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- W2064804975 abstract "Chloroplast NADP-malate dehydrogenase ((S)-malate:NADP+ oxidoreductase, EC 1.1.1.82) purified from pea (Pisum sativum) leaves can be activated by dithiothreitol-reduced chloroplast thioredoxin m or by reduction with dithiothreitol alone. Both thioredoxin m-dependent and dithiothreitol-dependent activation of NADP-malate dehydrogenase were more rapid at higher ionic strength (up to 2–3 M sult). Thioredoxin m-catalyzed dithiothreitol-dependent activation was maximal at 20 mM dithiothreitol, whereas direct activation of NADP-malate dehydrogenase by dithiothreiol was not saturated at 300 mM dithiothreitol. Both dithiothreitol and thioredoxin m-catalyzed activation were more rapid at higher pH, presumably reflecting ionization of the thiol groups of the dithiothreitol or thioredoxin m. Although dithiothreitol was the best low-molecular-weight activating agent, various monothiols, including 2-mercaptoethanol and glutathione, were capable of activating NADP-malate dehydrogenase either directly or via a thioredoxin-catalyzed reaction. Implications of this observation for the interpretation of previous results are discussed." @default.
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- W2064804975 date "1986-03-01" @default.
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- W2064804975 title "Studies on the mechanism of the reductive activation of NADP-malate dehydrogenase by thioredoxin m and low-molecular-weight thiols" @default.
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- W2064804975 doi "https://doi.org/10.1016/0167-4838(86)90221-9" @default.
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