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).
Tedeschi, G, Ceciliani, F, Ronchi, S, Simonic, T, Negri, A
Miura, R, Setoyama, C
Saitoh, Y, Homma, H, Hanai, T, Hirono, S, Koyama, N, Furuchi, T, Katane, M, Nakagome, I, Sekine, M, Tomoda, H
Saitoh, Y, Homma, H, Kaneko, Y, Kawata, T, Nakayama, K, Katane, M, Miyamoto, T, Sekine, M, Matsuda, S, Saitoh, Y
Baes, M, Brees, C, Van Veldhoven, PP, Miura, R, Amery, L, Mannaerts, GP, Setoyama, C
D-aspartate oxidase activity of DDO:FAD [peroxisomal matrix]
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