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- W1965152928 abstract "Abstract The effect of different salts on the NAD-specific isocitrate dehydrogenase from Blastocladiella emersonii has been studied. The results show that the salt inhibition depends on the size of the anions and that the ionic strength is of minor importance. The salts inhibit the enzyme in a competitive manner with regard to isocitrate. The isocitrate concentration giving half saturation increased by the same factor whether or not the activator AMP was present. The finding that higher salt concentrations are needed to inhibit the enzyme in the presence of AMP is due to the fact that in this case isocitrate is more tightly bound. Stopped-flow experiments demonstrated that when the enzyme was incubated with isocitrate and metal ions prior to initiation of the reaction by addition of NAD, the salt inhibition needed several seconds to be fully expressed. Moreover, a lag occurred before NADH was formed when the enzyme was mixed with its substrates and cofactor. The data suggest that the hysteretic properties of the enzyme are due to isomerization of the enzyme molecules, and that specific binding sites are involved in the salt inhibition." @default.
- W1965152928 created "2016-06-24" @default.
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- W1965152928 date "1975-02-01" @default.
- W1965152928 modified "2023-09-25" @default.
- W1965152928 title "Inhibitory effects of salts on the nicotinamide adenine dinucleotide specific isocitrate dehydrogenase from Blastocladiella emersonii" @default.
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- W1965152928 doi "https://doi.org/10.1016/0003-9861(75)90413-0" @default.
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