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- W2002105364 abstract "Summary In the duckweed Spirodela polyrhiza, NADP-dependent isocitrate dehydrogenases were detected and partially purified from cytosol (ICDH1; approximately 80 % of the total activity) and from chloroplasts (ICDH2; 20 %). The affinities of ICDH2 to isocitrate, NADP, Mn 2+ and Mg 2+ were higher than those of ICDH1. A possible metabolic regulation was tested by investigating the influence of several metabolites on the activity of both isoforms in vitro . Intermediates of the citrate cycle from the substrate side of ICDH (i.e. citrate, cis -aconitate, isocitrate) showed the tendency to stimulate both isoforms (with the exception of aconitate which inhibited ICDH1) whereas those intermediates from the product side (2-oxoglutarate, succinate) showed the opposite tendency. The strong inhibiting effect of 2-oxoglutarate may slow down the formation of this substrate of amino acid synthesis under conditions of a low nitrogen assimilation rate. Glutamate showed contrasting effects on the two isoforms: whereas ICDH1 was strongly stimulated (by more than 60 % at 300 μmol L −1 ), ICDH2 was strongly inhibited (e.g. by 60 % at 300 μmol L −1 and 80 % at 2 mmol L −1 ). The strong effects of glutamate clearly show the influence of an intermediate of the nitrogen metabolism on the rate of 2-oxoglutarate formation and thereby demonstrate possible interactions of nitrogen and carbon metabolisms by metabolic control of ICDHs." @default.
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- W2002105364 date "2002-01-01" @default.
- W2002105364 modified "2023-09-23" @default.
- W2002105364 title "Cytosolic and chloroplastic NADP-dependent isocitrate dehydrogenases in Spirodela polyrhiza. I. Regulation of activity by metabolitesin vitro" @default.
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- W2002105364 doi "https://doi.org/10.1078/0176-1617-00630" @default.
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