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EC Tree
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
d-glutamate oxidase,
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D-glutamic acid oxidase
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D-glutamic oxidase
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D-glutamate + H2O + O2 = 2-oxoglutarate + NH3 + H2O2
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oxidative deamination
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D-glutamate:oxygen oxidoreductase (deaminating)
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D-aspartate + H2O + O2
oxaloacetate + NH3 + H2O2
D-glutamate + H2O + O2
2-oxoglutarate + NH3 + H2O2
N-methyl-D-aspartate + H2O + O2
oxaloacetate + methylamine + H2O2
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much poorer substrate than D-glutamate or D-aspartate
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D-aspartate + H2O + O2
oxaloacetate + NH3 + H2O2
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20% higher activity with pure oxygen than in air
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D-aspartate + H2O + O2
oxaloacetate + NH3 + H2O2
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70% higher activity with pure oxygen than in air
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D-aspartate + H2O + O2
oxaloacetate + NH3 + H2O2
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poorer substrate than D-glutamate
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D-aspartate + H2O + O2
oxaloacetate + NH3 + H2O2
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poorer substrate than D-glutamate
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D-glutamate + H2O + O2
2-oxoglutarate + NH3 + H2O2
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highly specific, no deamination of other D-amino acids found, 30% higher activity with pure oxygen than in air
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D-glutamate + H2O + O2
2-oxoglutarate + NH3 + H2O2
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better substrate than D-aspartate
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D-glutamate + H2O + O2
2-oxoglutarate + NH3 + H2O2
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highly specific, 70% higher activity with pure oxygen than in air
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D-glutamate + H2O + O2
2-oxoglutarate + NH3 + H2O2
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better substrate than D-aspartate
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D-aspartate + H2O + O2
oxaloacetate + NH3 + H2O2
D-glutamate + H2O + O2
2-oxoglutarate + NH3 + H2O2
D-aspartate + H2O + O2
oxaloacetate + NH3 + H2O2
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20% higher activity with pure oxygen than in air
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D-aspartate + H2O + O2
oxaloacetate + NH3 + H2O2
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70% higher activity with pure oxygen than in air
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D-aspartate + H2O + O2
oxaloacetate + NH3 + H2O2
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poorer substrate than D-glutamate
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D-aspartate + H2O + O2
oxaloacetate + NH3 + H2O2
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poorer substrate than D-glutamate
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D-glutamate + H2O + O2
2-oxoglutarate + NH3 + H2O2
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highly specific, no deamination of other D-amino acids found, 30% higher activity with pure oxygen than in air
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D-glutamate + H2O + O2
2-oxoglutarate + NH3 + H2O2
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better substrate than D-aspartate
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D-glutamate + H2O + O2
2-oxoglutarate + NH3 + H2O2
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highly specific, 70% higher activity with pure oxygen than in air
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D-glutamate + H2O + O2
2-oxoglutarate + NH3 + H2O2
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better substrate than D-aspartate
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FAD
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cannot be replaced by FMN
FAD
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cannot be replaced by FMN
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D-malate
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competitive inhibitor
Glutarate
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competitive inhibitor
iodoacetamide
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64% inhibition at 1 mM
iodoacetate
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68% inhibition at 0.1 mM
L-aspartate
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slight inhibition at 100 mM
L-glutamate
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slight inhibition at 100 mM
m-tartrate
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competitive inhibitor
o-Iodosobenzoate
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32% inhibition at 0.1 mM
succinate
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slight inhibition at 1 mM
urethane
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31% inhibition at 10 mM
p-chloromercuribenzoate
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95% inhibition at 0.1 mM
p-chloromercuribenzoate
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74% inhibition at 0.01 mM
Veronal
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strong inhibition
Veronal
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60% inhibition at 8 mM
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ethanol
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2fold activation in the presence of ethanol
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4.5
D-Aspartate
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D-glutamate
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crayfish
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brenda
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brenda
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brenda
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brenda
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brenda
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brenda
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45000
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1 * 45000, SDS-PAGE
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monomer
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1 * 45000, SDS-PAGE
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21
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stable for more than 5 h
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-30°C, no loss of activity for several months
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to homogeneity, precipitation techniques, calcium phosphate gel treatment
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Fukunaga, S.; Yno, S.; Takahashi, M.; Taguchi, S.; Kera, Y.; Odani, S.; Yamada, R.H.
Purification and properties of D-glutamate oxidase from Candida boidinii 2201
J. Ferment. Bioeng.
85
579-583
1998
[Candida] boidinii
brenda
Urich, K.
D-Glutamtoxydase aus der Antennendruse des Flusskrebses Orconectes limosus: Reinigung und Charakterisierung
Z. Naturforsch. B
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1508-1511
1968
Faxonius limosus
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brenda
Rocca, E.; Ghiretti, F.
Purification and properties of D-glutamic acid oxidase from Octopus vulgaris Lam.
Arch. Biochem. Biophys.
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336-349
1958
Octopus vulgaris
brenda
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1.4.3.7 D-glutamate oxidase
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