DDO oxidizes D-Asp to OA

Stable Identifier
R-HSA-6810076
Type
Reaction [transition]
Species
Homo sapiens
Compartment
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Peroxisomal DDO (D-aspartate oxidase) catalyzes the oxidation of D-Asp (D-aspartate) to OA (oxaloacetate) with the formation of H2O2. The human enzyme is a monomer with an FAD cofactor (Katane et al. 2010, 2015; Setoyama & Miura 1997), as is its well-characterized bovine homolog (Negri et al. 1992). Its peroxisomal location is inferred from studies in cultured cells of fusion proteins containing the carboxyterminal peptide sequence of DDO (Amery et al. 1998).

Literature References
PubMed ID Title Journal Year
9163533 Structural and functional characterization of the human brain D-aspartate oxidase

Setoyama, C, Miura, R

J. Biochem. 1997
1601857 The primary structure of the flavoprotein D-aspartate oxidase from beef kidney

Negri, A, Ceciliani, F, Tedeschi, G, Simonic, T, Ronchi, S

J. Biol. Chem. 1992
20603179 Thiolactomycin inhibits D-aspartate oxidase: a novel approach to probing the active site environment

Katane, M, Saitoh, Y, Hanai, T, Sekine, M, Furuchi, T, Koyama, N, Nakagome, I, Tomoda, H, Hirono, S, Homma, H

Biochimie 2010
25747990 Characterization of the enzymatic and structural properties of human D-aspartate oxidase and comparison with those of the rat and mouse enzymes

Katane, M, Kawata, T, Nakayama, K, Saitoh, Y, Kaneko, Y, Matsuda, S, Saitoh, Y, Miyamoto, T, Sekine, M, Homma, H

Biol. Pharm. Bull. 2015
9820813 C-terminal tripeptide Ser-Asn-Leu (SNL) of human D-aspartate oxidase is a functional peroxisome-targeting signal

Amery, L, Brees, C, Baes, M, Setoyama, C, Miura, R, Mannaerts, GP, Van Veldhoven, PP

Biochem. J. 1998
Participants
Participant Of
Catalyst Activity
Catalyst Activity
Title
D-aspartate oxidase activity of DDO:FAD [peroxisomal matrix]
Physical Entity
Activity
Orthologous Events
Cross References
Rhea
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