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- W2149257862 abstract "A novel oxidase, catalyzing in the presence of oxygen the removal of four hydrogen atoms from a number of tetrahydroprotoberberines with simultaneous production of 1 mol H2O2 and H2O each, has been discovered and purified to homogeneity from Berberis wilsoniae cell cultures. This enzyme, (S)-tetrahydroprotoberberine oxidase, exhibited strict specificity for the (S)-enantiomer of tetrahydroprotoberberines and 1-benzylisoquinoline alkaloids, a pH optimum at 8.9, a molecular mass of 105 kDa and consisted of two subunits each of 53 kDa and covalently bound flavin. The Km values for (S)-scoulerine and (S)-norreticuline were 25 microM and 150 microM respectively. Concentration of the end-products, either protoberberines or H2O2, greater than 0.5 mM caused severe enzyme inhibition. This catalyst was responsible for the conversion of (S)-tetrahydrocolumbamine to the key intermediate, columbamine, in the metabolic pathway leading to berberine, jatrorrhizine and palmatine." @default.
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- W2149257862 date "1988-07-01" @default.
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- W2149257862 title "Purification and properties of (S)-tetrahydroprotoberberine oxidase from suspension-cultured cells of Berberis wilsoniae" @default.
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- W2149257862 doi "https://doi.org/10.1111/j.1432-1033.1988.tb14160.x" @default.
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