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Literature summary for 1.4.3.3 extracted from

  • Raibekas, A.A.; Fukui, K.; Massey, V.
    Design and properties of human D-amino acid oxidase with covalently attached flavin (2000), Proc. Natl. Acad. Sci. USA, 97, 3089-3093.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Homo sapiens

Protein Variants

Protein Variants Comment Organism
G281C decreased activity with D-amino acids Homo sapiens

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1
-
D-alanine wild-type Homo sapiens
8
-
D-alanine mutant G281C Homo sapiens
13
-
D-alanine FAD-S mutant enzyme Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
D-alanine + H2O + O2 Homo sapiens
-
pyruvic acid + NH3 + H2O2
-
?

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Homo sapiens

Source Tissue

Source Tissue Comment Organism Textmining
kidney
-
Homo sapiens
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
D-alanine + H2O + O2
-
Homo sapiens pyruvic acid + NH3 + H2O2
-
?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.5
-
D-alanine mutant G281C Homo sapiens
2.6
-
D-alanine FAD-S mutant enzyme Homo sapiens
10
-
D-alanine wild-type Homo sapiens

Cofactor

Cofactor Comment Organism Structure
FAD flavoprotein Homo sapiens