Methylenetetrahydrofolate Dehydrogenase (None)

Methylenetetrahydrofolate dehydrogenase (MTHFD) refers to a family of enzymes involved in folate-mediated one-carbon metabolism. These enzymes catalyze the reversible oxidation of 5,10-methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate using NADP+ as an electron acceptor. This activity is central to the interconversion of one-carbon units required for nucleotide biosynthesis and methylation reactions. MTHFD enzymes are key players in the folate cycle: Provide one-carbon units for synthesis of purines, thymidylates (dTMP), and remethylation of homocysteine to methionine. Support DNA synthesis/repair by generating substrates for thymidylate synthase. Participate in glyoxylate/dicarboxylate metabolism and overall cellular redox balance through NADPH production. MTHFD isoforms are being explored as potential drug targets—especially MTHFD2 due to its role in cancer cell proliferation and immune evasion mechanisms.

Other names

MTHFD5,10-methylenetetrahydrofolate dehydrogenaseC-1-tetrahydrofolate synthase

Inhibition of enzymatic activity