The genetic and biochemical properties of the D-amino acid oxidases in human tissues.
1. Two distinct forms of oxidases catalysing the oxidative deamidation of D-alpha-amino acids have been identified in human tissues: D-amino acid oxidase (DAMOX) and D-aspartate oxidase (DASOX). 2. The enzymes differ in their electrophoretic properties, tissue distribution, binding with flavine adenine denucleotide, heat stability, molecular size and possibly in subunit structure. 3. Neither enzyme exhibits genetic polymorphism in European populations, but a rare electrophoretic variant phenotype (DASOX 2-1) was identified which suggests that the DASOX locus is autosomal and independent of the DAMOX locus.
D000594:Amino Acid Oxidoreductases / Q000302:isolation & purification; D044383:Black People; D003605:D-Amino-Acid Oxidase / Q000235:genetics / Q000302:isolation & purification*; D050804:D-Aspartate Oxidase; D014644:Genetic Variation; D006358:Hot Temperature; D006801:Humans; D007526:Isoelectric Point; D007527:Isoenzymes / Q000302:isolation & purification*; D008099:Liver / Q000201:enzymology; D008970:Molecular Weight; D013379:Substrate Specificity; D013482:Superoxide Dismutase / Q000302:isolation & purification; D014018:Tissue Distribution; D044465:White People
D007527:Isoenzymes; D013482:Superoxide Dismutase; D000594:Amino Acid Oxidoreductases; D050804:D-Aspartate Oxidase; C494102:DDO protein, human; D003605:D-Amino-Acid Oxidase