In enzymology, a thymidylate synthase (FAD) (EC 2.1.1.148) is an enzyme that catalyzes the chemical reaction
5,10-methylenetetrahydrofolate + dUMP + FADH2 ⇌ {\displaystyle \rightleftharpoons } dTMP + tetrahydrofolate + FAD The 3 substrates of this enzyme are 5,10-methylenetetrahydrofolate, dUMP, and FADH2, whereas its 3 products are dTMP, tetrahydrofolate, and FAD. This enzyme belongs to the family of transferases, to be specific those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is 5,10-methylenetetrahydrofolate,FADH2:dUMP C-methyltransferase. Other names in common use include Thy1, and ThyX. This enzyme participates in pyrimidine metabolism and one carbon pool by folate. Most organisms, including humans, use the thyA- or TYMS-encoded classic thymidylate synthase whereas some bacteria use the similar flavin-dependent thymidylate synthase (FDTS) instead.
Structural studies As of late 2007, 3 structures have been solved for this class of enzymes, with PDB accession codes PDB: 2AF6, PDB: 2CFA, and PDB: 2GQ2.
See also Thymidylate synthetase
References
Myllykallio H, Lipowski G, Leduc D, Filee J, Forterre P, Liebl U (2002). "An alternative flavin-dependent mechanism for thymidylate synthesis". Science. 297 (5578): 105–7. Bibcode:2002Sci...297..105M. doi:10.1126/science.1072113. PMID 12029065. S2CID 12592540.


