Quinate:NAD oxidoreductase of germinating Phaseolus mungo seeds : Partial purification and some properties
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Quinate: NAD oxidoreductase, which catalyzes the interconversion of quinic acid and 3-dehydroquinic acid, has been extracted from liquid N_2-frozen powders of 2-day-old etiolated seedlings of Phaseolus mungo. The enzyme was partially purified by ammonium sulfate fractionation and by DEAE-cellulose and gel filtration column chromatographies, and was separable from shikimate: NADP oxidoreductase and 3-dehydroquinate hydro-lyase. The activity appeared to be maximal at pH 8.6-9.0. The apparent Km values at pH 8.6 were 0.48 mM for quinic acid and 0.043 mM for NAD. The involvement of sulfhydryl group in the reaction was demonstrated by the potent inhibitory action of both heavy metal ions and sulfhydryl inhibitors. The purified preparation of the enzyme was reasonably stable for storage in the presence of dithiothreitol. The metal ions tested, except Hg^<2+> and Ag^+, showed practically no inhibitory action on the enzyme activity. Aromatic amino acids and other aromatic and alicyclic compounds tested had little or no effect on the activity.
- 日本植物生理学会の論文
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