thymidylate synthase (FAD)

{{infobox enzyme

| Name = thymidylate synthase (FAD)

| EC_number = 2.1.1.148

| CAS_number = 850167-13-4

| GO_code = 0050797

| image = 5ior.jpg

| width = 270

| caption = Flavin-dependent thymidylate synthase tetramer, Thermotoga maritima

}}

In enzymology, a thymidylate synthase (FAD) ({{EC number|2.1.1.148}}) is an enzyme that catalyzes the chemical reaction

:5,10-methylenetetrahydrofolate + dUMP + FADH₂ $\backslash rightleftharpoons$ 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.{{cite journal |doi=10.1073/pnas.1206077109|doi-access=free|title=Folate binding site of flavin-dependent thymidylate synthase|year=2012|last1=Koehn|first1=E. M.|last2=Perissinotti|first2=L. L.|last3=Moghram|first3=S.|last4=Prabhakar|first4=A.|last5=Lesley|first5=S. A.|last6=Mathews|first6=I. I.|last7=Kohen|first7=A.|journal=Proceedings of the National Academy of Sciences|volume=109|issue=39|pages=15722–15727|pmid=23019356|pmc=3465422|bibcode=2012PNAS..10915722K}}