Translation of messenger RNA of pig kidney D-amino acid oxidase in a cell-free system.
In vitro synthesis of D-amino acid oxidase [D-amino acid: O2 oxidoreductase (deaminating), EC 1.4.3.3], one of the peroxisomal flavin enzymes, was performed using a rabbit reticulocyte lysate system in order to elucidate the biosynthetic pathway of the enzyme. The apparent molecular weight of the synthesized enzyme protein was the same as that of D-amino acid oxidase purified from pig kidney. On the other hand, the enzyme protein was not detectable when a wheat germ lysate system was used for the translation. Denaturation of pig kidney poly(A)+ RNA with methylmercury hydroxide prior to the translation was found to enhance the synthesis of the enzyme protein. These results suggest a tight conformational structure of the mRNA used.
D000818:Animals; D002474:Cell-Free System; D003605:D-Amino-Acid Oxidase / Q000096:biosynthesis* / Q000235:genetics; D007668:Kidney / Q000201:enzymology; D008767:Methylmercury Compounds / Q000494:pharmacology; D011061:Poly A / Q000502:physiology*; D014176:Protein Biosynthesis / Q000187:drug effects; D012333:RNA, Messenger / Q000502:physiology*; D013552:Swine
D008767:Methylmercury Compounds; D012333:RNA, Messenger; D011061:Poly A; D003605:D-Amino-Acid Oxidase; C020771:methylmercury hydroxide