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XB-ART-47939
Comp Biochem Physiol B Biochem Mol Biol October 1, 2013; 166 (2): 165-71.

D-Amino acid oxidase and presence of D-proline in Xenopus laevis.

Soma H , Furuya R , Kaneko R , Tsukamoto A , Shirasu K , Tanigawa M , Nagata Y .


Abstract
We purified D-amino acid oxidase (EC 1.4.3.3, DAO) from Xenopus laevis tadpoles. The optimal temperature and pH for enzyme activity were 35-40 °C and 8.3-9.0, respectively, depending on the substrate amino acids available to the enzyme; the highest activity was observed with D-proline followed by D-phenylalanine. Activity was significantly inhibited by p-hydroxymercuribenzoate, but only moderately by p-chloromercuribenzoate or benzoate. Enzyme activity was increased until the final tadpole stage, but was reduced to one-third in the adult and was localized primarily in the kidney. The tadpoles contained high concentrations of D-proline close to the final developmental stage and nearly no D-amino acids were detected in the adult frog, indicating that D-amino acid oxidase functions in metamorphosis.

PubMed ID: 23994361
Article link: Comp Biochem Physiol B Biochem Mol Biol

Genes referenced: dao



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