Disease relevance of Isocitric acid c

• Subsequently, the ability of CitM to transport D-isocitrate was demonstrated by competition experiments and by heterologous exchange in right-side-out membrane vesicles prepared from E. coli cells expressing citM [1].

High impact information on Isocitric acid c

• Similarly, the Km of NAD+-linked isocitrate dehydrogenase for threo-Ds-isocitrate was lower in permeabilized mitochondria than in extracts under all the conditions investigated [2].
• The oxidative decarboxylation of D-isocitrate catalyzed by NADP-linked isocitrate dehydrogenase is activated by NADPH, the product of the reaction [3].
• Saturation curves with respect to the substrate threo-DS-isocitrate complexed with the metals including manganous, cadmium, cobaltous and zinc ions showed sigmoid relationships characteristic of allosteric enzymes [4].
• Aluminum ions (Al3+) acted as a partial competitive inhibitor of the enzyme with respect to the substrate threo-Ds-isocitrate and inhibited the enzyme non-competitively with respect to NADP at pH 6.85 [5].
• Isocitrate lyase (threo-DS-isocitrate glyoxylate-lyase, EC 4.1.3.1) was isolated from cotyledons of Lupinus seedlings, purified 100-fold with respect to its initial specific activity and characterized (Km, pH optimum, Mg2+ requirement, sulfhydryl inhibitors, and synthase activity) [6].

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