asp metabolism and is involved in the regulation of D-Asp levels during physiological processes.

DO typically contains the Wierenga sequence for ADP binding at the N-terminus (GXGXXG, where X is an arbitrary amino acid) and the PTS1 sequence at the C-terminus (S/T/A/G/C/N-R/K/H-L/I/V/M/A/F/Y, PROSITE, PS00342). The human enzyme was shown to localize to the peroxisome, although the PTS1 sequence (SNL) of the human enzyme does not correspond to the consensual sequence. hDDO-1 encompasses the entire coding region and generates proteins that contain 341 amino acid residues, whereas hDDO-2 is an internally truncated form of hDDO-1 (282 amino acid residues). hDDO-1 and the other mammalian DDOs have the hDDO-1 and other mammalian DDOs have the same number of amino acid residues and high amino acid sequence identity (about 75% to 91%).

References:

Pollegioni L, Molla G, Sacchi S, Murtas G. Human D-aspartate Oxidase: A Key Player in D-aspartate Metabolism. Front Mol Biosci. 2021 Jun 23;8:689719. doi: 10.3389/fmolb.2021.689719. PMID: 34250021; PMCID: PMC8260693.
Saitoh Y, Katane M, Miyamoto T, Sekine M, Sakamoto T, Imai H, Homma H. Secreted d-aspartate oxidase functions in C. elegans reproduction and development. FEBS J. 2019 Jan;286(1):124-138. doi: 10.1111/febs.14691. Epub 2018 Nov 17. PMID: 30387556.

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