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Two isoenzymes of NADP-linked isocitrate dehydrogenase have been identified in Acinetobacter lwoffi and have been termed isoenzyme-I and isoenzyme-II. The isoenzymes may be separated by ion-exchange chromatography on DEAE-cellulose, by gel filtration on Sephadex G-200, or by zonal ultracentrifugation in a sucrose gradient. Low concentrations of glyoxylate or pyruvate effect considerable stimulation of the activity of isoenzyme-II. The isoenzymes also differ in pH-dependence of activity, kinetic parameters, stability to heat or urea and molecular size. Whereas isoenzyme-I resembles the NADP-linked isocitrate dehydrogenases from other organisms in having a molecular weight under 1, isoenzyme-II is a much larger enzyme (molecular weight around 3) resembling the NAD-linked isocitrate dehydrogenases of higher organisms.

biochemical journal. cellular aspects

The isocitrate dehydrogenases of <i>Acinetobacter lwoffi</i>. Separation and properties of two nicotinamide–adenine dinucleotide phosphate-linked isoenzymes

The isocitrate dehydrogenases of Acinetobacter lwoffi. Separation and properties of two nicotinamide–adenine dinucleotide phosphate-linked isoenzymes