Information on EC 1.4.3.1 - D-aspartate oxidase

Substrates: at least two genes encoding functional DASPOs (C47Ap and F18Ep). The two DASPOs differ in their substrate specificities and possibly also in their subcellular localization
Products: -

D-aspartate + H2O + O2

oxaloacetate + NH3 + H2O2

Substrates: 100% activity
Products: -

D-aspartate + H2O + O2

oxaloacetate + NH3 + H2O2

Substrates: -
Products: -

D-aspartate + H2O + O2

oxaloacetate + NH3 + H2O2

D-aspartate + H2O + O2

oxaloacetate + NH3 + H2O2

Substrates: -
Products: -

D-aspartate + H2O + O2

oxaloacetate + NH3 + H2O2

Substrates: -
Products: -

D-aspartate + H2O + O2

oxaloacetate + NH3 + H2O2

Substrates: -
Products: -

D-aspartate + H2O + O2

oxaloacetate + NH3 + H2O2

Chaunax fimbriatus

Substrates: -
Products: -

D-aspartate + H2O + O2

oxaloacetate + NH3 + H2O2

Cololabis saira

Substrates: -
Products: -

D-aspartate + H2O + O2

oxaloacetate + NH3 + H2O2

Substrates: -
Products: -

D-aspartate + H2O + O2

oxaloacetate + NH3 + H2O2

Evynnis tumifrons

Substrates: -
Products: -

D-aspartate + H2O + O2

oxaloacetate + NH3 + H2O2

Substrates: -
Products: -

D-aspartate + H2O + O2

oxaloacetate + NH3 + H2O2

391706, 391709, 391712

Substrates: -
Products: -

D-aspartate + H2O + O2

oxaloacetate + NH3 + H2O2

Substrates: this enzyme is proposed to have a role in the inactivation of the synaptically released D-aspartate
Products: -

D-aspartate + H2O + O2

oxaloacetate + NH3 + H2O2

711719, 711325

Substrates: -
Products: -

D-aspartate + H2O + O2

oxaloacetate + NH3 + H2O2

D-aspartate + H2O + O2

oxaloacetate + NH3 + H2O2

743836, 743063

Substrates: -
Products: -

D-aspartate + H2O + O2

oxaloacetate + NH3 + H2O2

Substrates: -
Products: -

D-aspartate + H2O + O2

oxaloacetate + NH3 + H2O2

Substrates: -
Products: -

D-aspartate + H2O + O2

oxaloacetate + NH3 + H2O2

Substrates: -
Products: -

D-aspartate + H2O + O2

oxaloacetate + NH3 + H2O2

Meretrix lusoria

Substrates: -
Products: -

D-aspartate + H2O + O2

oxaloacetate + NH3 + H2O2

Substrates: -
Products: -

D-aspartate + H2O + O2

oxaloacetate + NH3 + H2O2

391716

Substrates: -
Products: -

D-aspartate + H2O + O2

oxaloacetate + NH3 + H2O2

Q0E9Q7

Substrates: -
Products: -

D-aspartate + H2O + O2

oxaloacetate + NH3 + H2O2

Substrates: 100% activity
Products: -

D-aspartate + H2O + O2

oxaloacetate + NH3 + H2O2

686597, 711719, 711325, 711722

Substrates: -
Products: -

D-aspartate + H2O + O2

oxaloacetate + NH3 + H2O2

D-aspartate + H2O + O2

oxaloacetate + NH3 + H2O2

Q0E9Q7

Substrates: -
Products: -

D-aspartate + H2O + O2

oxaloacetate + NH3 + H2O2

Substrates: -
Products: -

D-aspartate + H2O + O2

oxaloacetate + NH3 + H2O2

Q0E9Q7

743350, 743836, 742426

Substrates: -
Products: -

D-aspartate + H2O + O2

oxaloacetate + NH3 + H2O2

Substrates: -
Products: -

D-aspartate + H2O + O2

oxaloacetate + NH3 + H2O2

391714, 391716, 391717, 657350

Substrates: -
Products: -

D-aspartate + H2O + O2

oxaloacetate + NH3 + H2O2

Oncorhynchus keta

Substrates: -
Products: -

D-aspartate + H2O + O2

oxaloacetate + NH3 + H2O2

Oncorhynchus masou

Substrates: -
Products: -

D-aspartate + H2O + O2

oxaloacetate + NH3 + H2O2

Substrates: -
Products: -

D-aspartate + H2O + O2

oxaloacetate + NH3 + H2O2

Substrates: -
Products: -

D-aspartate + H2O + O2

oxaloacetate + NH3 + H2O2

Substrates: ferricyanide and 2,6-dichlorophenolindophenol can also act as electron acceptors instead of O2
Products: -

D-aspartate + H2O + O2

oxaloacetate + NH3 + H2O2

Substrates: -
Products: -

D-aspartate + H2O + O2

oxaloacetate + NH3 + H2O2

391728, 711719

Substrates: -
Products: -

D-aspartate + H2O + O2

oxaloacetate + NH3 + H2O2

D-aspartate + H2O + O2

oxaloacetate + NH3 + H2O2

Substrates: -
Products: -

D-aspartate + H2O + O2

oxaloacetate + NH3 + H2O2

Substrates: -
Products: -

D-aspartate + H2O + O2

oxaloacetate + NH3 + H2O2

Substrates: -
Products: -

D-aspartate + H2O + O2

oxaloacetate + NH3 + H2O2

Penaeus japonicus

Substrates: -
Products: -

D-aspartate + H2O + O2

oxaloacetate + NH3 + H2O2

Substrates: -
Products: -

D-aspartate + H2O + O2

oxaloacetate + NH3 + H2O2

Procambarus clarkii

Substrates: -
Products: -

D-aspartate + H2O + O2

oxaloacetate + NH3 + H2O2

Substrates: -
Products: -

D-aspartate + H2O + O2

oxaloacetate + NH3 + H2O2

391706, 391716, 711719, 711722

Substrates: -
Products: -

D-aspartate + H2O + O2

oxaloacetate + NH3 + H2O2

D-aspartate + H2O + O2

oxaloacetate + NH3 + H2O2

Substrates: -
Products: -

D-aspartate + H2O + O2

oxaloacetate + NH3 + H2O2

Substrates: -
Products: -

D-aspartate + H2O + O2

oxaloacetate + NH3 + H2O2

Scomber japonicus

Substrates: -
Products: -

D-aspartate + H2O + O2

oxaloacetate + NH3 + H2O2

Substrates: -
Products: -

D-aspartate + H2O + O2

oxaloacetate + NH3 + H2O2

391726, 391728

Substrates: -
Products: -

D-aspartate + H2O + O2

oxaloacetate + NH3 + H2O2

Substrates: -
Products: -

D-aspartate + H2O + O2

oxaloacetate + NH3 + H2O2

711719, 712818

Substrates: -
Products: -

D-aspartate + H2O + O2

oxaloacetate + NH3 + H2O2

D-aspartate + H2O + O2

oxaloacetate + NH3 + H2O2

Substrates: -
Products: -

D-aspartate + H2O + O2

oxaloacetate + NH3 + H2O2

Substrates: -
Products: -

D-aspartate + H2O + O2

oxaloacetate + NH3 + H2O2

Substrates: -
Products: -

D-aspartate + H2O + O2

oxaloacetate + NH3 + H2O2

Trachurus japonicus

Substrates: -
Products: -

D-aspartate + H2O + O2

oxaloacetate + NH3 + H2O2

Turbo cornutus

Substrates: -
Products: -

D-aspartate + H2O + O2

oxaloacetate + NH3 + H2O2

Substrates: -
Products: -

D-aspartate + H2O + O2

oxaloacetate + NH3 + H2O2

Substrates: -
Products: -

D-aspartate + H2O + O2

oxaloacetate + NH3 + H2O2

677271

Substrates: DASPO plays an essential role in the assimilation of D-aspartate and acts as a detoxifying agent for D-aspartate. In the wild-type strain, the induction of ChDASPO activity strictly depends on the presence of D-aspartate and is little affected by the copresence of ammonium chloride, but it is significantly reduced by the copresence of both glucose and ammonium chloride, which, however, did not abolish the induction, allowing considerable expression of ChDASPO
Products: -

D-aspartate + H2O + O2

oxaloacetate + NH3 + H2O2

711719, 724597

Substrates: -
Products: -

D-aspartate + H2O + O2

oxaloacetate + NH3 + H2O2

Substrates: -
Products: -

D-aspartate + H2O + O2

oxaloacetate + NH3 + H2O2

Verasper variegatus

Substrates: -
Products: -

D-aspartate + H2O + O2

oxaloacetate + NH3 + H2O2

Xenopus laevis

391708

Substrates: intermediate product is iminoaspartate
Products: -

D-aspartate dimethylester + H2O + O2

oxaloacetic acid dimethylester + H2O2 + NH3

Substrates: -
Products: -

D-aspartate dimethylester + H2O + O2

oxaloacetic acid dimethylester + H2O2 + NH3

Substrates: -
Products: -

D-Glu + H2O + O2

2-oxoglutarate + H2O2 + NH3

Substrates: low activity
Products: -

D-Glu + H2O + O2

2-oxoglutarate + H2O2 + NH3

Q0E9Q7

Substrates: low activity
Products: -

D-Glu + H2O + O2

2-oxoglutarate + NH3 + H2O2

Substrates: preferred substrate
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D-Glu + H2O + O2

2-oxoglutarate + NH3 + H2O2

Substrates: -
Products: -

D-Glu + H2O + O2

2-oxoglutarate + NH3 + H2O2

Substrates: -
Products: -

D-Glu + H2O + O2

2-oxoglutarate + NH3 + H2O2

Substrates: low activity
Products: -

D-glutamate + H2O + O2

2-oxoglutarate + NH3 + H2O2

391705, 391706, 391707, 391717, 391720, 391723

Substrates: -
Products: -

D-glutamate + H2O + O2

2-oxoglutarate + NH3 + H2O2

Substrates: at least two genes encoding functional DASPOs (C47Ap and F18Ep). The two DASPOs differ in their substrate specificities and possibly also in their subcellular localization
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D-glutamate + H2O + O2

2-oxoglutarate + NH3 + H2O2

Substrates: activity is 2.5fold higher than with D-Asp, F18E3.7a gene product
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D-glutamate + H2O + O2

2-oxoglutarate + NH3 + H2O2

Substrates: activity is 67% of the activity with D-Asp, C47A10.5 gene product
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D-glutamate + H2O + O2

2-oxoglutarate + NH3 + H2O2

Substrates: C47Ap exhibits 247% activity and F18Ep exhibits 67% activity compared to D-aspartate as substrate
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D-glutamate + H2O + O2

2-oxoglutarate + NH3 + H2O2

Substrates: preferred substrate. It is possible that excess amounts of D-Glu are as toxic for Caenorhabditis elegans as they are for the silkworm, and that Caenorhabditis elegans needs DDOs to deaminate D-Glu and thereby neutralize the toxicity of diet-derived D-Glu
Products: -

D-glutamate + H2O + O2

2-oxoglutarate + NH3 + H2O2

Substrates: preferred substrate
Products: -

D-glutamate + H2O + O2

2-oxoglutarate + NH3 + H2O2

Substrates: -
Products: -

D-glutamate + H2O + O2

2-oxoglutarate + NH3 + H2O2

Substrates: -
Products: -

D-glutamate + H2O + O2

2-oxoglutarate + NH3 + H2O2

Substrates: -
Products: -

D-glutamate + H2O + O2

2-oxoglutarate + NH3 + H2O2

Substrates: -
Products: -

D-glutamate + H2O + O2

2-oxoglutarate + NH3 + H2O2

391706, 391712

Substrates: -
Products: -

D-glutamate + H2O + O2

2-oxoglutarate + NH3 + H2O2

Substrates: -
Products: -

D-glutamate + H2O + O2

2-oxoglutarate + NH3 + H2O2

Substrates: 14% activity compared to D-aspartate
Products: -

D-glutamate + H2O + O2

2-oxoglutarate + NH3 + H2O2

Q0E9Q7

762748, 762756

Substrates: -
Products: -

D-glutamate + H2O + O2

2-oxoglutarate + NH3 + H2O2

Substrates: -
Products: -

D-glutamate + H2O + O2

2-oxoglutarate + NH3 + H2O2

Substrates: -
Products: -

D-glutamate + H2O + O2

2-oxoglutarate + NH3 + H2O2

Substrates: -
Products: -

D-glutamate + H2O + O2

2-oxoglutarate + NH3 + H2O2

Substrates: ferricyanide and 2,6-dichlorophenolindophenol can also act as electron acceptors instead of O2
Products: -

D-glutamate + H2O + O2

2-oxoglutarate + NH3 + H2O2

Substrates: -
Products: -

D-glutamate + H2O + O2

2-oxoglutarate + NH3 + H2O2

Substrates: -
Products: -

D-glutamate + H2O + O2

2-oxoglutarate + NH3 + H2O2

Substrates: -
Products: -

D-glutamate + H2O + O2

2-oxoglutarate + NH3 + H2O2

Substrates: -
Products: -

D-glutamate + H2O + O2

2-oxoglutarate + NH3 + H2O2

Substrates: -
Products: -

D-glutamate + H2O + O2

2-oxoglutarate + NH3 + H2O2

391726

Substrates: -
Products: -

D-glutamate + H2O + O2

2-oxoglutarate + NH3 + H2O2

Substrates: -
Products: -

D-glutamate + H2O + O2

2-oxoglutarate + NH3 + H2O2

Substrates: -
Products: -

D-glutamate + H2O + O2

2-oxoglutarate + NH3 + H2O2

Thermomyces dupontii NBRC 30541

Substrates: -
Products: -

D-glutamate + H2O + O2

2-oxoglutarate + NH3 + H2O2

Substrates: -
Products: -

D-glutamate + H2O + O2

2-oxoglutarate + NH3 + H2O2

Substrates: -
Products: -

D-glutamate + H2O + O2

2-oxoglutarate + NH3 + H2O2

Substrates: -
Products: -

D-glutamate + H2O + O2

2-oxoglutarate + NH3 + H2O2

Substrates: -
Products: -

D-glutamine + H2O + O2

2-oxoglutaric acid + H2O2 + NH3

Substrates: -
Products: -

D-glutamine + H2O + O2

2-oxoglutaric acid + H2O2 + NH3

Substrates: -
Products: -

D-glutamine + H2O + O2

2-oxoglutaric acid + H2O2 + NH3

Substrates: -
Products: -

D-glutamine + H2O + O2

2-oxoglutaric acid + H2O2 + NH3

Thermomyces dupontii NBRC 30541

Substrates: -
Products: -

D-His + H2O + O2

3-(1H-imidazol-4-yl)-2-oxopropanoic acid + NH3 + H2O2

Substrates: low activity
Products: -

D-His + H2O + O2

3-(1H-imidazol-4-yl)-2-oxopropanoic acid + NH3 + H2O2

Q0E9Q7

Substrates: low activity
Products: -

D-histidine + H2O + O2

3-(1H-imidazol-4-yl)-2-oxopropanoic acid + NH3 + H2O2

Substrates: -
Products: -

D-histidine + H2O + O2

3-(1H-imidazol-4-yl)-2-oxopropanoic acid + NH3 + H2O2

Q0E9Q7

Substrates: -
Products: -

D-homocysteic acid + H2O + O2

2-oxo-4-sulfo-butanoate + NH3 + H2O2

Substrates: -
Products: -

D-homocysteic acid + H2O + O2

2-oxo-4-sulfo-butanoate + NH3 + H2O2

Substrates: -
Products: -

D-hydroxyglutarate + H2O + O2

Substrates: -
Products: -

D-hydroxyglutarate + H2O + O2

Substrates: -
Products: -

D-Pro + H2O + O2

2-oxopentanoic acid + NH3 + H2O2

Substrates: low activity
Products: -

D-Pro + H2O + O2

2-oxopentanoic acid + NH3 + H2O2

Q0E9Q7

Substrates: low activity
Products: -

D-proline + H2O + O2

2-oxopentanoic acid + NH3 + H2O2

391705, 391719, 391720

Substrates: -
Products: -

D-proline + H2O + O2

2-oxopentanoic acid + NH3 + H2O2

Substrates: -
Products: -

meso-2,3-diaminosuccinate + H2O + O2

Substrates: -
Products: -

meso-2,3-diaminosuccinate + H2O + O2

Substrates: -
Products: -

N-acetyl-DL-aspartate + H2O + O2

oxaloacetate + acetylamine + H2O2

Substrates: -
Products: -

N-acetyl-DL-aspartate + H2O + O2

oxaloacetate + acetylamine + H2O2

Substrates: -
Products: -

N-methyl-D-Asp + H2O + O2

oxaloacetate + methylamine + H2O2

Substrates: -
Products: -

N-methyl-D-Asp + H2O + O2

oxaloacetate + methylamine + H2O2

Substrates: high activity
Products: -

N-methyl-D-Asp + H2O + O2

oxaloacetate + methylamine + H2O2

Q0E9Q7

Substrates: high activity
Products: -

N-methyl-D-Asp + H2O + O2

oxaloacetate + methylamine + H2O2

Substrates: -
Products: -

N-methyl-D-Asp + H2O + O2

oxaloacetate + methylamine + H2O2

Substrates: -
Products: -

N-methyl-D-aspartate + H2O + O2

oxaloacetate + CH3NH2 + H2O2

391705, 391706, 391707, 391717

Substrates: -
Products: -

N-methyl-D-aspartate + H2O + O2

oxaloacetate + CH3NH2 + H2O2

Substrates: activity is 3.1fold higher than with D-Asp, F18E3.7a gene product
Products: -

N-methyl-D-aspartate + H2O + O2

oxaloacetate + CH3NH2 + H2O2

Substrates: activity is 1.1fold higher than with D-Asp, C47A10.5 gene product
Products: -

N-methyl-D-aspartate + H2O + O2

oxaloacetate + CH3NH2 + H2O2

Substrates: C47Ap exhibits 313% activity and F18Ep exhibits 110% activity compared to D-aspartate as substrate
Products: -

N-methyl-D-aspartate + H2O + O2

oxaloacetate + CH3NH2 + H2O2

Substrates: -
Products: -

N-methyl-D-aspartate + H2O + O2

oxaloacetate + CH3NH2 + H2O2

Substrates: -
Products: -

N-methyl-D-aspartate + H2O + O2

oxaloacetate + CH3NH2 + H2O2

Substrates: -
Products: -

N-methyl-D-aspartate + H2O + O2

oxaloacetate + CH3NH2 + H2O2

391706, 391712

Substrates: -
Products: -

N-methyl-D-aspartate + H2O + O2

oxaloacetate + CH3NH2 + H2O2

Substrates: -
Products: -

N-methyl-D-aspartate + H2O + O2

oxaloacetate + CH3NH2 + H2O2

Q0E9Q7

Substrates: -
Products: -

N-methyl-D-aspartate + H2O + O2

oxaloacetate + CH3NH2 + H2O2

Substrates: 83% activity compared to D-aspartate
Products: -

N-methyl-D-aspartate + H2O + O2

oxaloacetate + CH3NH2 + H2O2

Q0E9Q7

Substrates: -
Products: -

N-methyl-D-aspartate + H2O + O2

oxaloacetate + CH3NH2 + H2O2

Substrates: -
Products: -

N-methyl-D-aspartate + H2O + O2

oxaloacetate + CH3NH2 + H2O2

Substrates: -
Products: -

N-methyl-D-aspartate + H2O + O2

oxaloacetate + CH3NH2 + H2O2

Substrates: -
Products: -

N-methyl-D-aspartate + H2O + O2

oxaloacetate + CH3NH2 + H2O2

Substrates: -
Products: -

N-methyl-D-aspartate + H2O + O2

oxaloacetate + CH3NH2 + H2O2

Substrates: -
Products: -

N-methyl-D-aspartate + H2O + O2

oxaloacetate + CH3NH2 + H2O2

Substrates: -
Products: -

N-methyl-D-aspartate + H2O + O2

oxaloacetate + CH3NH2 + H2O2

Substrates: -
Products: -

N-methyl-D-aspartate + H2O + O2

oxaloacetate + CH3NH2 + H2O2

Substrates: -
Products: -

N-methyl-D-aspartate + H2O + O2

oxaloacetate + CH3NH2 + H2O2

Thermomyces dupontii NBRC 30541

Substrates: -
Products: -

N-methyl-D-aspartate + H2O + O2

oxaloacetate + CH3NH2 + H2O2

Substrates: -
Products: -

N-methyl-D-aspartate + H2O + O2

oxaloacetate + CH3NH2 + H2O2

Substrates: -
Products: -

N-methyl-D-aspartate + H2O + O2

oxaloacetate + methylamine + H2O2

Substrates: -
Products: -

N-methyl-D-aspartate + H2O + O2

oxaloacetate + methylamine + H2O2

Substrates: -
Products: -

N-methyl-D-aspartate + H2O + O2

oxaloacetate + methylamine + H2O2

Substrates: -
Products: -

N-methyl-D-aspartate + H2O + O2

oxaloacetate + methylamine + H2O2

Substrates: -
Products: -

N-methyl-D-aspartate + H2O + O2

oxaloacetate + methylamine + H2O2

Substrates: -
Products: -

N-methyl-D-aspartate + H2O + O2

oxaloacetate + methylamine + H2O2

Substrates: -
Products: -

N-methyl-D-aspartate + H2O + O2

oxaloacetate + methylamine + H2O2

Substrates: -
Products: -

N-methyl-D-aspartate + H2O + O2

oxaloacetate + methylamine + H2O2

Substrates: -
Products: -

N-methyl-D-aspartate + H2O + O2

oxaloacetate + methylamine + H2O2

Substrates: -
Products: -

N-methyl-D-aspartate + H2O + O2

oxaloacetate + methylamine + H2O2

Substrates: -
Products: -

N-methyl-D-Glu + H2O + O2

2-oxoglutarate + methylamine + H2O2

Substrates: low activity
Products: -

N-methyl-D-Glu + H2O + O2

2-oxoglutarate + methylamine + H2O2

Q0E9Q7

Substrates: low activity
Products: -

N-methyl-L-Asp + H2O + O2

oxaloacetate + methylamine + H2O2

Substrates: low activity
Products: -

N-methyl-L-Asp + H2O + O2

oxaloacetate + methylamine + H2O2

Q0E9Q7

Substrates: low activity
Products: -

additional information

391718

Substrates: chemical modification with phenylglyoxal results in irreversible loss of activity towards dicarboxylic D-amino acids, paralleled with a transient appearance of activity versus monocarboxylic ones
Products: -

additional information

additional information

391720

additional information

Substrates: no detectable activity with L-alanine, L-methionine, and L-arginine
Products: -

additional information

Substrates: H2O2 that is generated in the enzymatic reaction catalyzed by Caenorhabditis elegans DDO-1 and DDO-2 is conceivably degraded by catalase colocalized with each DDO
Products: -

additional information

Substrates: all Caenorhabditis elegans DDOs exhibit the highest catalytic efficiency for D-Glu, but their efficiencies differ considerably for D-Glu, D-Asp, and NMDA. The isozymes show only very low or undetectable levels of activity against the neutral and basic D-amino acids and no activity with L-amino acids and N-methyl-L-Asp
Products: -

additional information

Substrates: in contrast to the mammalian and Cryptococcus humicola DDOs, the three kinds of Caenorhabditis elegans DDOs show relatively higher catalytic efficiency against D-Glu than against D-Asp and NMDA
Products: -

additional information

Substrates: no substrates: D-Asn, D-Gln, D-Ser, D-Thr, D-Tyr, D-Ala, D-Val, D-Leu, D-Ile, D-Pro, D-Phe, D-Met, D-Trp, D-Cys, D-Lys, D-Arg, D-His, L-Asp, L-Glu, LAsn, L-Gln, L-Ser, L-Thr, L-Tyr, L-Ala, L-Val, L-Leu, L-Ile, L-Pro, L-Phe, L-Met, L-Trp, L-Cys, L-Lys, L-Arg, L-His, and Gly
Products: -

additional information

additional information

Substrates: structure-function relationships of DDO, overview
Products: -

additional information

Substrates: the enzyme exhibits low activities towards D-Glu and N-methyl-D-Glu, D-Asn, D-Pro and D-His. There is no activity detected towards D-Gln, D-Ser, D-Thr, D-Tyr, D-Ala, D-Val, D-Leu, D-Ile, D-Phe, D-Met, D-Trp, D-cysteine, D-Lys, D-Arg, L-Asp, L-Glu, N-methyl-L-Glu, L-Asn, L-Gln, L-Ser, L-Thr, L-Tyr, L-Ala, L-Val, L-Leu, L-Ile, L-Pro, L-Phe, L-Met, L-Trp, L-cysteine, L-Lys, L-Arg, L-His, or Gly
Products: -

additional information

additional information

Substrates: D-alanine,D-proline and L-asparagine are no substrates
Products: -

additional information

Substrates: Arg216, Tyr223, Arg237, Arg278, and Ser308 residues of DDO are presumed to be important in catalytic activity and substrate binding, overview
Products: -

additional information

Substrates: structure-function relationships of DDO, overview
Products: -

additional information

Q0E9Q7

Substrates: the enzyme exhibits no activity towards D-Gln, D-Ser, D-Thr, D-Ala, D-Val, D-Leu, D-Phe, D-Met, D-Trp, D-cysteine, D-Lys, D-Arg, L-Asp, L-Glu, L-Asn, L-Gln, L-Ser, L-Thr, L-Ala, L-Val, L-Leu, L-Phe, L-Met, L-Trp, L-cysteine, L-Lys, L-Arg, or L-His
Products: -

additional information

additional information

Substrates: D-AspO activity linearly increases with increasing D-Asp incubation times
Products: -

additional information

Substrates: Arg216, Tyr223, Arg237, Arg278, and Ser308 residues of DDO are presumed to be important in catalytic activity and substrate binding
Products: -

additional information

Substrates: substrate specificities of wild-type and mutants DDOs, overview
Products: -

additional information

Substrates: no activity with D-Ala, D-Ser, D-Pro, D-Val, D-Thr, D-Ile, D-Leu, D-Gln, D-Met, D-Phe, D-Tyr, D-Trp, D-Lys, D-His, D-Arg, and Gly
Products: -

additional information

Substrates: no activity with D-Ala, D-Ser, D-Pro, D-Val, D-Thr, D-Ile, D-Leu, D-Gln, D-Met, D-Phe, D-Tyr, D-Trp, D-Lys, D-His, D-Arg, and Gly
Products: -

show all columns Go to Natural Substrate Search

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NATURAL SUBSTRATE

NATURAL PRODUCT

REACTION DIAGRAM

ORGANISM

UNIPROT

LITERATURE

COMMENTARY

REVERSIBILITY
r=reversible
ir=irreversible
?=not specified

3 meso-2,3-diaminosuccinate + O2

pyrazine 2,5-dicarboxylic acid + pyrazine 2,6-dicarboxylic acid + 4 H2O + H2O2 + 2 NH3

D-Asp + H2O + O2

oxaloacetate + NH3 + H2O2

D-aspartate + H2O + O2

oxaloacetate + NH3 + H2O2

52 entries

D-Glu + H2O + O2

2-oxoglutarate + NH3 + H2O2

D-glutamate + H2O + O2

2-oxoglutarate + NH3 + H2O2

N-methyl-D-Asp + H2O + O2

oxaloacetate + methylamine + H2O2

N-methyl-D-aspartate + H2O + O2

oxaloacetate + methylamine + H2O2

additional information

Substrates: H2O2 that is generated in the enzymatic reaction catalyzed by Caenorhabditis elegans DDO-1 and DDO-2 is conceivably degraded by catalase colocalized with each DDO
Products: -

3 meso-2,3-diaminosuccinate + O2

pyrazine 2,5-dicarboxylic acid + pyrazine 2,6-dicarboxylic acid + 4 H2O + H2O2 + 2 NH3

Substrates: -
Products: -

3 meso-2,3-diaminosuccinate + O2

pyrazine 2,5-dicarboxylic acid + pyrazine 2,6-dicarboxylic acid + 4 H2O + H2O2 + 2 NH3

Substrates: -
Products: -

3 meso-2,3-diaminosuccinate + O2

pyrazine 2,5-dicarboxylic acid + pyrazine 2,6-dicarboxylic acid + 4 H2O + H2O2 + 2 NH3

Substrates: -
Products: -

3 meso-2,3-diaminosuccinate + O2

pyrazine 2,5-dicarboxylic acid + pyrazine 2,6-dicarboxylic acid + 4 H2O + H2O2 + 2 NH3

Substrates: -
Products: -

3 meso-2,3-diaminosuccinate + O2

pyrazine 2,5-dicarboxylic acid + pyrazine 2,6-dicarboxylic acid + 4 H2O + H2O2 + 2 NH3

Substrates: -
Products: -

D-Asp + H2O + O2

oxaloacetate + NH3 + H2O2

Substrates: -
Products: -

D-Asp + H2O + O2

oxaloacetate + NH3 + H2O2

Substrates: high activity
Products: -

D-Asp + H2O + O2

oxaloacetate + NH3 + H2O2

Q0E9Q7

Substrates: high activity
Products: -

D-Asp + H2O + O2

oxaloacetate + NH3 + H2O2

Substrates: -
Products: -

D-Asp + H2O + O2

oxaloacetate + NH3 + H2O2

Substrates: high activity
Products: -

D-Asp + H2O + O2

oxaloacetate + NH3 + H2O2

Substrates: -
Products: -

D-Asp + H2O + O2

oxaloacetate + NH3 + H2O2

Substrates: the enzyme shows high activity only with D-aspartate
Products: -

D-aspartate + H2O + O2

oxaloacetate + NH3 + H2O2

391705, 391706, 391707, 391708, 391711, 391717, 391718, 391719, 391720, 391721, 391722, 391723, 391724, 391725, 711719

Substrates: -
Products: -

D-aspartate + H2O + O2

oxaloacetate + NH3 + H2O2

711719, 725959

Substrates: -
Products: -

D-aspartate + H2O + O2

oxaloacetate + NH3 + H2O2

Substrates: -
Products: -

D-aspartate + H2O + O2

oxaloacetate + NH3 + H2O2

Substrates: -
Products: -

D-aspartate + H2O + O2

oxaloacetate + NH3 + H2O2

Substrates: -
Products: -

D-aspartate + H2O + O2

oxaloacetate + NH3 + H2O2

Chaunax fimbriatus

Substrates: -
Products: -

D-aspartate + H2O + O2

oxaloacetate + NH3 + H2O2

Cololabis saira

Substrates: -
Products: -

D-aspartate + H2O + O2

oxaloacetate + NH3 + H2O2

Substrates: -
Products: -

D-aspartate + H2O + O2

oxaloacetate + NH3 + H2O2

Evynnis tumifrons

Substrates: -
Products: -

D-aspartate + H2O + O2

oxaloacetate + NH3 + H2O2

Substrates: -
Products: -

D-aspartate + H2O + O2

oxaloacetate + NH3 + H2O2

391706, 391712

Substrates: -
Products: -

D-aspartate + H2O + O2

oxaloacetate + NH3 + H2O2

Substrates: this enzyme is proposed to have a role in the inactivation of the synaptically released D-aspartate
Products: -

D-aspartate + H2O + O2

oxaloacetate + NH3 + H2O2

711719, 711325

Substrates: -
Products: -

D-aspartate + H2O + O2

oxaloacetate + NH3 + H2O2

743836, 743063

Substrates: -
Products: -

D-aspartate + H2O + O2

oxaloacetate + NH3 + H2O2

Substrates: -
Products: -

D-aspartate + H2O + O2

oxaloacetate + NH3 + H2O2

Substrates: -
Products: -

D-aspartate + H2O + O2

oxaloacetate + NH3 + H2O2

Meretrix lusoria

Substrates: -
Products: -

D-aspartate + H2O + O2

oxaloacetate + NH3 + H2O2

Substrates: -
Products: -

D-aspartate + H2O + O2

oxaloacetate + NH3 + H2O2

391716, 711719, 711325, 711722

Substrates: -
Products: -

D-aspartate + H2O + O2

oxaloacetate + NH3 + H2O2

Q0E9Q7

Substrates: -
Products: -

D-aspartate + H2O + O2

oxaloacetate + NH3 + H2O2

Substrates: -
Products: -

D-aspartate + H2O + O2

oxaloacetate + NH3 + H2O2

Q0E9Q7

743350, 743836, 742426

Substrates: -
Products: -

D-aspartate + H2O + O2

oxaloacetate + NH3 + H2O2

Substrates: -
Products: -

D-aspartate + H2O + O2

oxaloacetate + NH3 + H2O2

391714, 391716, 391717, 657350

Substrates: -
Products: -

D-aspartate + H2O + O2

oxaloacetate + NH3 + H2O2

Oncorhynchus keta

Substrates: -
Products: -

D-aspartate + H2O + O2

oxaloacetate + NH3 + H2O2

Oncorhynchus masou

Substrates: -
Products: -

D-aspartate + H2O + O2

oxaloacetate + NH3 + H2O2

Substrates: -
Products: -

D-aspartate + H2O + O2

oxaloacetate + NH3 + H2O2

391727, 391728

Substrates: -
Products: -

D-aspartate + H2O + O2

oxaloacetate + NH3 + H2O2

391728, 711719

Substrates: -
Products: -

D-aspartate + H2O + O2

oxaloacetate + NH3 + H2O2

Substrates: -
Products: -

D-aspartate + H2O + O2

oxaloacetate + NH3 + H2O2

Substrates: -
Products: -

D-aspartate + H2O + O2

oxaloacetate + NH3 + H2O2

Substrates: -
Products: -

D-aspartate + H2O + O2

oxaloacetate + NH3 + H2O2

Penaeus japonicus

Substrates: -
Products: -

D-aspartate + H2O + O2

oxaloacetate + NH3 + H2O2

Substrates: -
Products: -

D-aspartate + H2O + O2

oxaloacetate + NH3 + H2O2

Procambarus clarkii

Substrates: -
Products: -

D-aspartate + H2O + O2

oxaloacetate + NH3 + H2O2

Substrates: -
Products: -

D-aspartate + H2O + O2

oxaloacetate + NH3 + H2O2

391706, 391716, 711719, 711722

Substrates: -
Products: -

D-aspartate + H2O + O2

oxaloacetate + NH3 + H2O2

Substrates: -
Products: -

D-aspartate + H2O + O2

oxaloacetate + NH3 + H2O2

Substrates: -
Products: -

D-aspartate + H2O + O2

oxaloacetate + NH3 + H2O2

Scomber japonicus

Substrates: -
Products: -

D-aspartate + H2O + O2

oxaloacetate + NH3 + H2O2

Substrates: -
Products: -

D-aspartate + H2O + O2

oxaloacetate + NH3 + H2O2

391726, 391728, 711719, 712818, 723870

Substrates: -
Products: -

D-aspartate + H2O + O2

oxaloacetate + NH3 + H2O2

Substrates: -
Products: -

D-aspartate + H2O + O2

oxaloacetate + NH3 + H2O2

Substrates: -
Products: -

D-aspartate + H2O + O2

oxaloacetate + NH3 + H2O2

Trachurus japonicus

Substrates: -
Products: -

D-aspartate + H2O + O2

oxaloacetate + NH3 + H2O2

Turbo cornutus

Substrates: -
Products: -

D-aspartate + H2O + O2

oxaloacetate + NH3 + H2O2

Substrates: -
Products: -

D-aspartate + H2O + O2

oxaloacetate + NH3 + H2O2

677271

D-aspartate + H2O + O2

oxaloacetate + NH3 + H2O2

711719, 724597

Substrates: -
Products: -

D-aspartate + H2O + O2

oxaloacetate + NH3 + H2O2

Substrates: -
Products: -

D-aspartate + H2O + O2

oxaloacetate + NH3 + H2O2

Verasper variegatus

Substrates: -
Products: -

D-aspartate + H2O + O2

oxaloacetate + NH3 + H2O2

Xenopus laevis

391708

Substrates: intermediate product is iminoaspartate
Products: -

D-Glu + H2O + O2

2-oxoglutarate + NH3 + H2O2

Substrates: preferred substrate
Products: -

D-Glu + H2O + O2

2-oxoglutarate + NH3 + H2O2

Substrates: -
Products: -

N-methyl-D-Asp + H2O + O2

oxaloacetate + methylamine + H2O2

Substrates: -
Products: -

N-methyl-D-Asp + H2O + O2

oxaloacetate + methylamine + H2O2

Substrates: -
Products: -

N-methyl-D-aspartate + H2O + O2

oxaloacetate + methylamine + H2O2

Substrates: -
Products: -

N-methyl-D-aspartate + H2O + O2

oxaloacetate + methylamine + H2O2

Substrates: -
Products: -

N-methyl-D-aspartate + H2O + O2

oxaloacetate + methylamine + H2O2

Substrates: -
Products: -

N-methyl-D-aspartate + H2O + O2

oxaloacetate + methylamine + H2O2

Substrates: -
Products: -

N-methyl-D-aspartate + H2O + O2

oxaloacetate + methylamine + H2O2

Substrates: -
Products: -

N-methyl-D-aspartate + H2O + O2

oxaloacetate + methylamine + H2O2

Substrates: -
Products: -

N-methyl-D-aspartate + H2O + O2

oxaloacetate + methylamine + H2O2

Substrates: -
Products: -

show all columns Go to Cofactor Search

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COFACTOR

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

IMAGE

FAD

46 entries

FMN

10% activity when FAD is replaced with FMN

FAD

391706, 391707, 391708, 391711, 391717, 391718, 391720, 391724, 391725

FAD

391706, 391716

FAD

391706, 391709, 391712

FAD

FAD

FAD

FAD

FAD

FAD

FAD

FAD

FAD

FAD

FAD

FAD

1 mol flavin per mol protein

391719, 391721

FAD

1 mol flavin per mol protein

FAD

FAD

dependent

FAD

FAD

one molecule of FAD is noncovalently bound to one molecule of DDO, the enzyme contains a FAD-binding consensus sequence Gly-X-Gly-X-X-Gly

FAD

one molecule of FAD is noncovalently bound to one molecule of DDO, the enzyme contains a FAD-binding consensus sequence Gly-X-Gly-X-X-Gly

FAD

one molecule of FAD is noncovalently bound to one molecule of DDO, the enzyme contains a FAD-binding consensus sequence Gly-X-Gly-X-X-Gly

FAD

one molecule of FAD is noncovalently bound to one molecule of DDO, the enzyme contains a FAD-binding consensus sequence Gly-X-Gly-X-X-Gly

FAD

one molecule of FAD is noncovalently bound to one molecule of DDO

FAD

one molecule of FAD is noncovalently bound to one molecule of DDO, the enzyme contains a FAD-binding consensus sequence Gly-X-Gly-X-X-Gly

FAD

one molecule of FAD is noncovalently bound to one molecule of DDO, the enzyme contains a FAD-binding consensus sequence Gly-X-Gly-X-X-Gly

FAD

FAD

FAD

FAD

FAD

FAD

FAD

FAD

one molecule of FAD is noncovalently bound to one molecule of DDO

FAD

FAD

FAD

Q0E9Q7

FAD

FAD

FAD

Q0E9Q7

FAD

Kd value 0.128 microM

FAD

Q0E9Q7

FAD

typical absorption spectrum associated with flavoproteins with maxima at 273, 375, and 455 nm

FAD

the flavin ring is located at the interface between the two protein domains, with nearly all hydrogen-bond donors and acceptors of FAD interacting with protein atoms

FAD

flavoprotein with a noncovalently but tightly attached FAD

FAD

Q0E9Q7

protein shows a classical absorbance spectrum of a FAD-containing protein, with absorbance maxima at 449, 361 and 273 nm, and a 273 nm/449 nm absorbance ratio of 10.4

show all columns Go to Metals and Ions Search

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METALS and IONS

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

additional information

additional information

not influenced by Na+, K+, Mg2+, Ca2+, Co2+, Mn2+, and Zn2+

additional information

not influenced by Na+, K+, Mg2+, Ca2+, Co2+, Mn2+, and Zn2+

show all columns Go to Inhibitor Search

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INHIBITOR

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

IMAGE

(5R)-4-hydroxy-3,5-dimethyl-5-[(1E)-2-methyl-1,3-butadienyl]-2(5H)-thiophenone

1-hydroxy-1H-indole-2-carboxylic acid

2-amino-5-chlorobenzoic acid

2-amino-5-methylthiophene-3-carboxylic acid

2-aminopyridine-3-carboxylic acid

2-aminopyridine-4-carboxylic acid

2-hydroxy-6-methylpyridine-3-carboxylic acid

2-oxoglutaric acid

at 6.67 mM 64% inhibition

3-aminobenzoic acid

3-aminopyridine-2-carboxylic acid

3-aminopyridine-4-carboxylic acid

3-hydroxypyridine-2-carboxylic acid

4-aminopyridine-2-carboxylic acid

4-aminopyridine-3-carboxylic acid

4-carbamoylthiophene-2-carboxylic acid

5-(dimethylamino)pyridine-3-carboxylic acid

5-(methylamino)pyridine-3-carboxylic acid

5-(trifluoromethyl)pyridine-3-carboxylic acid

5-aminonicotinic acid

5-aminopyridine-2-carboxylic acid

5-bromopyridine-3-carboxylic acid

5-chloro-2-hydroxybenzoic acid

5-chloropyridine-3-carboxylic acid

5-fluoro-2-hydroxybenzoic acid

5-fluoropyridine-3-carboxylic acid

5-hydroxypyridine-3-carboxylic acid

5-methoxypyridine-3-carboxylic acid

5-methylpyridine-3-carboxylic acid

5-nitropyridine-3-carboxylic acid

5-phenylpyridine-3-carboxylic acid

5-sulfopyridine-3-carboxylic acid

6-aminopyridine-2-carboxylic acid

6-aminopyridine-3-carboxylic acid

7-hydroxy-4-hydro-1,2,4-triazolo[4,3-a]pyrimidine-6-carboxylic acid

adipic acid

at 6.67 mM 15% inhibition

Aminooxyacetate

benzoate

benzoic acid

Citric acid

at 6.67 mM 29% inhibition

Cu2+

90.7% residual activity at 1 mM

D-malate

D-Tartaric acid

at 6.67 mM 77% inhibition

Fe2+

86.5% residual activity at 1 mM

Fumaric acid

at 6.67 mM 78% inhibition

Glutaric acid

at 6.67 mM 62% inhibition

KCN

L-Glu

89.3% residual activity at 1 mM

L-leucine

6% inhibition at 6.67 mM

L-Malic acid

at 6.67 mM 79% inhibition

L-Tartaric acid

at 6.67 mM 24% inhibition

L-Tartrate

L-valine

6% inhibition at 6.67 mM

malate

52% inhibition at 50 mM

malonate

malonic acid

meso-tartrate

N-Methyl-D-aspartate

substrate inhibition

Ni2+

93.3% residual activity at 1 mM

olanzapine

oxalic acid

at 6.67 mM 40% inhibition

oxaloacetic acid

at 6.67 mM 90% inhibition

pyridin-3-amine

pyridine-3,5-dicarboxylic acid

pyridine-3-carboxylic acid

pyridoxal 5'-phosphate

93.5% residual activity at 0.2 mM

pyrido[2,3-b]pyrazine-2,3(1H,4H)-dione

Q0E9Q7

Kd value 19.8 microM

succinic acid

at 6.67 mM 66% inhibition

thiolactomycin

additional information

(5R)-4-hydroxy-3,5-dimethyl-5-[(1E)-2-methyl-1,3-butadienyl]-2(5H)-thiophenone

i.e. thiolactomycin, active site-directed DDO inhibitor, competitive inhibition, competes with both the substrate and the coenzyme FAD; i.e. thiolactomycin, competitive inhibition, competes with both the substrate and the coenzyme FAD

(5R)-4-hydroxy-3,5-dimethyl-5-[(1E)-2-methyl-1,3-butadienyl]-2(5H)-thiophenone

i.e. thiolactomycin, active site-directed DDO inhibitor involving binding via Arg237, mixed type of inhibition, competes with both the substrate and the coenzyme FAD, structural models of mouse DDO/TLM complexes; i.e. thiolactomycin, competitive inhibition, competes with both the substrate and the coenzyme FAD

5-aminonicotinic acid

5-aminonicotinic acid

Q0E9Q7

directly binds to the active site

5-aminonicotinic acid

Q0E9Q7

Kd value 5.7 microM

5-aminonicotinic acid

directly binds to the active site

Aminooxyacetate

66.4% residual activity at 1 mM

Aminooxyacetate

Q0E9Q7

Aminooxyacetate

benzoate

31% inhibition at 10 mM

benzoate

43% inhibition at 10 mM

D-malate

90% inhibition at 0.33 mM

D-malate

competitive inhibitor, at 20 mM 34% inhibition

D-malate

33% inhibition

D-malate

87.8% residual activity at 10 mM

L-Tartrate

391705, 391707, 391708

L-Tartrate

competitive inhibitor

L-Tartrate

at 10 mM

malonate

malonate

malonate

malonate

malonate

competitive inhibition

malonate

malonate

Q0E9Q7

malonate

at 0.66 mM 78% inhibition

malonate

malonate

malonate

malonate

malonate

competitive inhibitor, at 20 mM 53% inhibition

malonate

60% inhibition

malonate

malonate

62.1% residual activity at 10 mM

meso-tartrate

meso-tartrate

meso-tartrate

56% inhibition at 40 mM

meso-tartrate

53% inhibition at 40 mM

meso-tartrate

meso-tartrate

meso-tartrate

52% inhibition 50 mM

meso-tartrate

competitive inhibition

meso-tartrate

meso-tartrate

Q0E9Q7

meso-tartrate

34% inhibition at 10 mM

meso-tartrate

meso-tartrate

meso-tartrate

meso-tartrate

34% inhibition at 10 mM

meso-tartrate

meso-tartrate

meso-tartrate

70% inhibition at 10 mM

meso-tartrate

high affinity for meso-tartrate

meso-tartrate

meso-tartrate

9% inhibition at 20 mM

meso-tartrate

olanzapine

olanzapine

Q0E9Q7

thiolactomycin

thiolactomycin

thiolactomycin

thiolactomycin

thiolactomycin

thiolactomycin

thiolactomycin

thiolactomycin

additional information

not inhibited by EDTA, ATP, ADP, AMP, cAMP, and L-Asp

additional information

not inhibited by EDTA, ATP, ADP, AMP, cAMP, and L-Asp

additional information

not inhibited by clozapine, chlorpromazine, haloperidol, bupropion, fluoxetine, and amitriptyline

additional information

not inhibited by clozapine, chlorpromazine, haloperidol, bupropion, fluoxetine, and amitriptyline

additional information

benzoate has no inhibitory effect

additional information

Q0E9Q7

not inhibited by clozapine, chlorpromazine, haloperidol, bupropion, fluoxetine, and amitriptyline

additional information

not inhibited by 10 mM meso-tartrate, benzoate, anthranilate, and crotonate

additional information

not inhibited by 10 mM meso-tartrate, benzoate, anthranilate, and crotonate

show all columns Go to Activating Compound Search

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ACTIVATING COMPOUND

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

IMAGE

D-Aspartate

substrate activation at D-aspartate concentrations above 0.2 mM

D-Glu

substrate activation at D-glutamate concentrations above 4 mM

Go to Disease Search

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DISEASE

TITLE OF PUBLICATION

LINK TO PUBMED

Dyskinesias

Higher free D-aspartate and N-methyl-D-aspartate levels prevent striatal depotentiation and anticipate L-DOPA-induced dyskinesia.

21946266

Zellweger Syndrome

The human L-pipecolic acid oxidase is similar to bacterial monomeric sarcosine oxidases rather than D-amino acid oxidases.

11330064

show all columns Go to KM Value Search

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KM VALUE [mM]

SUBSTRATE

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

IMAGE

4.5

cis-2,3-piperidine dicarboxylic acid

742

D-alanine

pH and temperature not specified in the publication

16.2

D-alpha-aminoadipic acid

83.4

D-Asn

mutant enzyme H56N, at pH 7.5 and 37°C

1 - 13.4

D-Asp

16 entries

0.38 - 240

D-asparagine

0.38 - 8.77

D-Aspartate

31 entries

150 - 540

D-aspartate dimethylester

D-aspartic acid-beta-hydroxamate

21 - 39.4

D-Gln

0.68 - 106

D-Glu

9 entries

0.23 - 166

D-glutamate

19 entries

25.7 - 815

D-glutamine

8.8 - 96

D-histidine

9.8

D-homocysteic acid

8.8

D-Leu

mutant enzyme H56N, at pH 7.5 and 37°C

8.5 - 31.8

D-Met

14.3 - 34.8

D-Phe

0.9 - 440

D-proline

15.2

DL-2-amino-3-phosphonopropanoic acid

1.7

DL-cysteic acid

143

glycyl-D-aspartic acid

4.8

meso-2,3-Diaminosuccinate

2.85 - 27.9

N-methyl-D-Asp

0.84 - 1.84

N-methyl-D-asparagine

0.2 - 103

N-Methyl-D-aspartate

20 entries

0.17 - 2.01

6 entries

additional information

D-Asp

pH 7.0, 20°C, recombinant mutant R243D

D-Asp

pH 7.0, 20°C, recombinant mutant R243E

2.1

D-Asp

at pH 8.3 and 37°C

2.26

D-Asp

at pH 8.3 and 37°C

2.5

D-Asp

pH 7.0, 20°C, recombinant wild-type enzyme

2.5

D-Asp

wild type enzyme, at pH 7.5 and 37°C

3.8

D-Asp

pH 7.0, 20°C, recombinant mutant R243M

3.81

D-Asp

pH 8.3, 37°C, recombinant DDO-3

4.2

D-Asp

pH 8.3, 37°C, recombinant DDO-2

4.22

D-Asp

pH 8.2, 37°C, kidney

4.26

D-Asp

pH 8.2, 37°C, brain

4.41

D-Asp

pH 8.2, 37°C, liver

5.54

D-Asp

pH 8.3, 37°C, recombinant DDO-1

7.37

D-Asp

Q0E9Q7

at pH 8.3 and 37°C

10.3

D-Asp

pH 7.0, 20°C, recombinant mutant R243K

13.4

D-Asp

pH 7.0, 20°C, recombinant mutant R243A

0.38

D-asparagine

recombinant F18Ep protein, in 40 mM sodium diphosphate buffer (pH 8.3), at 37°C

2.02

D-asparagine

recombinant C47Ap protein, in 40 mM sodium diphosphate buffer (pH 8.3), at 37°C

D-asparagine

D-asparagine

D-asparagine

wild-type, pH 8.3, 25°C

101.4

D-asparagine

Q0E9Q7

pH 8.3, 25°C

240

D-asparagine

0.38

D-Aspartate

37°C, pH 8.3, F18E3.7a gene product

0.86

D-Aspartate

O2 as acceptor

0.87

D-Aspartate

mutant F248Y, pH 7, 60°C

1.05

D-Aspartate

wild-type, pH 8.3, 25°C

1.2

D-Aspartate

Q0E9Q7

mutant enzyme S308G fused N-terminally with glutathione S-transferase, at 37°C in 40 mM sodium diphosphate buffer (pH 8.3)

1.3

D-Aspartate

pH and temperature not specified in the publication

1.6

D-Aspartate

at 25°C

1.78

D-Aspartate

Q0E9Q7

mutant enzyme S308A fused N-terminally with glutathione S-transferase, at 37°C in 40 mM sodium diphosphate buffer (pH 8.3)

2.02

D-Aspartate

37°C, pH 8.3, C47A10.5 gene product

2.1

D-Aspartate

Q0E9Q7

pH 8.3, 25°C

2.2

D-Aspartate

at 4°C

2.37

D-Aspartate

Q0E9Q7

His-tagged mutant enzyme S308G, at 37°C in 40 mM sodium diphosphate buffer (pH 8.3)

2.5

D-Aspartate

at pH 8.3

2.7

D-Aspartate

2.7

D-Aspartate

2.9

D-Aspartate

37°C, pH 7.5

3.7

D-Aspartate

3.7

D-Aspartate

4.3

D-Aspartate

4.5

D-Aspartate

4.87

D-Aspartate

Q0E9Q7

wild type enzyme fused N-terminally with glutathione S-transferase, at 37°C in 40 mM sodium diphosphate buffer (pH 8.3)

5.19

D-Aspartate

5.2

D-Aspartate

ferricyanide as acceptor

5.5

D-Aspartate

pH not specified in the publication, temperature not specified in the publication

5.7

D-Aspartate

at pH 7.4

5.8

D-Aspartate

7.3

D-Aspartate

Q0E9Q7

His-tagged wild type enzyme, at 37°C in 40 mM sodium diphosphate buffer (pH 8.3)

7.5

D-Aspartate

pH not specified in the publication, temperature not specified in the publication

7.63

D-Aspartate

Q0E9Q7

mutant enzyme S308Y, at 37°C in 40 mM sodium diphosphate buffer (pH 8.3)

7.7

D-Aspartate

8.77

D-Aspartate

wild-type, pH 7, 60°C

150

D-aspartate dimethylester

540

D-aspartate dimethylester

D-Gln

mutant enzyme H56N, at pH 7.5 and 37°C

39.4

D-Gln

mutant enzyme H56A, at pH 7.5 and 37°C

0.68

D-Glu

pH 8.3, 37°C, recombinant DDO-3

0.8

D-Glu

pH 8.3, 37°C, recombinant DDO-2

1.06

D-Glu

pH 8.3, 37°C, recombinant DDO-1

2.6

D-Glu

pH 7.0, 20°C, recombinant wild-type enzyme

6.77

D-Glu

pH 8.2, 37°C, kidney

6.91

D-Glu

pH 8.2, 37°C, brain

7.52

D-Glu

pH 8.2, 37°C, liver

106

D-Glu

pH 7.0, 20°C, recombinant wild-type enzyme

106

D-Glu

wild type enzyme, at pH 7.5 and 37°C

0.23

D-glutamate

37°C, pH 8.3, C47A10.5 gene product

0.23

D-glutamate

recombinant C47Ap protein, in 40 mM sodium diphosphate buffer (pH 8.3), at 37°C

0.25

D-glutamate

37°C, pH 8.3, F18E3.7a gene product

0.25

D-glutamate

recombinant F18Ep protein, in 40 mM sodium diphosphate buffer (pH 8.3), at 37°C

0.59

D-glutamate

at pH 8.3

0.71

D-glutamate

mutant F248Y, pH 7, 60°C

2.1

D-glutamate

at pH 7.4

2.16

D-glutamate

wild-type, pH 7, 60°C

5.6

D-glutamate

5.7

D-glutamate

ferricyanide as acceptor

6.2

D-glutamate

8.8

D-glutamate

9.7

D-glutamate

9.7

D-glutamate

31.5

D-glutamate

wild-type, pH 8.3, 25°C

62.6

D-glutamate

37°C, pH 7.5

68.4

D-glutamate

Q0E9Q7

pH 8.3, 25°C

152

D-glutamate

166

D-glutamate

O2 as acceptor

25.7

D-glutamine

mutant F248Y, pH 7, 60°C

108

D-glutamine

wild-type, pH 7, 60°C

600

D-glutamine

815

D-glutamine

815

D-glutamine

8.8

D-histidine

Q0E9Q7

pH 8.3, 25°C

D-histidine

wild-type, pH 8.3, 25°C

8.5

D-Met

mutant enzyme H56A, at pH 7.5 and 37°C

31.8

D-Met

mutant enzyme H56N, at pH 7.5 and 37°C

14.3

D-Phe

mutant enzyme H56A, at pH 7.5 and 37°C

34.8

D-Phe

mutant enzyme H56N, at pH 7.5 and 37°C

0.9

D-proline

169

D-proline

Q0E9Q7

pH 8.3, 25°C

339

D-proline

wild-type, pH 8.3, 25°C

440

D-proline

2.85

N-methyl-D-Asp

pH 8.2, 37°C, kidney

3.05

N-methyl-D-Asp

pH 8.2, 37°C, brain

3.41

N-methyl-D-Asp

pH 8.2, 37°C, liver

8.87

N-methyl-D-Asp

pH 8.3, 37°C, recombinant DDO-3

9.23

N-methyl-D-Asp

pH 8.3, 37°C, recombinant DDO-2

14.6

N-methyl-D-Asp

pH 8.3, 37°C, recombinant DDO-1

15.7

N-methyl-D-Asp

pH 7.0, 20°C, recombinant wild-type enzyme

27.9

N-methyl-D-Asp

pH 7.0, 20°C, recombinant wild-type enzyme

0.84

N-methyl-D-asparagine

recombinant C47Ap protein, in 40 mM sodium diphosphate buffer (pH 8.3), at 37°C

1.84

N-methyl-D-asparagine

recombinant F18Ep protein, in 40 mM sodium diphosphate buffer (pH 8.3), at 37°C

0.2

N-Methyl-D-aspartate

0.84

N-Methyl-D-aspartate

37°C, pH 8.3, C47A10.5 gene product

1.5

N-Methyl-D-aspartate

1.84

N-Methyl-D-aspartate

37°C, pH 8.3, F18E3.7a gene product

1.95

N-Methyl-D-aspartate

Q0E9Q7

mutant enzyme S308G fused N-terminally with glutathione S-transferase, at 37°C in 40 mM sodium diphosphate buffer (pH 8.3)

2.67

N-Methyl-D-aspartate

Q0E9Q7

His-tagged mutant enzyme S308G, at 37°C in 40 mM sodium diphosphate buffer (pH 8.3)

2.76

N-Methyl-D-aspartate

wild-type, pH 8.3, 25°C

4.2

N-Methyl-D-aspartate

Q0E9Q7

pH 8.3, 25°C

4.23

N-Methyl-D-aspartate

Q0E9Q7

mutant enzyme S308A fused N-terminally with glutathione S-transferase, at 37°C in 40 mM sodium diphosphate buffer (pH 8.3)

6.59

N-Methyl-D-aspartate

Q0E9Q7

wild type enzyme fused N-terminally with glutathione S-transferase, at 37°C in 40 mM sodium diphosphate buffer (pH 8.3)

6.7

N-Methyl-D-aspartate

mutant F248Y, pH 7, 60°C

6.8

N-Methyl-D-aspartate

7.81

N-Methyl-D-aspartate

Q0E9Q7

mutant enzyme S308Y fused N-terminally with glutathione S-transferase, at 37°C in 40 mM sodium diphosphate buffer (pH 8.3)

8.02

N-Methyl-D-aspartate

Q0E9Q7

His-tagged wild type enzyme, at 37°C in 40 mM sodium diphosphate buffer (pH 8.3)

N-Methyl-D-aspartate

N-Methyl-D-aspartate

N-Methyl-D-aspartate

47.7

N-Methyl-D-aspartate

85.3

N-Methyl-D-aspartate

37°C, pH 7.5

103

N-Methyl-D-aspartate

wild-type, pH 7, 60°C

0.17

at 4°C

0.34

wild-type, pH 8.3, 25°C

0.46

at 25°C

0.547

apparent value, using D-glutamate as substrate

0.613

apparent value, using D-aspartate as substrate

2.01

apparent value, using N-methyl-D-aspartate as substrate

additional information

kinetics of wild-type and mutant enzymes, overview

additional information

D-AspO kinetics in different tissues, overview

additional information

kinetics in comparison to the human DDO, overview

show all columns Go to Turnover Number Search

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TURNOVER NUMBER [1/s]

SUBSTRATE

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

IMAGE

1.62

D-alanine

pH and temperature not specified in the publication

3.9

D-Asn

mutant enzyme H56N, at pH 7.5 and 37°C

1.3 - 121

D-Asp

12 entries

3.07 - 11.4

D-asparagine

0.183 - 123

D-Aspartate

11 entries

2.2 - 4.5

D-Gln

0.76 - 35.4

D-Glu

2 - 217

D-glutamate

9 entries

39.9 - 144

D-glutamine

0.71 - 1.2

D-histidine

0.7

D-Leu

mutant enzyme H56N, at pH 7.5 and 37°C

4 - 11.5

D-Met

3.1 - 4.1

D-Phe

1.2 - 5.5

D-proline

1.52 - 84.5

N-methyl-D-Asp

3 - 6.13

N-methyl-D-asparagine

3 - 155

N-Methyl-D-aspartate

30 - 635

1.3

D-Asp

pH 7.0, 20°C, recombinant mutant R243E

1.4

D-Asp

pH 7.0, 20°C, recombinant mutant R243K

2.51

D-Asp

pH 8.3, 37°C, recombinant DDO-3

9.49

D-Asp

pH 8.3, 37°C, recombinant DDO-2

9.83

D-Asp

Q0E9Q7

at pH 8.3 and 37°C

26.1

D-Asp

pH 8.3, 37°C, recombinant DDO-1

31.1

D-Asp

at pH 8.3 and 37°C

62.6

D-Asp

pH 7.0, 20°C, recombinant mutant R243M

68.4

D-Asp

at pH 8.3 and 37°C

74.5

D-Asp

pH 7.0, 20°C, recombinant wild-type enzyme

74.5

D-Asp

wild type enzyme, at pH 7.5 and 37°C

121

D-Asp

pH 7.0, 20°C, recombinant mutant R243D

3.07

D-asparagine

recombinant F18Ep protein, in 40 mM sodium diphosphate buffer (pH 8.3), at 37°C

4.29

D-asparagine

recombinant C47Ap protein, in 40 mM sodium diphosphate buffer (pH 8.3), at 37°C

8.3

D-asparagine

wild-type, pH 8.3, 25°C

11.4

D-asparagine

Q0E9Q7

pH 8.3, 25°C

0.183

D-Aspartate

0.183

D-Aspartate

50 mM potassium phosphate buffer, 0.3 mM EDTA, pH 7.4, 4°C

0.725

D-Aspartate

50 mM potassium phosphate buffer, 0.3 mM EDTA, pH 7.4, 25°C

3.07

D-Aspartate

37°C, pH 8.3, F18E3.7a gene product

3.13

D-Aspartate

37°C, pH 8.3, C47A10.5 gene product

27.9

D-Aspartate

pH and temperature not specified in the publication

50.9

D-Aspartate

mutant F248Y, pH 7, 60°C

58.4

D-Aspartate

Q0E9Q7

pH 8.3, 25°C

81.3

D-Aspartate

wild-type, pH 8.3, 25°C

82.6

D-Aspartate

37°C, pH 7.5

123

D-Aspartate

wild-type, pH 7, 60°C

2.2

D-Gln

mutant enzyme H56A, at pH 7.5 and 37°C

4.5

D-Gln

mutant enzyme H56N, at pH 7.5 and 37°C

0.76

D-Glu

pH 8.3, 37°C, recombinant DDO-3

2.6

D-Glu

wild type enzyme, at pH 7.5 and 37°C

3.01

D-Glu

pH 8.3, 37°C, recombinant DDO-2

35.4

D-Glu

pH 8.3, 37°C, recombinant DDO-1

D-glutamate

37°C, pH 7.5

2.11

D-glutamate

37°C, pH 8.3, F18E3.7a gene product

2.11

D-glutamate

recombinant F18Ep protein, in 40 mM sodium diphosphate buffer (pH 8.3), at 37°C

5.31

D-glutamate

37°C, pH 8.3, C47A10.5 gene product

5.31

D-glutamate

recombinant C47Ap protein, in 40 mM sodium diphosphate buffer (pH 8.3), at 37°C

11.3

D-glutamate

wild-type, pH 8.3, 25°C

16.8

D-glutamate

Q0E9Q7

pH 8.3, 25°C

58.1

D-glutamate

mutant F248Y, pH 7, 60°C

217

D-glutamate

wild-type, pH 7, 60°C

39.9

D-glutamine

mutant F248Y, pH 7, 60°C

144

D-glutamine

wild-type, pH 7, 60°C

0.71

D-histidine

Q0E9Q7

pH 8.3, 25°C

1.2

D-histidine

wild-type, pH 8.3, 25°C

D-Met

mutant enzyme H56N, at pH 7.5 and 37°C

11.5

D-Met

mutant enzyme H56A, at pH 7.5 and 37°C

3.1

D-Phe

mutant enzyme H56A, at pH 7.5 and 37°C

4.1

D-Phe

mutant enzyme H56N, at pH 7.5 and 37°C

1.2

D-proline

wild-type, pH 8.3, 25°C

5.5

D-proline

Q0E9Q7

pH 8.3, 25°C

1.52

N-methyl-D-Asp

pH 8.3, 37°C, recombinant DDO-3

6.04

N-methyl-D-Asp

pH 8.3, 37°C, recombinant DDO-2

84.5

N-methyl-D-Asp

pH 8.3, 37°C, recombinant DDO-1

N-methyl-D-asparagine

recombinant F18Ep protein, in 40 mM sodium diphosphate buffer (pH 8.3), at 37°C

6.13

N-methyl-D-asparagine

recombinant C47Ap protein, in 40 mM sodium diphosphate buffer (pH 8.3), at 37°C

N-Methyl-D-aspartate

37°C, pH 8.3, F18E3.7a gene product

6.13

N-Methyl-D-aspartate

37°C, pH 8.3, C47A10.5 gene product

38.1

N-Methyl-D-aspartate

37°C, pH 7.5

68.9

N-Methyl-D-aspartate

mutant F248Y, pH 7, 60°C

73.6

N-Methyl-D-aspartate

wild-type, pH 8.3, 25°C

112.1

N-Methyl-D-aspartate

Q0E9Q7

pH 8.3, 25°C

155

N-Methyl-D-aspartate

wild-type, pH 7, 60°C

apparent value, using D-glutamate as substrate

172

apparent value, using D-aspartate as substrate

635

apparent value, using N-methyl-D-aspartate as substrate

show all columns Go to kcat/KM Value Search

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kcat/KM VALUE [1/mMs^-1]

SUBSTRATE

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

IMAGE

0.047

D-Asn

mutant enzyme H56N, at pH 7.5 and 37°C

1.354 - 121000

D-Asp

12 entries

0.11 - 0.12

D-asparagine

14 - 77.4

D-Aspartate

0.055 - 0.213

D-Gln

0.024 - 33440

D-Glu

0.25 - 100

D-glutamate

1.3 - 15.5

D-glutamine

0.011 - 0.08

D-histidine

0.074

D-Leu

mutant enzyme H56N, at pH 7.5 and 37°C

0.125 - 1.35

D-Met

0.119 - 0.218

D-Phe

0.003 - 0.03

D-proline

172 - 5787

N-methyl-D-Asp

1.5 - 26.7

N-Methyl-D-aspartate

1.354

D-Asp

Q0E9Q7

at pH 8.3 and 37°C

14.104

D-Asp

at pH 8.3 and 37°C

29.8

D-Asp

wild type enzyme, at pH 7.5 and 37°C

32.651

D-Asp

at pH 8.3 and 37°C

136

D-Asp

pH 7.0, 20°C, recombinant mutant R243K

650

D-Asp

pH 7.0, 20°C, recombinant mutant R243E

658

D-Asp

pH 8.3, 37°C, recombinant DDO-3

2258

D-Asp

pH 8.3, 37°C, recombinant DDO-2

4712

D-Asp

pH 8.3, 37°C, recombinant DDO-1

16500

D-Asp

pH 7.0, 20°C, recombinant mutant R243M

29800

D-Asp

pH 7.0, 20°C, recombinant wild-type enzyme

121000

D-Asp

pH 7.0, 20°C, recombinant mutant R243D

0.11

D-asparagine

Q0E9Q7

pH 8.3, 25°C

0.12

D-asparagine

wild-type, pH 8.3, 25°C

D-Aspartate

wild-type, pH 7, 60°C

27.8

D-Aspartate

Q0E9Q7

pH 8.3, 25°C

58.6

D-Aspartate

mutant F248Y, pH 7, 60°C

77.4

D-Aspartate

wild-type, pH 8.3, 25°C

0.055

D-Gln

mutant enzyme H56A, at pH 7.5 and 37°C

0.213

D-Gln

mutant enzyme H56N, at pH 7.5 and 37°C

0.024

D-Glu

wild type enzyme, at pH 7.5 and 37°C

D-Glu

pH 7.0, 20°C, recombinant wild-type enzyme

1117

D-Glu

pH 8.3, 37°C,recombinant DDO-3

1117

D-Glu

pH 8.3, 37°C, recombinant DDO-3

3759

D-Glu

pH 8.3, 37°C,recombinant DDO-2

3759

D-Glu

pH 8.3, 37°C, recombinant DDO-2

33440

D-Glu

pH 8.3, 37°C, recombinant DDO-1

0.25

D-glutamate

Q0E9Q7

pH 8.3, 25°C

0.36

D-glutamate

wild-type, pH 8.3, 25°C

D-glutamate

mutant F248Y, pH 7, 60°C

100

D-glutamate

wild-type, pH 7, 60°C

1.3

D-glutamine

wild-type, pH 7, 60°C

15.5

D-glutamine

mutant F248Y, pH 7, 60°C

0.011

D-histidine

wild-type, pH 8.3, 25°C

0.08

D-histidine

Q0E9Q7

pH 8.3, 25°C

0.125

D-Met

mutant enzyme H56N, at pH 7.5 and 37°C

1.35

D-Met

mutant enzyme H56A, at pH 7.5 and 37°C

0.119

D-Phe

mutant enzyme H56N, at pH 7.5 and 37°C

0.218

D-Phe

mutant enzyme H56A, at pH 7.5 and 37°C

0.003

D-proline

wild-type, pH 8.3, 25°C

0.03

D-proline

Q0E9Q7

pH 8.3, 25°C

172

N-methyl-D-Asp

pH 8.3, 37°C, recombinant DDO-3

562

N-methyl-D-Asp

pH 7.0, 20°C, recombinant wild-type enzyme

654

N-methyl-D-Asp

pH 8.3, 37°C, recombinant DDO-2

5787

N-methyl-D-Asp

pH 8.3, 37°C, recombinant DDO-1

1.5

N-Methyl-D-aspartate

wild-type, pH 7, 60°C

10.2

N-Methyl-D-aspartate

mutant F248Y, pH 7, 60°C

26.7

N-Methyl-D-aspartate

wild-type, pH 8.3, 25°C

26.7

N-Methyl-D-aspartate

Q0E9Q7

pH 8.3, 25°C

show all columns Go to Ki Value Search

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Ki VALUE [mM]

INHIBITOR

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

IMAGE

0.66

(5R)-4-hydroxy-3,5-dimethyl-5-[(1E)-2-methyl-1,3-butadienyl]-2(5H)-thiophenone

pH 8.3, 37°C

0.0038

5-aminonicotinic acid

at pH 8.3 and 37°C

0.0151

7-hydroxy-4-hydro-1,2,4-triazolo[4,3-a]pyrimidine-6-carboxylic acid

at pH 8.3 and 37°C

1.416 - 1.915

Aminooxyacetate

0.011 - 13.3

D-malate

0.06 - 5.4

malonate

6 entries

0.153

malonic acid

at pH 8.3 and 37°C

0.472 - 61

meso-tartrate

additional information

inhibition kinetics

1.416

Aminooxyacetate

at pH 8.3 and 37°C

1.492

Aminooxyacetate

at pH 8.3 and 37°C

1.915

Aminooxyacetate

Q0E9Q7

at pH 8.3 and 37°C

0.011

D-malate

13.3

D-malate

0.06

malonate

0.153

malonate

at pH 8.3 and 37°C

1.22

malonate

Q0E9Q7

at pH 8.3 and 37°C

1.562

malonate

at pH 8.3 and 37°C

1.59

malonate

pH 8.3, 37°C

5.4

malonate

0.472

meso-tartrate

at pH 8.3 and 37°C

0.681

meso-tartrate

at pH 8.3 and 37°C

1.94

meso-tartrate

pH 8.3, 37°C

2.089

meso-tartrate

show all columns Go to IC50 Value Search

Q0E9Q7

at pH 8.3 and 37°C

meso-tartrate

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IC50 VALUE [mM]

INHIBITOR

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

IMAGE

1.86

(5R)-4-hydroxy-3,5-dimethyl-5-[(1E)-2-methyl-1,3-butadienyl]-2(5H)-thiophenone

Mus musculus

pH 8.3, 37°C

1-hydroxy-1H-indole-2-carboxylic acid

Homo sapiens

IC50 above 1 mM, at pH 8.3 and 37°C

2-amino-5-chlorobenzoic acid

Homo sapiens

IC50 above 10 mM, at pH 8.3 and 37°C

2-aminopyridine-3-carboxylic acid

Homo sapiens

IC50 above 1 mM, at pH 8.3 and 37°C

0.1

2-aminopyridine-4-carboxylic acid

Homo sapiens

IC50 above 0.1 mM, at pH 8.3 and 37°C

2-hydroxy-6-methylpyridine-3-carboxylic acid

Homo sapiens

IC50 above 10 mM, at pH 8.3 and 37°C

3-aminobenzoic acid

Homo sapiens

IC50 above 10 mM, at pH 8.3 and 37°C

3-aminopyridine-2-carboxylic acid

Homo sapiens

IC50 above 1 mM, at pH 8.3 and 37°C

3-aminopyridine-4-carboxylic acid

Homo sapiens

IC50 above 5 mM, at pH 8.3 and 37°C

3-hydroxypyridine-2-carboxylic acid

Homo sapiens

IC50 above 10 mM, at pH 8.3 and 37°C

0.1

4-aminopyridine-2-carboxylic acid

Homo sapiens

IC50 above 0.1 mM, at pH 8.3 and 37°C

0.1

4-aminopyridine-3-carboxylic acid

Homo sapiens

IC50 above 0.1 mM, at pH 8.3 and 37°C

4-carbamoylthiophene-2-carboxylic acid

Homo sapiens

IC50 above 5 mM, at pH 8.3 and 37°C

5-(dimethylamino)pyridine-3-carboxylic acid

Homo sapiens

IC50 above 1 mM, at pH 8.3 and 37°C

3.541

5-(methylamino)pyridine-3-carboxylic acid

Homo sapiens

at pH 8.3 and 37°C

5-(trifluoromethyl)pyridine-3-carboxylic acid

Homo sapiens

IC50 above 10 mM, at pH 8.3 and 37°C

0.0219

5-aminonicotinic acid

Homo sapiens

at pH 8.3 and 37°C

5-aminopyridine-2-carboxylic acid

Homo sapiens

IC50 above 10 mM, at pH 8.3 and 37°C

5-bromopyridine-3-carboxylic acid

Homo sapiens

IC50 above 10 mM, at pH 8.3 and 37°C

5-chloro-2-hydroxybenzoic acid

Homo sapiens

IC50 above 10 mM, at pH 8.3 and 37°C

5-chloropyridine-3-carboxylic acid

Homo sapiens

IC50 above 10 mM, at pH 8.3 and 37°C

5-fluoro-2-hydroxybenzoic acid

Homo sapiens

IC50 above 10 mM, at pH 8.3 and 37°C

5-fluoropyridine-3-carboxylic acid

Homo sapiens

IC50 above 10 mM, at pH 8.3 and 37°C

3.351

5-hydroxypyridine-3-carboxylic acid

Homo sapiens

at pH 8.3 and 37°C

5-methoxypyridine-3-carboxylic acid

Homo sapiens

IC50 above 10 mM, at pH 8.3 and 37°C

5.472

5-methylpyridine-3-carboxylic acid

Homo sapiens

at pH 8.3 and 37°C

5-nitropyridine-3-carboxylic acid

Homo sapiens

IC50 above 10 mM, at pH 8.3 and 37°C

5-phenylpyridine-3-carboxylic acid

Homo sapiens

IC50 above 5 mM, at pH 8.3 and 37°C

5-sulfopyridine-3-carboxylic acid

Homo sapiens

IC50 above 10 mM, at pH 8.3 and 37°C

0.1

6-aminopyridine-2-carboxylic acid

Homo sapiens

IC50 above 0.1 mM, at pH 8.3 and 37°C

2.364

6-aminopyridine-3-carboxylic acid

Homo sapiens

at pH 8.3 and 37°C

5.3

malonate

Mus musculus

pH 8.3, 37°C

8.71

meso-tartrate

Mus musculus

pH 8.3, 37°C

0.0014 - 0.0231

olanzapine

pyridin-3-amine

Homo sapiens

IC50 above 10 mM, at pH 8.3 and 37°C

pyridine-3,5-dicarboxylic acid

Homo sapiens

IC50 above 10 mM, at pH 8.3 and 37°C

2.778

pyridine-3-carboxylic acid

Homo sapiens

at pH 8.3 and 37°C

0.0014

olanzapine

Mus musculus

Q0E9Q7

in the presence of 0.004 mM FAD, pH and temperature not specified in the publication

0.0231

olanzapine

Homo sapiens

in the presence of 0.004 mM FAD, pH and temperature not specified in the publication

show all columns Go to Specific Activity Search

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SPECIFIC ACTIVITY [µmol/min/mg]

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

0.00021

from kidney

0.00048

from liver

0.00053

from brain

0.00055

from liver

0.0006

from kidney

0.00062

from kidney

0.00076

from kidney

0.00119

0.00144

from liver

0.00233

from liver

0.0035

0.04

0.08

unpurified recombinant enzyme

0.09

pH 7.0, 20°C, purified recombinant mutant R243A, substrate D-Asp

0.1

Q0E9Q7

wild type enzyme, at 37°C in 40 mM sodium diphosphate buffer (pH 8.3) with D-glutamate as substrate

0.11

Q0E9Q7

mutant enzyme S308Y, at 37°C in 40 mM sodium diphosphate buffer (pH 8.3) with D-glutamate as substrate

0.12

with D-Pro as substrate, at pH 8.3 and 37°C

0.14

with D-His as substrate, at pH 8.3 and 37°C

0.16

Q0E9Q7

with D-Asn as substrate, at pH 8.3 and 37°C

0.24

Q0E9Q7

mutant enzyme S308A, at 37°C in 40 mM sodium diphosphate buffer (pH 8.3) with D-glutamate as substrate

0.4

0.46

Q0E9Q7

with D-Glu as substrate, at pH 8.3 and 37°C

0.47

with N-methyl-L-Asp as substrate, at pH 8.3 and 37°C

0.5

pH 7.0, 20°C, purified recombinant mutant R243K, substrate D-Glu

0.53

Q0E9Q7

substrate D-glutamate, pH 8.3, 37°C

0.55

Q0E9Q7

mutant enzyme S308G, at 37°C in 40 mM sodium diphosphate buffer (pH 8.3) with D-glutamate as substrate

pH 7.0, 20°C, purified recombinant mutant R243E, substrate D-Glu

1.2

pH 7.0, 20°C, purified recombinant mutant R243D, substrate N-methyl-D-Asp

1.5

pH 7.0, 20°C, purified recombinant mutant R243K, substrate D-Asp

1.6

pH 7.0, 20°C, purified recombinant wild-type enzyme, substrate D-Glu

1.77

substrate D-glutamate, pH 8.3, 37°C

1.9

pH 7.0, 20°C, purified recombinant mutant R243E, substrate D-Asp

11.7

Q0E9Q7

substrate D-aspartate, pH 8.3, 37°C

12.2

Q0E9Q7

with D-Asp as substrate, at pH 8.3 and 37°C

123

13.1

169

60°C, pH 7.5

18.5

pH 7.0, 20°C, purified recombinant mutant R243D, substrate D-Glu

181

pH 7.0, 20°C, purified recombinant mutant R243D, substrate D-Asp

2.37

Q0E9Q7

mutant enzyme S308Y, at 37°C in 40 mM sodium diphosphate buffer (pH 8.3) with D-aspartate as substrate

2.4

ferricyanide as electron acceptor

2.54

Q0E9Q7

mutant enzyme S308Y, at 37°C in 40 mM sodium diphosphate buffer (pH 8.3) with N-methyl-D-aspartate as substrate

2.93

with D-Asn as substrate, at pH 8.3 and 37°C

25.3

29.1

3.17

with N-methyl-D-Glu as substrate, at pH 8.3 and 37°C

4.31

Q0E9Q7

wild type enzyme, at 37°C in 40 mM sodium diphosphate buffer (pH 8.3) with D-aspartate as substrate

4.32

Q0E9Q7

wild type enzyme, at 37°C in 40 mM sodium diphosphate buffer (pH 8.3) with N-methyl-D-aspartate as substrate

substrate D-aspartate, pH 8.3, 37°C

46.3

37°C, pH 7.5

5.55

Q0E9Q7

mutant enzyme S308A, at 37°C in 40 mM sodium diphosphate buffer (pH 8.3) with D-aspartate as substrate

5.92

Q0E9Q7

mutant enzyme S308A, at 37°C in 40 mM sodium diphosphate buffer (pH 8.3) with N-methyl-D-aspartate as substrate

51.7

substrate D-aspartate, pH 8.3, 37°C

recombinant enzyme after 775fold purification

65.3

substrate D-glutamate, pH 8.3, 37°C

7.82

with D-Glu as substrate, at pH 8.3 and 37°C

76.1

pH 7.0, 20°C, purified recombinant mutant R243M, substrate D-Asp

87.5

with D-Asp as substrate, at pH 8.3 and 37°C

9.2

pH 7.0, 20°C, purified recombinant wild-type enzyme, substrate N-methyl-D-Asp

9.24

Q0E9Q7

mutant enzyme S308G, at 37°C in 40 mM sodium diphosphate buffer (pH 8.3) with D-aspartate as substrate

91.2

with N-methyl-D-Asp as substrate, at pH 8.3 and 37°C

93.7

pH 7.0, 20°C, purified recombinant wild-type enzyme, substrate D-Asp

additional information

mutant activities with D-Ala and D-Arg, overview

0.00119

from liver

0.00119

from kidney

0.04

pH 7.0, 20°C, purified recombinant mutant R243E, substrate N-methyl-D-Asp

0.04

pH 7.0, 20°C, purified recombinant mutant R243K, substrate N-methyl-D-Asp

13.1

Q0E9Q7

mutant enzyme S308G, at 37°C in 40 mM sodium diphosphate buffer (pH 8.3) with N-methyl-D-aspartate as substrate

13.1

Q0E9Q7

with N-methyl-D-Asp as substrate, at pH 8.3 and 37°C

13.1

pH 7.0, 20°C, purified recombinant mutant R243M, substrate D-Glu

show all columns Go to pH Optimum Search

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pH OPTIMUM

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

assay at

7.5

7.5 - 9

8.2

8.3

8.7

9.5

additional information

optimum depends on the order of addition of the reactands

7.5

7.5

7.5

8.3

show all columns Go to pH Range Search

assay at

8.3

assay at

8.3

assay at

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pH RANGE

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

4.5 - 11

show all columns Go to Temperature Optimum Search

largely destroyed below or over this range

5 - 9

activity assay range

6 - 12.5

the activity increases gradually as the pH is increased from 6.0 to 8.3, remains approximately constant at pH 8.3 to 12.5, and decreases rapidly when the pH is greater than 12.5. No enzymatic activity is detected at very low and high pH levels (5.0 and 13.0), respectively

6.5 - 9.5

8.3 - 11

Q0E9Q7

8.3 - 12.5

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TEMPERATURE OPTIMUM

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

assay at

33 - 37

show all columns Go to Organism Search

assay at

assay at

assay at

Q0E9Q7

only manually annotated data include textmining data from AMENDAenzyme occurrence in organism, localization and source tissue with reliability ranks include all textmining data from AMENDAenzyme occurrence in organism, localization and source tissue with reliability ranks + FRENDAco-occurrence of enzyme names and organism names (less precise)

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ORGANISM

COMMENTARY

LITERATURE

UNIPROT

SEQUENCE DB

SOURCE

391705, 391706, 391707, 391708, 391711, 391717, 391718, 391719, 391720, 391721, 391722, 391723, 391724, 391725, 711719

brenda

brenda

anglerfish

brenda

saury

brenda

yellow sea bream

brenda

strain elongantum Y-105

brenda

japanese sea perch

brenda

Meretrix lusoria

hard clam

brenda

scallop

brenda

mussel

brenda

no activity in Rubrobacter xylanophilus

741688

brenda

391714, 391716, 391717, 657350

brenda

Oncorhynchus keta

chum salmon

brenda

Oncorhynchus masou

land-locked masu salmon

brenda

brenda

brenda

olive flounder

brenda

kuruma prawn

brenda

smelt fish

brenda

Procambarus clarkii

crayfish

brenda

marbled sole

brenda

Sprague-Dawley

brenda

sardine

brenda

Scomber japonicus

chub mackerel

brenda

brenda

filefish

brenda

brenda

Thermomyces dupontii NBRC 30541

brenda

flying squid

brenda

horse mackerel

brenda

turban shell

brenda

brenda

right-eyed flounder

brenda

brenda

673583, 725959

brenda

at least three genes encoding functional DDO isozymes DDO-1, DDO-2, and DDO-3

brenda

at least two genes encoding functional DASPOs (C47Ap and F18Ep). The two DASPOs differ in their substrate specificities and possibly also in their subcellular localization

brenda

gene C47Ap encoding isozyme DDO-1, gene F18Ep encoding isozyme DDO-2, and gene F20Hp encoding isozyme DDO-3

brenda

isoform DDO-1

Q19564

SwissProt

brenda

isoform DDO-2

SwissProt

brenda

isoform DDO1

SwissProt

brenda

isoform DDO3

UniProt

brenda

brenda

isoform DDO-1

Q19564

SwissProt

brenda

isoform DDO-2

SwissProt

brenda

brenda

common carp

brenda

391706, 391709, 391712, 711325, 711719

brenda

742035, 743063, 743836

UniProt

brenda

762746

C9K4X7

UniProt

brenda

UniProt

brenda

the human DDO gene produces alternative transcripts encoding for three putative DASPO isoforms, constituted by 341 (the canonical form), 369, and 282 amino acids

763024

UniProt

brenda

brenda

Q0E9Q7

UniProt

brenda

686597, 711325, 711719, 711722

brenda

742035, 742426, 743133

Q0E9Q7

UniProt

brenda

brenda

743350, 743836, 762748, 762756

Q0E9Q7

UniProt

brenda

male ICR mice

brenda

brenda

rainbow trout

brenda

brenda

red sea bream

brenda

brenda

adult male green frogs

brenda

391716, 711719, 711722

brenda

742035, 762748

UniProt

brenda

Sprague-Dawley

brenda

brenda

UniProt

brenda

711719, 723870

brenda

prepuberal female pigs

brenda

brenda

SwissProt

brenda

677271, 711719, 724597

brenda

SwissProt

brenda

i.e. Asterotremella humicola

SwissProt

brenda

show all columns Go to Source Tissue Search

only manually annotated data include textmining data from AMENDAenzyme occurrence in organism, localization and source tissue with reliability ranks

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SOURCE TISSUE

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

SOURCE

Q0E9Q7

brenda

brenda

relatively high enzyme expression just after birth, the content gradually decreases thereafter

brenda

coelomocyte

DDO3 is secreted from the cells where it is produced into the body fluid and taken up by scavenger coelomocytes

brenda

egg

brenda

504 hours old

brenda

brenda

brenda

brenda

brenda

brenda

brenda

brenda

brenda

brenda

primary cultured

brenda

brenda

brenda

brenda

pheochromocytoma cells

brenda

Q0E9Q7

brenda

brenda

Q0E9Q7

brenda

additional information

9 entries

adrenal gland

adrenal cortex and adrenal medulla epinephrine cells

brenda

brenda

brenda

brenda

brenda

body wall muscle

brenda

mainly localized in neurons

brenda

two forms encoded named DDO-1 and DDO-2, DDO-1 is characterized

brenda

brenda

cerebellar cortex Bergmann glia

brenda

Q0E9Q7

brenda

brenda

Q0E9Q7

brenda

brenda

brenda

embryonic, D-Asp initially emerges in the hindbrain and then spreads into the forebrain. Within nerve cells of the rat embryonic brain, D-Asp first occurs in the cell bodies of neuroblasts in the outer layer of the neuronal epithelium, and then it appears in the processes of the cells

brenda

brenda

brenda

brenda

Q0E9Q7

brenda

relatively high enzyme expression just after birth, the content gradually decreases thereafter

brenda

brenda

brenda

female pudendum

brenda

gill

brenda

brenda

brenda

head

brenda

brenda

brenda

brenda

brenda

brenda

brenda

brenda

brenda

brenda

brenda

brenda

brenda

brenda

hepatopancreas

brenda

brenda

brenda

brenda

brenda

brenda

brenda

Q0E9Q7

brenda

brenda

hypodermis

brenda

brenda

in the cell bodies of the neurons

brenda

brenda

brenda

brenda

brenda

brenda

brenda

brenda

brenda

brenda

brenda

brenda

kidney

391705, 391707, 391717, 391719, 391720, 391721, 391723, 391724, 391725

brenda

tubule

brenda

cortex

391711, 391718, 391722

brenda

brenda

brenda

brenda

brenda

brenda

brenda

brenda

brenda

Q0E9Q7

brenda

brenda

in Bowman's capsule, renal thin limbs of Henle's loop

brenda

kidney

brenda

brenda

brenda

brenda

brenda

brenda

brenda

brenda

brenda

kidney

brenda

brenda

brenda

brenda

brenda

brenda

brenda

brenda

brenda

brenda

brenda

brenda

brenda

brenda

brenda

brenda

brenda

brenda

brenda

brenda

brenda

brenda

brenda

brenda

muscle

brenda

brenda

brenda

pharyngeal muscle

brenda

brenda

D-Asp content in the adult rat pineal gland is very high, especially in the distal (caudal) region of the gland, little staining is found in the proximal (rostral) region

brenda

brenda

brenda

brenda

intermediate lobe

brenda

brenda

prolactin-producing cells in the anterior lobe and microglial cells in the posterior lobe, D-Asp immunoreactivity is observed specifically in prolactin-producing mammotrophs or in a closely related cell type

brenda

pituitary gland

growth hormone-positive cells and almost all proopiomelanocortin-positive cells

brenda

brenda

brenda

brenda

brenda

brenda

brenda

brenda

brenda

with about 80 units/mg thyroid enzyme activity

brenda

thyroid gland

with about 80 units/mg thyroid enzyme activity

brenda

brenda

additional information

development-related patterns of D-Asp expression differ among various mammalian tissues, overview

brenda

additional information

in males, DDO3 is secreted from the seminal vesicle into the seminal fluid in a signal peptide-dependent manner during mating with hermaphrodites. In hermaphrodites, DDO3 is secreted from the proximal gonadal sheath cells in a signal peptide-dependent manner and transferred to the oocyte surface

brenda

additional information

brenda

additional information

development-related patterns of D-Asp expression differ among various mammalian tissues, overview

brenda

additional information

development-related patterns of D-Asp expression differ among various mammalian tissues, overview

brenda

additional information

development-related patterns of D-Asp expression differ among various mammalian tissues, overview

brenda

additional information

development-related patterns of D-Asp expression differ among various mammalian tissues, overview

brenda

additional information

development-related patterns of D-Asp expression differ among various mammalian tissues, overview

brenda

additional information

immunohistochemic analysis, overview

712818

brenda

show all columns Go to Localization Search

only manually annotated data include textmining data from AMENDAenzyme occurrence in organism, localization and source tissue with reliability ranks

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LOCALIZATION

ORGANISM

UNIPROT

COMMENTARY

GeneOntology No.

LITERATURE

SOURCE

brenda

in magnocellular neurons of the rat supraoptic nucleus, but not in other subcellular structures of the nucleus and soma, including the nucleoplasm and cytoplasm

792

brenda

brenda

in magnocellular neurons of the rat supraoptic nucleus

brenda

DDO-2

brenda

brenda

DDO-3

711718, 711719

brenda

extracellular

in hermaphrodites, DDO3 is secreted from the proximal gonadal sheath cells in a signal peptide-dependent manner and transferred to the oocyte surface. In males, DDO3 is secreted from the seminal vesicle into the seminal fluid in a signal peptide-dependent manner during mating with hermaphrodites. DDO3 is secreted from the cells where it is produced into the body fluid and taken up by scavenger coelomocytes

brenda

391706, 391719, 711719

brenda

peroxisome

DDO-1

brenda

brenda

brenda

brenda

brenda

brenda

its C-terminus has a peroxisome targeting signal

brenda

brenda

brenda

brenda

brenda

brenda

brenda

brenda

brenda

brenda

brenda

5777

brenda

peroxisome

brenda

brenda

5777

brenda

peroxisome

brenda

brenda

brenda

brenda

brenda

brenda

Highest Expressing Human Cell Lines

Filter by:

Cell Line Links

Gene Links

show all columns Go to General Information Search

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GENERAL INFORMATION

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

metabolism

physiological function

11 entries

additional information

melatonin secretion and D-Asp release from pinealocytes are enhanced by stimulation with noradrenaline, after which the melatonin secretion is suppressed by the action of the released D-Asp on the cells. Through this negative feedback mechanism, noradrenaline may regulate its ability to induce melatonin secretion in the pineal gland

metabolism

in frog tissue, D-AspO plays an essential role in modulating the D-Asp concentration, exaggerated D-Asp concentrations activate SOD1 as cytoprotective mechanism in the kidney, whereas, in the brain and in the heart, where the antioxidant action of SOD1 is limited, caspase 3 is activated, overview

metabolism

H2O2 is essential for the iodination of the tyrosyl residues to produce mono- and diiodotyrosine that are the precursors for the synthesis of thyroid hormones T3 and T4. interaction of endogenous D-Asp, D-AspO, and D-aspartate racemase in thyroid gland constitutes an additional biochemical pathway for the production of H2O2 and consequently for the synthesis of thyroid hormones, overview

metabolism

metabolism

the reductive half-reaction is reversible. The kinetic mechanism follows a ternary complex mechanism characterized by a very fast step of flavin reduction followed by a rate-limiting reoxidation step

physiological function

relevance of D-Asp and DDO to NMDA receptor-related disease, D-Asp protects against sensorimotor-gating deficits, which are observed in schizophrenic patients, overview. D-Asp is important in the development and neurogenesis of the brain

physiological function

D-Asp is important in the development and neurogenesis of the brain. D-Asp plays a regulatory role in the synthesis and secretion of prolactin in the anterior lobe of the pituitary gland. D-Asp directly interacts with DNA and/or acts on nuclear protein(s) involved in the regulation of gene transcription, through which d-Asp controls gene expression in the hypothalamo-neurohypophyseal system

physiological function

relevance of D-Asp and DDO to NMDA receptor-related disease, overview. Phenotype of DDO-deficient mice, DDO-deficient mice display significant deficits in prepulse inhibition, and exhibit reduced immobility time in the Porsolt forced-swim test, a model of depression, suggesting that the genetic ablation of DDO has a specific antidepressant action, overview

physiological function

D-AspO plays an essential role in decreasing excessive amounts of D-Asp in frog tissues

physiological function

D-Asp oxidase is a FAD-containing flavoprotein that catalyzes the oxidative deamination of D-amino acids with O2 to generate the corresponding 2-oxo acids, along with H2O2 and NH3. DDO is highly specific for acidic D-amino acids, such as D-Asp, N-methyl-D-Asp, and D-Glu

physiological function

in frog tissue, D-AspO plays an essential role in modulating the D-Asp concentration. Induction of oxidative stress following D-Asp exposure is primarily related to its metabolism by inducible D-AspO

physiological function

the D-aspartate oxidase isoforms are involved in egg-laying events and the early development of Caenorhabditis elegans, playing an important role in the development and maturation of germ cells

physiological function

Q0E9Q7

age-related changes in D-aspartate oxidase promoter methylation control extracellular D-aspartate levels and prevent precocious cell death during brain aging. The enzyme expression is critical to regulate the content of the N-methyl-D-aspartate receptor agonist D-aspartate in adulthood

physiological function

Q0E9Q7

the enzyme plays a role in the modulation of glutamatergic system homeostasis in the mammalian brain

743350

physiological function

the isoform responsible for in vivo metabolism of D-glutamate is DDO3, which is also required for normal self-fertility, hatching, and lifespan

physiological function

the D-aspartate oxidase isoforms are involved in egg-laying events and the early development of Caenorhabditis elegans, playing an important role in the development and maturation of germ cells

Go to AA Sequence and Transmembrane Helices SearchGo to Localization Prediction

Show AA Sequence and Transmembrane Helices (1049 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.

Go to PDB and Structure Links Search

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PDB

SCOP

CATH

UNIPROT

ORGANISM

show all columns Go to Molecular Weight Search

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MOLECULAR WEIGHT

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

146000

152000

SDS-PAGE

164000

gel filtration

30000

native PAGE

365000

4 * 365000, low-angle laser light scattering photometry

37000

37607

x * 37636, DDO-1, sequence calculation, x * 37607, DDO-2, sequence calculation, x * 42501, DDO-3, sequence calculation

37610

F18Ep, calculated from sequence of cDNA

37620

calculated from amino acid sequence

37636

x * 37636, DDO-1, sequence calculation, x * 37607, DDO-2, sequence calculation, x * 42501, DDO-3, sequence calculation

37640

C47Ap, calculated from sequence of cDNA

37659

1 * 37659, amino acid analysis

37660

apoprotein, amino acid analysis

38000

380000

4 * 380000, SDS-PAGE

38300

gel filtration

39000

39200

gel filtration

39459

4 * 39459, deduced from nucleotide sequence

40000

41770

His-tagged F18Ep, calculated from sequence of cDNA

41790

His-tagged C47Ap, calculated from sequence of cDNA

42501

x * 37636, DDO-1, sequence calculation, x * 37607, DDO-2, sequence calculation, x * 42501, DDO-3, sequence calculation

146000

low-angle laser light scattering photometry

146000

PAGE

146000

Q0E9Q7

PAGE

37000

SDS-PAGE

37000

recombinant protein, SDS-PAGE

38000

show all columns Go to Subunit Search

recombinant protein, SDS-PAGE

38000

x * 38000, SDS-PAGE

39000

containing 1 molecule of FAD, SDS-PAGE

39000

1 * 39000, SDS-PAGE

40000

SDS-PAGE

40000

4 * 40000, SDS-PAGE

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SUBUNIT

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

homotetramer

monomer

tetramer

additional information

x * 37636, DDO-1, sequence calculation, x * 37607, DDO-2, sequence calculation, x * 42501, DDO-3, sequence calculation

x * 37000-38000

x * 37000-38000

x * 37000-38000

x * 38000, SDS-PAGE

x * 40000, SDS-PAGE

homotetramer

4 * 365000, low-angle laser light scattering photometry

homotetramer

4 * 380000, SDS-PAGE

homotetramer

4 * 37000-38000

homotetramer

gel filtration

homotetramer

4 * 37000-38000

homotetramer

gel filtration

monomer

1 * 37659, amino acid analysis

monomer

1 * 39000, SDS-PAGE

monomer

1 * 37000-38000

monomer

1 * 38647, calculated from sequence

monomer

1 * 45000, SDS-PAGE

monomer

Thermomyces dupontii NBRC 30541

1 * 45000, SDS-PAGE

tetramer

Q0E9Q7

4 * 41700, calculated from sequence, His-tagged protein

tetramer

4 * 41700, calculated from sequence, His-tagged protein

tetramer

4 * 39459, deduced from nucleotide sequence

tetramer

4 * 40000, SDS-PAGE

additional information

three-dimensional structure by homology-modeling

additional information

three-dimensional structure by homology-modeling

additional information

three-dimensional model of ChDDO, comparison with the crystal structure of a yeast Rhodotorula gracilis D-amino acid oxidase, EC 1.4.3.3

Go to Crystallization (commentary) Search

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CRYSTALLIZATION (Commentary)

ORGANISM

UNIPROT

LITERATURE

structure of mutants C141Y and C143G, to 3.22 A resolution. The FAD-binding domain is comprised of residues 1-46, 143-192, 282-335 with the canonical dinucleotide binding fold observed in several flavoenzymes, and the substrate-binding domain (residues 47-142, 193-281) is characterized by a large, eight-stranded, mixed beta-sheet

sitting drop vapor diffusion method, using 510%(w/v) PEG 8000, 100 mM sodium dihydrogen phosphate (or 100 mM potassium dihydrogen phosphate), 100 mM sodium acetate (pH 4.7)

show all columns Go to Protein Variants Search

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PROTEIN VARIANTS

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

C141Y

variant produces crystals suitable for X-ray analysis

C143G

variant produces crystals suitable for X-ray analysis

H54A

variant shows a lower maximal activity and kinetic efficiency compared to the wild-type

R216Q

C9K4X7

single nucleotiode polymorphism, reduces enzyme activity towards acidic D-amino acids, decreases the binding affinity for the coenzyme FAD and decreases the temperature stability. Cultured mammalian cells reveal elevated D-aspartate level in cultures of R216Q cells

762746

R237A

variant shows a lower maximal activity and kinetic efficiency compared to the wild-type

S308N

R216A

mutant with significantly reduced activity

R216E

mutant with significantly reduced activity

R216L

mutant with significantly reduced activity

R216M

mutant with significantly reduced activity

R216X

activities of mouse DDO against acidic D-amino acids are virtually extinguished or significantly reduced by replacements of the Arg216 residue with other amino acid residues

R237A

R237E

mutant with significantly reduced activity

R237X

activities of mouse DDO against acidic D-amino acids are virtually extinguished or significantly reduced by replacements of the Arg237 residue with other amino acid residues

R237Y

mutant with significantly reduced activity

S308A

Q0E9Q7

has a significantly higher catalytic efficiency towards D-Asp and N-methyl-D-Asp, and a higher affinity for FAD compared to the wild type enzyme

S308G

S308Y

Q0E9Q7

has a significantly lower catalytic efficiency towards D-Asp and N-methyl-D-Asp, and a lower affinity for FAD compared to the wild type enzyme

F248Y

H56A

H56D

the mutant exhibits no significant activity toward acidic D-amino acids

H56F

the mutant exhibits no significant activity toward acidic D-amino acids

H56K

the mutant exhibits no significant activity toward acidic D-amino acids

H56N

R243A

site-directed mutagenesis, inactive mutant

R243D

site-directed mutagenesis, the mutant exhibits different spectral features of bound flavin from that of the wild-type enzyme. R243D exhibits approximately 2fold higher DDO activity than that of the wild-type with a high substrate specificity to D-aspartate. Kinetic analysis shows that R243D mutant has a 2.5fold lower Km and a 1.6fold higher kcat for D-aspartate compared to the wild-type enzyme, resulting in approximately 4fold higher catalytic efficiency

R243E

site-directed mutagenesis, the mutant exhibits different spectral features of bound flavin from that of the wild-type enzyme and displays lower DDO activity. The mutant also oxidizes the substrates of DAO, D-Ala and D-Arg, albeit with very low activities

R243K

site-directed mutagenesis, the mutant exhibits different spectral features of bound flavin from that of the wild-type enzyme and displays lower DDO activity

R243M

additional information

intense D-Asp immunoreactivity is observed in the intermediate lobe of the pituitary gland of the DDO-deficient mice, phenotype of DDO-deficient mice, detailed overview

R237A

mutant with significantly reduced activity

R237A

site-directed mutagenesis, active site mutant, shows reduced binding of inhibitor thiolactomycin compared to the wild-type enzyme

S308G

Q0E9Q7

has a significantly higher catalytic efficiency towards D-Asp and N-methyl-D-Asp, and a higher affinity for FAD compared to the wild type enzyme

S308G

the mutation results in lack of a side-chain OH group at position 308, and increases mutant enzyme catalytic efficiency against D-Asp and NMDA to about 7-10times higher than that of the wild-type enzyme. Moreover, the dissociation-constant value for FAD of this Gly-substitution mutant is significantly lower than that of the wild-type enzyme, suggesting that it has enhanced ability to bind to FAD

F248Y

mutation markedly increases substrate-binding affinity

F248Y

Thermomyces dupontii NBRC 30541

mutation markedly increases substrate-binding affinity

H56A

the mutant exhibits no significant activity toward acidic D-amino acids

H56A

the mutant gains the ability to utilize neutral D-amino acids as substrates, such as D-methionine, D-phenylalanine and D-glutamine

H56N

the mutant exhibits no significant activity toward acidic D-amino acids

H56N

the mutant gains the ability to utilize neutral D-amino acids as substrates, such as D-methionine, D-phenylalanine and D-glutamine

show all columns Go to pH Stability Search

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pH STABILITY

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

5 - 10

6 - 8.5

fairly stable

7.5 - 12

after 30 min incubation time, the enzyme is stable at pH 8.3 to 11.0 and retains 80% and 60% of its maximum activity at pH 7.5 and pH 12.0, respectively

7.5 - 9

show all columns Go to Temperature Stability Search

the activity increases gradually as pH increases from pH 5.5 to 7.5, exhibits an almost constant value over pH 7.5 to 9.0, and decreases as the pH increases over pH 9.0

stable

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TEMPERATURE STABILITY

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

30 - 60

after 30 min of incubation, there is no loss of activity until the preincubation temperature reaches 45°C, and 9% of the maximum activity is lost at 50°C. The enzyme retains half of its maximum activity at 55°C, while almost all of the activity is lost at 60°C

little loss of activity

48.8

melting temperature

T50 value

52.5

melting temperature, presence of FAD

complete loss of activity

Go to General Stability Search

30 min, 65% residual activity

stable

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GENERAL STABILITY

ORGANISM

UNIPROT

LITERATURE

enzyme stability decreases following a decrease in protein concentration, and externally added FAD cannot repress the destabilization

Go to Storage Stability Search

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STORAGE STABILITY

ORGANISM

UNIPROT

LITERATURE

-10°C, deionized water, several days, 100% activity

Go to Purification (commentary) Search

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PURIFICATION (Commentary)

ORGANISM

UNIPROT

LITERATURE

expressed in Escherichia coli, mixture of 80-91% active FAD-containing and 9-20% inactive OH-FAD containing enzyme

391707, 391708, 391719

His GraviTrap column chromatography

HiTrap Chelating HP column chromatography

recombinant

recombinant C47A10.5 gene product

recombinant chDDO, ammonium sulfate, Butyl-Sepharose, SP-Sepharose

recombinant DDO-1, DDO-2, and DDO-3 from Escherichia coli to homogeneity or near homogeneity

recombinant enzyme

recombinant enzyme from Escherichia coli

recombinant F18E3.7a gene product

recombinant His-tagged wild-type and mutant DDOs from Escherichia coli strain Rosetta (DE3) by metal affinity chromatography and gel filtration

recombinant protein, purified to homogeneity from the soluble fraction by HiTrap chelating chromatography

Q0E9Q7

SP-Toyopearl column chromatography, Q-Sepharose column chromatography, PPG-Toyopearl column chromatography, and SuperSW3000 gel filtration

TSK gel filtration

His GraviTrap column chromatography

His GraviTrap column chromatography

Q0E9Q7

684387, 742035

His GraviTrap column chromatography

His GraviTrap column chromatography

recombinant enzyme from Escherichia coli

recombinant enzyme from Escherichia coli

recombinant enzyme from Escherichia coli

recombinant enzyme from Escherichia coli

Go to Cloned (commentary) Search

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CLONED (Commentary)

ORGANISM

UNIPROT

LITERATURE

expressed in Escherichia coli

expressed in Escherichia coli BL21

expressed in Escherichia coli BL21 Star (DE 3) cells

expressed in Escherichia coli BL21(DE3) cells

expressed in Escherichia coli BL21(DE3) pLysS cells

expressed in Escherichia coli GI724 cells

391707, 391711

expressed in Escherichia coli L21(DE3)pLysS cells

expressed in Escherichia coli strain BL21(DE3)pLysS

Q0E9Q7

expressed in Escherichia coli strains BL21(DE3)pLysS and JM 109

expression in Escherichia coli

expression of GST-tagged, N-terminally His-tagged, and S-tagged DDO

expression of His-tagged wild-type and mutant DDOs in Escherichia coli strain Rosetta (DE3)

from brain, expressed in Escherichia coli

from kidney, expressed in Escherichia coli

genes F20Hp, C47Ap, and F18Ep, expression of DDO-1, DDO-2, and DDO-3 in Escherichia coli

the C47A10.5 gene product is expressed in Escherichia coli as recombinant protein with an N-terminal His-tag

the F18E3.7a gene product is expressed in Escherichia coli as recombinant protein with an N-terminal His-tag

the His-tagged enzyme is expressed in Escherichia coli BL21(DE3) cells

expressed in Escherichia coli BL21(DE3) cells

expressed in Escherichia coli BL21(DE3) cells

expressed in Escherichia coli BL21(DE3) cells

expressed in Escherichia coli BL21(DE3) pLysS cells

expressed in Escherichia coli BL21(DE3) pLysS cells

Q0E9Q7

expressed in Escherichia coli BL21(DE3) pLysS cells

expression in Escherichia coli

expression in Escherichia coli

expression in Escherichia coli

Q0E9Q7

762748, 762756

expression in Escherichia coli

expression in Escherichia coli

expression in Escherichia coli

expression in Escherichia coli

from kidney, expressed in Escherichia coli

from kidney, expressed in Escherichia coli

from kidney, expressed in Escherichia coli

Go to Expression Search

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EXPRESSION

ORGANISM

UNIPROT

LITERATURE

chronic D-Asp treatment leads to upregulation of D-AspO expression in all tissues, along with up- or downregulation of superoxide dismutase 1 and caspase 3 depending on the tissues, overview. D-Asp treated kidney showed the highest D-AspO activity

D-Asp specifically triggers D-AspO activity

show all columns Go to Application Search

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APPLICATION

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

drug development

medicine

the additional N-terminal peptide present in the DASPO_369 splicing isoform only has been identified in hippocampus of Alzheimer's disease female patients, while peptides corresponding to the remaining part of the protein are present in samples from male and female healthy controls and Alzheimer's disease patients. Upon expression in U87 human glioblastoma cells, the DASPO_369 protein shows a lower expression compared with the canonical isoform. Both protein isoforms are active, localize to the peroxisomes, are very stable, and are primarily degraded through the ubiquitin-proteasome system

763024

molecular biology

This enzyme is proposed to have a role in the inactivation of the synaptically released D-aspartate. Its C-terminus has a peroxisome targeting signal.

drug development

a DDO inhibitor that augments brain D-Asp levels can be a potent antipsychotic drug for the treatment of NMDA receptor-related disease

drug development

a DDO inhibitor that augments brain D-Asp levels can be a potent antipsychotic drug for the treatment of NMDA receptor-related disease

top print hide References Search

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REF.

AUTHORS

TITLE

JOURNAL

VOL.

PAGES

YEAR

ORGANISM (UNIPROT)

PUBMED ID

SOURCE

Sacchi, S.; Lorenzi, S.; Molla, G.; Pilone, M.S.; Rossetti, C.; Pollegioni, L.

Engineering the substrate specificity of D-amino-acid oxidase

J. Biol. Chem.

277

27510-27516

2002

Bos taurus

12021281

brenda

Zaar, K.; Kost, H.P.; Schad, A.; Volkl, A.; Baumgart, E.; Fahimi, H.D.

Cellular and subcellular distribution of D-aspartate oxidase in human and rat brain

J. Comp. Neurol.

450

272-282

2002

Bos taurus, Homo sapiens, Rattus norvegicus, Rattus norvegicus Sprague-Dawley

12209855

brenda

Negri, A.; Tedeschi, G.; Ceciliani, F.; Ronchi, S.

Purification of beef kidney D-aspartate oxidase overexpressed in Escherichia coli and characterization of its redox potentials and oxidative activity towards agonists and antagonists of excitatory amino acid receptors

Biochim. Biophys. Acta

1431

212-222

1999

Bos taurus

10209293

brenda

391708

Tedeschi, G.; Negri, A.; Bernardini, G.; Oungre, E.; Ceciliani, F.; Ronchi, S.

D-Aspartate oxidase is present in ovaries, eggs and embryos but not in testis of Xenopus laevis

Comp. Biochem. Physiol. B

124

489-494

1999

Bos taurus, Xenopus laevis

10665376

brenda

Amery, L.; Brees, C.; Baes, M.; Setoyama, C.; Miura, R.; Mannaerts, G.P.; Van Veldhoven, P.P.

C-terminal tripeptide Ser-Asn-Leu (SNL) of human D-aspartate oxidase is a functional peroxisome-targeting signal

Biochem. J.

336

367-371

1998

Homo sapiens

9820813

brenda

Kera, Y.; Hasegawa, S.; Watanabe, T.; Segawa, H.; Yamada, R.H.

D-Aspartate oxidase and free acidic D-amino acids in fish tissues

Comp. Biochem. Physiol. B

119

95-100

1998

Cyprinus carpio, Carassius langsdorfii, Oncorhynchus mykiss, Seriola quinqueradiata, Pagrus major

brenda

391711

Simonic, T.; Duga, S.; Negri, A.; Tedeschi, G.; Malcovati, M.; Tenchini, M.L.; Ronchi, S.

cDNA cloning and expression of the flavoprotein D-aspartate oxidase from bovine kidney cortex

Biochem. J.

322

729-735

1997

Bos taurus

9148742

brenda

Setoyama, C.; Miura, R.

Structural and functional characterization of the human brain D-aspartate oxidase

J. Biochem.

121

798-803

1997

Homo sapiens

9163533

brenda

Yamada, R.h.; Ujiie, H.; Kera, Y.; Nakase, T.; Kitagawa, K.; Imasaka, T.; Arimoto, K.; Takahashi, M.; Matsumura, Y.

Purification and properties of D-aspartate oxidase from Cryptococcus humicolus UJ1

Biochim. Biophys. Acta

1294

153-158

1996

Vanrija humicola, Vanrija humicola UJ1

8645733

brenda

Tedeschi, G.; Negri, A.; Ceciliani, F.; Ronchi, S.; Vetere, A.; D'Aniello, G.; D'Aniello, A.

Properties of the flavoenzyme D-aspartate oxidase from Octopus vulgaris

Biochim. Biophys. Acta

1207

217-222

1994

Octopus vulgaris

7915543

brenda

Wakayama, M.; Nakashima, S.; Sakai, K.; Moriguchi, M.

Isolation, enzyme production and characterization of D-aspartate oxidase from Fusarium sacchari var. elongatum Y-105

J. Ferment. Bioeng.

377-379

1994

Fusarium sacchari

brenda

391716

D'Aniello, A.; D'Onofrio, G.; Pischetola, M.; D'Aniello, G.; Vetere, A.; Petrucelli, L.; Fisher, G.H.

Biological role of D-amino acid oxidase and D-aspartate oxidase. Effects of D-amino acids

J. Biol. Chem.

268

26941-26949

1993

Mus musculus, Octopus vulgaris, Rattus norvegicus

7903300

brenda

D'Aniello, A.; Vetere, A.; Petrucelli, L.

Further study on the specificity of D-amino acid oxidase and of D-aspartate oxidase and time course for complete oxidation of D-amino acids

Comp. Biochem. Physiol. B

105

731-734

1993

Bos taurus, Octopus vulgaris

8103425

brenda

391718

Tedeschi, G.; Negri, A.; Ceciliani, F.; Biondi, P.A.; Secchi, C.; Ronchi, S.

Chemical modification of functional arginyl residues in beef kidney D-aspartate oxidase

Eur. J. Biochem.

205

127-132

1992

Bos taurus

1555574

brenda

Negri, A.; Tedeschi, G.; Ceciliani, F.; Simonic, T.

Structural studies of beef kidney D-aspartate oxidase

Flavins and Flavoproteins (Proc. Int. Symp. , 10th, Meeting Date 1990, Curti, B. , Ronchi S. , Zanetti, G. , eds. ) de Gruyter, Berlin, New York

179-187

1990

Bos taurus

brenda

391720

Tedeschi, G.; Negri, A.; Biondi, P.A.; Secchi, C.; Ronchi, S.

Modification of substrate specificity of D-aspartate oxidase chemically modified phenylglyoxal

Flavins and Flavoproteins (Proc. Int. Symp. , 10th, Meeting Date 1990, Curti, B. , Ronchi S. , Zanetti, G. , eds. ) de Gruyter, Berlin, New York

189-192

1990

Bos taurus

brenda

Negri, A.; Massey, V.; Williams, C.H.; Schopfer, L.M.

The kinetic mechanism of beef kidney D-aspartate oxidase

J. Biol. Chem.

263

13557-13563

1988

Bos taurus

2901415

brenda

391722

Negri, A.; Massey, V.; Williams, C.H.

D-Aspartate oxidase from beef kidney. Purification and properties

J. Biol. Chem.

262

10026-10034

1987

Bos taurus

3611051

brenda

Burns, C.L.; Main, D.E.; Buckthal, D.J.; Hamilton, G.A.

Thiazolidine-2-carboxylate derivatives formed from glyoxylate and L-cysteine or L-cysteinylglycine as possible physiological substrates for D-aspartate oxidase

Biochem. Biophys. Res. Commun.

125

1039-1045

1984

Bos taurus

6151397

brenda

391724

Nasu, S.; Wicks, F.D.; Gholson, R.K.

The mammalian enzyme which replaces B protein of E.coli quinolinate synthetase is D-aspartate oxidase

Biochim. Biophys. Acta

704

240-252

1982

Bos taurus

7049247

brenda

Rinaldi, A.; Pellegrini, M.; Crifo, C.; de Marco, C.

Oxidation of meso-diaminosuccinic acid, a possible natural substrate for D-aspartate oxidase

Eur. J. Biochem.

117

635-638

1981

Bos taurus

7285908

brenda

391726

Jaroszewicz, L.

D-Asparatate oxidase in the thyroid gland

Enzyme

80-89

1975

Sus scrofa

236180

brenda

Dixon, M.; Kenworthy, P.

D-aspartate oxidase of kidney

Biochim. Biophys. Acta

146

54-76

1967

Oryctolagus cuniculus

6060479

brenda

Still, J.L.; Sperling, E.

On the prosthetic group of the D-aspartic oxidase

J. Biol. Chem.

182

585-589

1950

Sus scrofa, Oryctolagus cuniculus, Ovis aries

brenda

Takahashi, S.; Takahashi, T.; Kera, Y.; Matsunaga, R.; Shibuya, H.; Yamada, R.H.

Cloning and expression in Escherichia coli of the D-aspartate oxidase gene from the yeast Cryptococcus humicola and characterization of the recombinant enzyme

J. Biochem.

135

533-540

2004

Vanrija humicola (Q75WF1), Vanrija humicola

15115779

brenda

Sarower, M.G.; Matsui, T.; Abe, H.

Distribution and characteristics of D-amino acid and D-aspartate oxidases in fish tissues

J. Exp. Zool. A

295

151-159

2003

Chaunax fimbriatus, Cololabis saira, Cyprinus carpio, Evynnis tumifrons, Lateolabrax japonicus, Oncorhynchus keta, Oncorhynchus masou, Oncorhynchus mykiss, Pagrus major, Paralichthys olivaceus, Plecoglossus altivelis, Pseudopleuronectes yokohamae, Sardinops melanosticta, Scomber japonicus, Thamnaconus tessellatus, Trachurus japonicus, Verasper variegatus

12541299

brenda

Sarower, M.G.; Matsui, T.; Abe, H.

Distribution and substrate specificity of D-amino acid and D-aspartate oxidases in marine invertebrates

Science Asia

335-340

2004

Meretrix lusoria, Mizuhopecten yessoensis, Mytilus galloprovincialis, Octopus vulgaris, Penaeus japonicus, Procambarus clarkii, Todarodes pacificus, Turbo cornutus

brenda

Katane, M.; Seida, Y.; Sekine, M.; Furuchi, T.; Homma, H.

Caenorhabditis elegans has two genes encoding functional D-aspartate oxidases

FEBS J.

274

137-149

2007

Caenorhabditis elegans

17140416

brenda

677271

Takahashi, S.; Kakuichi, T.; Fujii, K.; Kera, Y.; Yamada, R.

Physiological role of D-aspartate oxidase in the assimilation and detoxification of D-aspartate in the yeast Cryptococcus humicola

Yeast

1203-1212

2005

Vanrija humicola

16278929

brenda

Katane, M.; Furuchi, T.; Sekine, M.; Homma, H.

Molecular cloning of a cDNA encoding mouse D-aspartate oxidase and functional characterization of its recombinant proteins by site-directed mutagenesis

Amino Acids

69-78

2007

Mus musculus

17469229

brenda

Katane, M.; Hanai, T.; Furuchi, T.; Sekine, M.; Homma, H.

Hyperactive mutants of mouse D-aspartate oxidase: mutagenesis of the active site residue serine 308

Amino Acids

75-82

2008

Mus musculus (Q0E9Q7), Mus musculus

18235994

brenda

686597

Huang, A.S.; Lee, D.A.; Blackshaw, S.

D-Aspartate and D-aspartate oxidase show selective and developmentally dynamic localization in mouse retina

Exp. Eye Res.

704-709

2008

Mus musculus

18314103

brenda

Yamamoto, A.; Tanaka, H.; Ishida, T.; Horiike, K.

Functional and structural characterization of D-aspartate oxidase from porcine kidney: non-Michaelis kinetics due to substrate activation

J. Biochem.

141

363-376

2007

Sus scrofa (A3KCL7), Sus scrofa

17234685

brenda

Katane, M.; Saitoh, Y.; Hanai, T.; Sekine, M.; Furuchi, T.; Koyama, N.; Nakagome, I.; Tomoda, H.; Hirono, S.; Homma, H.

Thiolactomycin inhibits D-aspartate oxidase: a novel approach to probing the active site environment

Biochimie

1371-1378

2010

Homo sapiens, Mus musculus

20603179

brenda

Katane, M.; Saitoh, Y.; Seida, Y.; Sekine, M.; Furuchi, T.; Homma, H.

Comparative characterization of three D-aspartate oxidases and one D-amino acid oxidase from Caenorhabditis elegans

Chem. Biodivers.

1424-1434

2010

Caenorhabditis elegans

20564561

brenda

Katane, M.; Homma, H.

D-aspartate oxidase: The sole catabolic enzyme acting on free D-aspartate in mammals

Chem. Biodivers.

1435-1449

2010

Homo sapiens, Rattus norvegicus, Mus musculus, Sus scrofa, Ovis aries, Bos taurus, Vanrija humicola, Caenorhabditis elegans

20564562

brenda

Burrone, L.; Di Giovanni, M.; Di Fiore, M.M.; Baccari, G.C.; Santillo, A.

Effects of D-aspartate treatment on D-aspartate oxidase, superoxide dismutase, and caspase 3 activities in frog (Rana esculenta) tissues

Chem. Biodivers.

1459-1466

2010

Pelophylax lessonae

20564564

brenda

Topo, E.; Fisher, G.; Sorricelli, A.; Errico, F.; Usiello, A.; DAniello, A.

Thyroid hormones and D-aspartic acid, D-aspartate oxidase, D-aspartate racemase, H2O2, and ROS in rats and mice

Chem. Biodivers.

1467-1478

2010

Mus musculus, Rattus norvegicus

20564565

brenda

di Giovanni, M.; Burrone, L.; Baccari, G.; Topo, E.; Santillo, A.

Distribution of free D-aspartic acid and D-aspartate oxidase in frog Rana esculenta tissues

J. Exp. Zool.

313 A

137-143

2010

Pelophylax lessonae

20108220

brenda

Takahashi, S.; Matsumoto, S.; Maruyama, K.; Wakaizumi, A.; Abe, K.; Kera, Y.; Yamada, R.

An active-site mutation enhances the catalytic activity of the yeast Cryptococcus humicola D-aspartate oxidase

J. Mol. Catal. B

235-240

2009

Vanrija humicola (Q75WF1)

brenda

712818

Yamamoto, A.; Tanaka, H.; Ishida, T.; Horiike, K.

D-aspartate oxidase localisation in pituitary and pineal glands of the female pig

J. Neuroendocrinol.

1165-1172

2010

Sus scrofa

20819121

brenda

Senda, M.; Yamamoto, A.; Tanaka, H.; Ishida, T.; Horiike, K.; Senda, T.

Crystallization and preliminary crystallographic analysis of D-aspartate oxidase from porcine kidney

Acta Crystallogr. Sect. F

644-646

2012

Sus scrofa

22684060

brenda

Kato, S.; Ikuta, T.; Hemmi, H.; Takahashi, S.; Kera, Y.; Yoshimura, T.

Enzymatic assay for D-aspartic acid using D-aspartate oxidase and oxaloacetate decarboxylase

Biosci. Biotechnol. Biochem.

2150-2152

2012

Vanrija humicola

23132574

brenda

Saitoh, Y.; Katane, M.; Kawata, T.; Maeda, K.; Sekine, M.; Furuchi, T.; Kobuna, H.; Sakamoto, T.; Inoue, T.; Arai, H.; Nakagawa, Y.; Homma, H.

Spatiotemporal localization of D-amino acid oxidase and D-aspartate oxidases during development in Caenorhabditis elegans

Mol. Cell. Biol.

1967-1983

2012

Caenorhabditis elegans, Caenorhabditis elegans (Q19564), Caenorhabditis elegans (O45307), Caenorhabditis elegans N2, Caenorhabditis elegans N2 (Q19564), Caenorhabditis elegans N2 (O45307)

22393259

brenda

741688

Takahashi, S.; Furukawara, M.; Omae, K.; Tadokoro, N.; Saito, Y.; Abe, K.; Kera, Y.

A highly stable d-amino acid oxidase of the thermophilic bacterium Rubrobacter xylanophilus

Appl. Environ. Microbiol.

7219-7229

2014

no activity in Rubrobacter xylanophilus

25217016

brenda

Katane, M.; Kawata, T.; Nakayama, K.; Saitoh, Y.; Kaneko, Y.; Matsuda, S.; Saitoh, Y.; Miyamoto, T.; Sekine, M.; Homma, H.

Characterization of the enzymatic and structural properties of human D-aspartate oxidase and comparison with those of the rat and mouse enzymes

Biol. Pharm. Bull.

298-305

2015

Homo sapiens (Q99489), Homo sapiens, Mus musculus (Q0E9Q7), Mus musculus, Rattus norvegicus (D3ZDM7)

25747990

brenda

742426

Florio, E.; Keller, S.; Coretti, L.; Affinito, O.; Scala, G.; Errico, F.; Fico, A.; Boscia, F.; Sisalli, M.J.; Reccia, M.G.; Miele, G.; Monticelli, A.; Scorziello, A.; Lembo, F.; Colucci-DAmato, L.; Minchiotti, G.; Avvedimento, V.E.; Usiello, A.; Cocozza, S.; Chiariotti, L.

Tracking the evolution of epialleles during neural differentiation and brain development D-Aspartate oxidase as a model gene

Epigenetics

41-54

2017

Mus musculus (Q0E9Q7)

27858532

brenda

Takahashi, S.; Shimada, K.; Nozawa, S.; Goto, M.; Abe, K.; Kera, Y.

Possible role of a histidine residue in the substrate specificity of yeast D-aspartate oxidase

J. Biochem.

159

371-378

2016

Vanrija humicola (Q75WF1), Vanrija humicola

26519738

brenda

Katane, M.; Yamada, S.; Kawaguchi, G.; Chinen, M.; Matsumura, M.; Ando, T.; Doi, I.; Nakayama, K.; Kaneko, Y.; Matsuda, S.; Saitoh, Y.; Miyamoto, T.; Sekine, M.; Yamaotsu, N.; Hirono, S.; Homma, H.

Identification of novel D-aspartate oxidase inhibitors by in silico screening and their functional and structural characterization in vitro

J. Med. Chem.

7328-7340

2015

Homo sapiens (Q99489), Homo sapiens

26322531

brenda

Punzo, D.; Errico, F.; Cristino, L.; Sacchi, S.; Keller, S.; Belardo, C.; Luongo, L.; Nuzzo, T.; Imperatore, R.; Florio, E.; De Novellis, V.; Affinito, O.; Migliarini, S.; Maddaloni, G.; Sisalli, M.J.; Pasqualetti, M.; Pollegioni, L.; Maione, S.; Chiariotti, L.; Usiello, A.

Age-related changes in D-aspartate oxidase promoter methylation control extracellular D-aspartate levels and prevent precocious cell death during brain aging

J. Neurosci.

3064-3078

2016

Mus musculus (Q0E9Q7), Mus musculus

26961959

brenda

Han, H.; Miyoshi, Y.; Koga, R.; Mita, M.; Konno, R.; Hamase, K.

Changes in D-aspartic acid and D-glutamic acid levels in the tissues and physiological fluids of mice with various D-aspartate oxidase activities

J. Pharm. Biomed. Anal.

116

47-52

2015

Mus musculus

26058797

brenda

743350

Cristino, L.; Luongo, L.; Squillace, M.; Paolone, G.; Mango, D.; Piccinin, S.; Zianni, E.; Imperatore, R.; Iannotta, M.; Longo, F.; Errico, F.; Vescovi, A.L.; Morari, M.; Maione, S.; Gardoni, F.; Nistico, R.; Usiello, A.

D-aspartate oxidase influences glutamatergic system homeostasis in mammalian brain

Neurobiol. Aging

1890-1902

2015

Mus musculus (Q0E9Q7)

25771393

brenda

Sacchi, S.; Novellis, V.; Paolone, G.; Nuzzo, T.; Iannotta, M.; Belardo, C.; Squillace, M.; Bolognesi, P.; Rosini, E.; Motta, Z.; Frassineti, M.; Bertolino, A.; Pollegioni, L.; Morari, M.; Maione, S.; Errico, F.; Usiello, A.

Olanzapine, but not clozapine, increases glutamate release in the prefrontal cortex of freely moving mice by inhibiting D-aspartate oxidase activity

Sci. Rep.

46288

2017

Mus musculus (Q0E9Q7), Homo sapiens (Q99489), Homo sapiens

28393897

brenda

Takahashi, S.; Osugi, K.; Shimekake, Y.; Shinbo, A.; Abe, K.; Kera, Y.

Characterization and improvement of substrate-binding affinity of D-aspartate oxidase of the thermophilic fungus Thermomyces dupontii

Appl. Microbiol. Biotechnol.

103

4053-4064

2019

Thermomyces dupontii, Thermomyces dupontii NBRC 30541

30937498

brenda

762746

Katane, M.; Kanazawa, R.; Kobayashi, R.; Oishi, M.; Nakayama, K.; Saitoh, Y.; Miyamoto, T.; Sekine, M.; Homma, H.

Structure-function relationships in human D-aspartate oxidase characterisation of variants corresponding to known single nucleotide polymorphisms

Biochim. Biophys. Acta

1865

1129-1140

2017

Homo sapiens (C9K4X7), Homo sapiens

28629864

brenda

Katane, M.; Kuwabara, H.; Nakayama, K.; Saitoh, Y.; Miyamoto, T.; Sekine, M.; Homma, H.

Rat D-aspartate oxidase is more similar to the human enzyme than the mouse enzyme

Biochim. Biophys. Acta

1866

806-812

2018

Rattus norvegicus (D3ZDM7), Mus musculus (Q0E9Q7), Mus musculus

29292239

brenda

Katane, M.; Kuwabara, H.; Nakayama, K.; Saitoh, Y.; Miyamoto, T.; Sekine, M.; Homma, H.

Biochemical characterization of d-aspartate oxidase from Caenorhabditis elegans its potential use in the determination of free D-glutamate in biological samples

Biochim. Biophys. Acta

1868

140442

2020

Caenorhabditis elegans (O45307), Caenorhabditis elegans

32376478

brenda

Puggioni, V.; Savinelli, A.; Miceli, M.; Molla, G.; Pollegioni, L.; Sacchi, S.

Biochemical characterization of mouse D-aspartate oxidase

Biochim. Biophys. Acta

1868

140472

2020

Mus musculus (Q0E9Q7), Mus musculus

32553892

brenda

Molla, G.; Chaves-Sanjuan, A.; Savinelli, A.; Nardini, M.; Pollegioni, L.

Structure and kinetic properties of human D-aspartate oxidase, the enzyme-controlling D-aspartate levels in brain

FASEB J.

1182-1197

2020

Homo sapiens (Q99489), Homo sapiens

31914658

brenda