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

BRENDA support

Literature summary for 1.4.3.15 extracted from

  • 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 (2020), Biochim. Biophys. Acta Proteins Proteom., 1868, 140442 .
    View publication on PubMed
Search for more literature for 1.4.3.15

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli, culture conditions for production of recombinant DDO-1 are optimized Caenorhabditis elegans

Organism

Organism UniProt Comment Textmining
Caenorhabditis elegans O45307
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Caenorhabditis elegans

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
D-aspartate + H2O + O2
-
 Caenorhabditis elegans oxaloacetate + NH3 + H2O2
-
 ?
D-glutamate + H2O + O2 the enzyme (DDO-1) efficiently and selectively degrades D-glutamate in addition to D-aspartate, even in the presence of various other amino acids Caenorhabditis elegans 2-oxoglutarate + NH3 + H2O2
-
 ?

Synonyms

Synonyms Comment Organism
D-aspartate oxidase
-
 Caenorhabditis elegans
DDO
-
 Caenorhabditis elegans
DDO-1
-
 Caenorhabditis elegans

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
37
-
 pH 8.3, 30 min, no loss of activity Caenorhabditis elegans
50
-
 pH 8.3, 30 min, the enzyme retainsd 65% of its maximum activity Caenorhabditis elegans
60
-
 pH 8.3, 30 min, almost all of the activity is lost Caenorhabditis elegans

Cofactor

Cofactor Comment Organism Structure
FAD flavoprotein with a noncovalently but tightly attached FAD Caenorhabditis elegans