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- W2024779574 abstract "Abstract The isocitrate dehydrogenase activity specific for NADP+ has been studied in early turbot larvae and compared with that of their adult counterparts. The activity showed a broad optimum pH between 7.9 and 9.0, and an optimum temperature of 40°C (with an E a of 23.3 kJ/mol) and was inhibited by high ionic strength and heavy metals. The apparent K m values for the substrates were 16.7 μM for isocitrate, 3.5 for NADP+, 29.6 μM for Mg2+ and 3.3 μM for the Mg-isocitrate complex. The effect of the absence of Mg2+ on the enzyme affinity for its substrates is also reported. The enzyme stability was decreased by iodoacetic acid and this effect reverted by isocitrate. The enzyme activity was inhibited by metabolites such as citrate, oxoglutarate and adenine dinucleotides. It was also fully inhibited by the concerted action of glyoxylate and oxaloacetate." @default.
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- W2024779574 date "1994-01-01" @default.
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- W2024779574 title "Biochemical studies in marine species—II. NADP+-dependent isocitrate dehydrogenase from turbot (Scophthalmus maximus L.) larvae" @default.
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- W2024779574 doi "https://doi.org/10.1016/0305-0491(94)90225-9" @default.
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