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Literature summary extracted from

  • 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 (2007), J. Biochem., 141, 363-376.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
1.4.3.1 D-Aspartate substrate activation at D-aspartate concentrations above 0.2 mM Sus scrofa
1.4.3.1 D-Glu substrate activation at D-glutamate concentrations above 4 mM Sus scrofa

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.4.3.1 expressed in Escherichia coli BL21 Star (DE 3) cells Sus scrofa

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.4.3.1 meso-tartrate high affinity for meso-tartrate Sus scrofa
1.4.3.1 N-Methyl-D-aspartate substrate inhibition Sus scrofa

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.4.3.1 0.547
-
 O2 apparent value, using D-glutamate as substrate Sus scrofa
1.4.3.1 0.613
-
 O2 apparent value, using D-aspartate as substrate Sus scrofa
1.4.3.1 2.01
-
 O2 apparent value, using N-methyl-D-aspartate as substrate Sus scrofa

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.4.3.1 146000
-
 low-angle laser light scattering photometry Sus scrofa
1.4.3.1 152000
-
 SDS-PAGE Sus scrofa
1.4.3.1 365000
-
 4 * 365000, low-angle laser light scattering photometry Sus scrofa
1.4.3.1 380000
-
 4 * 380000, SDS-PAGE Sus scrofa

Organism

EC Number Organism UniProt Comment Textmining
1.4.3.1 Sus scrofa A3KCL7
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.4.3.1 SP-Toyopearl column chromatography, Q-Sepharose column chromatography, PPG-Toyopearl column chromatography, and SuperSW3000 gel filtration Sus scrofa

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.4.3.1 kidney
-
 Sus scrofa
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.4.3.1 0.08
-
 unpurified recombinant enzyme Sus scrofa
1.4.3.1 62
-
 recombinant enzyme after 775fold purification Sus scrofa

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.4.3.1 D-aspartate + H2O + O2
-
 Sus scrofa oxaloacetate + NH3 + H2O2
-
 ?
1.4.3.1 D-glutamate + H2O + O2
-
 Sus scrofa 2-oxoglutarate + NH3 + H2O2
-
 ?
1.4.3.1 N-methyl-D-aspartate + H2O + O2
-
 Sus scrofa oxaloacetate + CH3NH2 + H2O2
-
 ?

Subunits

EC Number Subunits Comment Organism
1.4.3.1 homotetramer 4 * 365000, low-angle laser light scattering photometry Sus scrofa
1.4.3.1 homotetramer 4 * 380000, SDS-PAGE Sus scrofa

Synonyms

EC Number Synonyms Comment Organism
1.4.3.1 DDO
-
 Sus scrofa

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.4.3.1 30
-
 O2 apparent value, using D-glutamate as substrate Sus scrofa
1.4.3.1 172
-
 O2 apparent value, using D-aspartate as substrate Sus scrofa
1.4.3.1 635
-
 O2 apparent value, using N-methyl-D-aspartate as substrate Sus scrofa

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.4.3.1 7.5 9
-
 Sus scrofa

pH Stability

EC Number pH Stability pH Stability Maximum Comment Organism
1.4.3.1 7.5 9 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 Sus scrofa

Cofactor

EC Number Cofactor Comment Organism Structure
1.4.3.1 FAD
-
 Sus scrofa