Partial Prification and Characterization of Dihydrouracil Oxidase, a Flavoprotein from Rhodotorula glutinis

概要

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An enzyme that uses molecular oxygen to oxidize dihydrouracil and dihydrothymine to uracil and thymine, respectively, has been found in the cells of Rhodotorula glutinis IFO-0389. This enzyme has been partially purified by conventional techniques and has been demonstrated to contain FMN. Its molecular weight was approximately 80,000. The Michaelis constant was 50 μM for both dihydrouracil and dihydrothymine.The isoelectric point was pH 5.5. The enzyme activity was optimal between pH 7 and 8. Stoichiometric studies showed that 1 mol of dihydrouracil was converted into 1 mol of uracil and hydrogen peroxide with the consumption of 1 mol of oxygen. We tentatively named this enzyme dihydrouracil oxidase.
社団法人日本生物工学会の論文
1986-06-25