DDO oxidizes D-Asp to OA
D-Asp + H2O + O2 → OA + NH4+ + H2O2
- Reactome
- R-HSA-6810076
- Compartment
- peroxisomal matrix
- Rhea
- RHEA:12513
Inputs
- D-AspCHEBI:29990, C4H6NO4, peroxisomal matrix
- H2OCHEBI:15377, H2O, peroxisomal matrix
- O2CHEBI:15379, O2, peroxisomal matrix
Outputs
- OACHEBI:16452, C4H2O5, peroxisomal matrix
- NH4+CHEBI:28938, H4N, peroxisomal matrix
- H2O2CHEBI:16240, H2O2, peroxisomal matrix
Catalysed by
- D-aspartate oxidase activity of DDO:FAD [peroxisomal matrix]EC 1.4.3.1
Literature
- C-terminal tripeptide Ser-Asn-Leu (SNL) of human D-aspartate oxidase is a functional peroxisome-targeting signal Biochem. J., 1998
- Characterization of the enzymatic and structural properties of human D-aspartate oxidase and comparison with those of the rat and mouse enzymes Biol. Pharm. Bull., 2015
- Thiolactomycin inhibits D-aspartate oxidase: a novel approach to probing the active site environment Biochimie, 2010
- The primary structure of the flavoprotein D-aspartate oxidase from beef kidney J. Biol. Chem., 1992
- Structural and functional characterization of the human brain D-aspartate oxidase J. Biochem., 1997