DDO oxidizes D-Asp to OA

Stable Identifier
Reaction [transition]
Homo sapiens
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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
1601857 The primary structure of the flavoprotein D-aspartate oxidase from beef kidney

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

J. Biol. Chem. 1992
9163533 Structural and functional characterization of the human brain D-aspartate oxidase

Miura, R, Setoyama, C

J. Biochem. 1997
20603179 Thiolactomycin inhibits D-aspartate oxidase: a novel approach to probing the active site environment

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

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

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

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

Biochem. J. 1998
Catalyst Activity

D-aspartate oxidase activity of DDO:FAD [peroxisomal matrix]

Orthologous Events
Cross References
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