Disease relevance of DDO

• The complete primary structure of the peroxisomal flavoenzyme D-aspartate oxidase from beef kidney has been determined by analyses of the peptides obtained through fragmentation of the carboxymethylated protein with trypsin, CNBr, heptafluorobutyric acid/CNBr and Staphylococcus aureus V8 protease [1].
• The flavoenzyme d-aspartate oxidase from beef kidney (DASPO, EC 1.4. 3.1) has been overexpressed in Escherichia coli [2].

High impact information on DDO

• Thus, D-aspartate oxidase presents two types of heterogeneity in the polypeptide chain in addition to the one already described concerning the possible content of FAD or 6-hydroxyflavin adenine dinucleotide [1].
• The flavoprotein D-aspartate oxidase (EC 1.4.3.1) has been purified to homogeneity from beef kidney cortex [3].
• D-Aspartate oxidase (EC 1.4.3.1) was assayed in subcellular fractions and in highly purified peroxisomes from rat, bovine and sheep kidney cortex as well as from rat liver [4].
• D-Aspartate oxidase (EC 1.4.3.1; D-ASPOX) specifically oxidizes the D-isomers of dicarboxylic amino acids such as aspartic or glutamic acid [5].
• We propose that the two essential arginine residues are located in the substrate binding site of D-aspartate oxidase [6].

Chemical compound and disease context of DDO

• The immediate reaction product of D-aspartate oxidase (iminoaspartate) is condensed with dihydroxyacetone phosphate to form quinolinate in a reaction catalyzed by E. coli quinolinate synthetase A protein [7].

Biological context of DDO

• Structural investigations show similarities in both the amino-acid composition and the N-terminal amino-acid sequence to bovine D-aspartate oxidase and porcine D-amino-acid oxidase [8].

Associations of DDO with chemical compounds

• Oxidation of meso-diaminosuccinic acid, a possible natural substrate for D-aspartate oxidase [9].
• Chemical modification of beef kidney D-aspartate oxidase by phenylglyoxal is a biphasic process involving the transient formation of an enzymatic species with a decreased activity versus dicarboxylic substrates, an increased activity versus D-proline and a new activity versus other monocarboxylic D-amino acids which is absent in the native protein [6].
• Thiazolidine-2-carboxylate derivatives formed from glyoxylate and L-cysteine or L-cysteinylglycine as possible physiological substrates for D-aspartate oxidase [10].
• Adducts of glyoxylate with L-cysteine or L-cysteinylglycine were found to be excellent substrates at low concentrations for beef kidney D-aspartate oxidase [10].
• The results imply that these thiazolidine derivatives are the likely physiological reactants for mammalian D-aspartate oxidase [10].

References