Abstract
Isocitrate dehydrogenase (IDH) in oleaginous microorganisms plays an essential role in fatty acid synthesis. We expressed and purified an IDH isozyme from the oleaginous fungus Mortierella alpina (MaIDH4) and identified its enzymatic properties. MaIDH4 is NADP+-dependent and has no detectable activity with NAD+. It exerts its maximum activity when Mn2+ is used as a cofactor, followed by Mg2+. The optimum temperatures was 60 °C and 65 °C, and the optimum pH was 8.5 and 9.5, in the presence of Mn2+ and Mg2+, respectively. The catalytic efficiency of MaIDH4 for NADP+ was 16.33 (Mn2+) and 3.86 (Mg2+) μM−1s−1, while that for isocitrate was 3.06 (Mn2+) and 0.65 (Mg2+) μM−1s−1. Characterization of the enzymatic properties of MaIDH4 provides a basis for further understanding lipid synthesis in M. alpina.
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