Folic acid pathway enzyme

Folic acid pathway enzymes are a group of **enzymes involved in the cellular processing and utilization of folic acid** (vitamin B9), which is essential for one-carbon transfer reactions. These include key steps in the **synthesis and repair of DNA**, methylation reactions that regulate gene expression, and amino acid interconversions. Major examples include **dihydrofolate reductase** (DHFR), which reduces folic acid to its active form tetrahydrofolate; **thymidylate synthase**, required for thymidine production; **methionine synthase**, which regenerates methionine from homocysteine; as well as several formyltransferases involved in purine biosynthesis[2][3]. These pathways are critical for rapidly dividing cells—such as those found in tumors—which is why several anticancer drugs target these enzymes by inhibiting their activity. Disruption can lead to impaired cell division or abnormal methylation patterns associated with cancer development. Deficiency or inhibition also affects blood cell formation and can result in anemia or developmental abnormalities such as neural tube defects during pregnancy. Note on correctness: The term "Folic acid pathway enzymes" refers collectively to a family/group rather than a single molecular target. For structured data purposes it is preferable to specify individual enzyme names such as "Dihydrofolate reductase" or "Thymidylate synthase." Therefore, **is_incorrect = true** because this entry lacks specificity—it does not refer uniquely to one canonical protein but rather an entire metabolic network.[1][2][3]

Other names

Folate metabolism enzymesFolate pathway enzymesOne-carbon metabolism enzymesEnzymes of folic acid metabolism

Inhibition of dihydrofolate reductase to block tetrahydrofolate production and thus DNA synthesis (e.g., methotrexate)[1] - Inhibition of thymidylate synthase or other folic acid-dependent enzymes to disrupt nucleotide biosynthesis[2]