Reactome | DDO oxidizes D-Asp to OA

DDO oxidizes D-Asp to OA

Stable Identifier

R-HSA-6810076

Type

Reaction [transition]

Species

Homo sapiens

Compartment

peroxisomal matrix

Synonyms

D-aspartate + H2O + O2 => H2O2 + NH4(+) + oxaloacetate

ReviewStatus

5/5

Locations in the PathwayBrowser

Expand all

General

SBML | | PDF

SVG | | PPTX | SBGN

Click the image above or here to open this reaction in the Pathway Browser
The layout of this reaction may differ from that in the pathway view due to the constraints in pathway layout

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 Negri, A, Ceciliani, F, Tedeschi, G, Simonic, T, Ronchi, S	J. Biol. Chem.	1992
9163533	Structural and functional characterization of the human brain D-aspartate oxidase Setoyama, C, Miura, R	J. Biochem.	1997
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