Activity and Substrate Specificity of D-Amino Acid Oxidase in Kidneys of Various Animals

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Activity and substrate specificity of D-amino acid oxidase (EC 1. 4. 3. 3) from the kidney homogenates of four mammals (human, monkey, rat and mouse), one bird (chicken) and one amphibian (frog) were examined. Purified D-amino acid oxidase obtained from hog kidney was also examined. The highest specific activity was obtained from kidney homogenate when D-alanine was used as a substrate. The enzyme in frog kidney homogenate oxidized D-methionine at an exceptionally high rate. The enzymes of frog and chicken hardly oxidized D-tryptophan, whereas the enzymes of mammals oxidized it at a substantial rate. In human and monkey, D-phenylalanine was the best substrate among the D-amino acids examined for substrate specificity of the enzyme reaction, while in other animals, D-proline was the best substrate. The results, though preliminary, imply that a difference in substrate specificity correlates to phylogenical relationships among animals.
社団法人日本動物学会の論文
1981-09-25