Dihydrofolate reductase (DHFR)

The term "Folate metabolism enzyme" is not a specific canonical name but refers to a group of enzymes involved in the cellular processing of folates. The most clinically relevant and commonly targeted member is Dihydrofolate reductase (DHFR). DHFR catalyzes the reduction of dihydrofolic acid to tetrahydrofolic acid using NADPH as an electron donor—a critical step for regenerating active folates required for one-carbon transfer reactions in nucleotide biosynthesis and amino acid interconversion[1][3][4]. Inhibition of DHFR disrupts DNA synthesis, repair, and methylation processes essential for rapidly dividing cells; this underlies its role as a major target in cancer chemotherapy by agents such as methotrexate[1][2]. Other enzymes within the folate pathway include serine hydroxymethyltransferase, methionine synthase, glycinamide ribonucleotide transformylase, among others—each contributing to nucleotide or amino acid biosynthesis or methylation cycles[2][3]. Note: The query "Folate metabolism enzyme" is too broad; it should be mapped specifically to "Dihydrofolate reductase" when referring to drug targets unless context indicates another specific enzyme. If more detail on other individual enzymes is needed (e.g., methionine synthase), those should be specified.

Other names

Folate metabolism enzymeFolate pathway enzymeTetrahydrofolate synthase (rare)Dihydrofolate reductase (DHFR) family enzymes

Competitive inhibition of dihydrofolate reductase to block tetrahydrofolate production, thereby inhibiting DNA synthesis and cell division[1][2].