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Purification and characterization of 3,4-dihydroxyphenylalanine oxidative deaminase from Rhodobacter sphaeroides OU5

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An enzyme involved in the catabolism of 3,4-dihydroxyphenylalanine (DOPA) was isolated from Rhodobacter sphaeroides OU5. The enzyme catalyzes the formation of 3,4-dihydroxyphenylpyruvic acid (DOPP) and ammonia from DOPA. Formation of ammonia by DOPA oxidative deaminase was O2 dependent and the enzyme isolated to its homogeneity has 100% affinity for DOPA. DOPA oxidative deaminase is functional at low concentrations of the substrate (<100 mol·L-1) and is independent of NADH. The molecular mass of the purified enzyme is ~190 kDa and the enzyme could be a pentamer of 54, 42, 34, 25, and 23 kDa subunits as determined by SDS-PAGE.

Une enzyme impliquée dans le catabolisme de la 3,4-dihydroxyphénylalanine (DOPA) a été isolée de Rhodobacter sphaeroides OU5. L’enzyme catalyse la formation d’acide 3,4-dihydroxyphénylalanine pyruvique (DOPP) et d’ammoniac à partir de la DOPA. La formation de d’ammoniac par la DOPA désaminase oxydative est dépendante de l’O2 et l’enzyme isolée à homogénéité a 100 % d’affinité pour la DOPA. La DOPA désaminase oxydative est fonctionnelle à faible concentration de substrat (<100 mol·L-1) et est indépendante du NADH. La masse moléculaire de l’enzyme purifiée est d’environ 190 kDa et l’enzyme pourrait être constituée d’un pentamère de sous-unités de 54, 42, 34, 25 et 23 kDa, tel que déterminé par SDS PAGE.

Document Type: Research Article

Publication date: October 1, 2008

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  • Published since 1954, this monthly journal contains new research in the field of microbiology including applied microbiology and biotechnology; microbial structure and function; fungi and other eucaryotic protists; infection and immunity; microbial ecology; physiology, metabolism and enzymology; and virology, genetics, and molecular biology. It also publishes review articles and notes on an occasional basis, contributed by recognized scientists worldwide.
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