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Fig. 3 | Cancer & Metabolism

Fig. 3

From: Human mitochondrial MTHFD2 is a dual redox cofactor-specific methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase

Fig. 3

Redox cofactor specificity of MTHFD2 with CH2-H4PteGlu5. CH2-THF dehydrogenase activity of purified MTHFD2 was assayed with respect to CH2-H4PteGlu5 concentration using NAD+ (1.0 mM) (panel a) or NADP+ (6.0 mM) (panel b). NAD+-dependent reactions also included 25 mM P i . The data were fit to the Michaelis-Menten equation. c The ratio of NAD+- to NADP+-dependent activity plotted as a function of CH2-H4PteGlu5 2concentration. The 0–150 μM CH2-H4PteGlu5 range is magnified in panel (d). Data for MTHFD2L from ref. [11]. The shaded boxes in c and d indicate the reported mitochondrial matrix concentration ranges for 5,10-CH2-THF as described in Fig. 2

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