Abstract
The presence of a new enzyme functioning at the methylcitric acid cycle concerning propionate metabolism was demonstrated. The enzyme was separated from the usual aconitate hydratase (EC 4.2.1.3) of Saccharomycopsis lipolytica by DEAE-Sephadex column chromatography. The partially purified enzyme preparation could dehydrate synthetic 2-methylcitrate to form 2-methyl-cis-aconitate. The enzyme preparation had no activity on citrate, threo-DL-isocitrate, threo-Ds-2-methylisocitrate, DL-homocitrate and DL-citramalate. The optimum pH for enzyme activity was observed between 6.5 to 7.0. The molecular weight was estimated to be about 78,000. The trivial name of 2-methylcitrate dehydratase was hereafter given to the new enzyme. On the other hand, the enzyme fraction separated as aconitate hydratase with the chromatography could strongly catalyze the reversible reaction between 2-methyl-cis-aconitate and threo-Ds-2-methylisocitrate but had no activity on synthetic 2-methylcitrate.
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