Abstract
Succinate dehydrogenase (EC 1.3.99.1) from Dictyostelium discoideum was purified 40-fold. The pH optimum for the reaction under in vitro conditions was 7.4. Divalent cations showed no effect on the enzyme activity. Lineweaver-Burk plots of initial velocity data were linear. The K m value for succinate was calculated to be 0.22 m M. Apparent K i values for fumarate, malonate, and oxaloacetate were 0.4, 0.02, and 0.003 m M, respectively. All three showed a competitive inhibition pattern. A comparison of the reaction rate in vivo with the calculated enzyme activity required in vivo ( V v) suggests that succinate dehydrogenase may be rate controlling to flux through the citric acid cycle.
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