SUMMARY: In cell-free extracts of , an organism which has been reported to be isocitrate lyase negative, an isocitrate lyase activity of 52 ± 18 nmol min (mg protein) was observed after anaerobic growth in a chemostat on acetate plus nitrate, i.e. during denitrification. Following growth on succinate plus nitrate, isocitrate lyase activity was only 1 ± 2 nmol min (mg protein). In cell-free extracts derived from aerobic chemostat cultures isocitrate lyase activity was always nil. The identity of the enzyme was analysed using a number of different methods, namely () three different enzyme assays, () C-NMR spectroscopy of the reaction products, () HPLC analysis of the reaction products, () mass spectrometry of derivatized glyoxylate enzymically produced from isocitrate and () radiography of derivatized glyoxylate enzymically produced from [C]citrate. All these methods gave results consistent with the enzyme-catalysed conversion of isocitrate to glyoxylate and succinate.


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