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Comments on Katherine M Walstrom et al. (2001) International C. elegans Meeting "Biochemical Characterization of C. elegans Malate Dehydrogenase" (0)
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Katherine M Walstrom, & Danny Gonzalez (2001). Biochemical Characterization of C. elegans Malate Dehydrogenase presented in International C. elegans Meeting. Unpublished information; cite only with author permission.
In my laboratory, we are overexpressing and biochemically characterizing C. elegans malate dehydrogenase (MDH), the last enzyme in the citric acid cycle. This enzyme, encoded by putative gene F20H11.3, appears to be the mitochondrial form of MDH, since it contains a mitochondrial import presequence. We have overexpressed and purified a version of this enzyme with the mitochondrial import presequence removed at the predicted cleavage site of the mitochondrial processing protease. The purified MDH enzyme has malate dehydrogenase activity that follows Michaelis-Menten kinetics when plotted versus oxaloacetate concentration, and the resulting Km is similar to the Km values for other MDH enzymes. Interestingly, the temperature dependence of the enzyme is a bell-shaped curve with a peak at approximately 30degC, suggesting that the enzyme is adapted to the growing temperature of C. elegans . We are grateful to Yuji Kohara for providing the cDNA clone of MDH.