Purification and characterization of isocitrate lyase from Rhodopseudomonas sp. No. 7.

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Abstract
Isocitrate lyase was purified from the purple nonsulfur bacterium Rhodopseudomonas sp. No. 7. The purified enzyme was electrophoretically homogeneous. The molecular weights of the native enzyme and its subunit were estimated to be approximate 250, 000 and 62, 000 by gel filtration chromatography and SOS-polyacrylamide gel electrophoresis, respectively. The optimum pH for its activity was 6.5. The optimum temperature was 45°C. The Km for DL-isocitrate was 0.136 mM in potassium phosphate buffer (pH 6.0). Mg2+ was required for full activity of the enzyme as a non-essential activator. The enzyme activity was inhibited by SH-blocking reagents. Non-competitive inhibitory effects on the enzyme were examined with malate and succinate. The Ki for malate and succinate were 2.7 and 0.24 mM, respectively.

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