Abstract
Methylisocitrate lyase catalyzing the cleavage of threoi-ds-2-methylisocitrate into pyruvate and succinate was purified about 60-fold from cell free extracts of Candida lipolytica. The purified enzyme required a divalent cation and a sulfhydryl compound for maximum activity. Sulfhydryl reagents strongly inhibited enzyme activity. The molecular weight was estimated to be about 1.2 × 105 by gel filtration. The enzyme was specific for threo-ds-2-methyliso-citrate (Km=7.7 × 10−4 m) and did not catalyze the cleavage of threo-dl-isocitrate. Attempts to detect condensation between pyruvate and succinate by the preparation were unsuccessful. The enzyme was activated by NAD but noncompetitively inhibited by NADH and NADPH: these results support the idea that this enzyme is also a regulatory enzyme of the methylcitric acid cycle concerning the oxidation of propionate to pyruvate.
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