Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 1.4.3.1 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

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

Cloned(Commentary)

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

Inhibitors

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

KM Value [mM]

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

Molecular Weight [Da]

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

Organism

Organism UniProt Comment Textmining
Sus scrofa A3KCL7
-
-

Purification (Commentary)

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

Source Tissue

Source Tissue Comment Organism Textmining
kidney
-
Sus scrofa
-

Specific Activity [micromol/min/mg]

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

Substrates and Products (Substrate)

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

Subunits

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

Synonyms

Synonyms Comment Organism
DDO
-
Sus scrofa

Turnover Number [1/s]

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

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5 9
-
Sus scrofa

pH Stability

pH Stability pH Stability Maximum Comment Organism
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

Cofactor Comment Organism Structure
FAD
-
Sus scrofa