1. Structural studies

2. See also

3. References

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 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.^[1]

Structural studies

As of late 2007, 3 structures have been solved for this class of enzymes, with PDB accession codes {{PDB link|2AF6}}, {{PDB link|2CFA}}, and {{PDB link|2GQ2}}.

See also

• Thymidylate synthetase

References

• {{cite journal |vauthors=Myllykallio H, Lipowski G, Leduc D, Filee J, Forterre P, Liebl U | date = 2002 | title = An alternative flavin-dependent mechanism for thymidylate synthesis | journal = Science | volume = 297 | pages = 105–7 | pmid = 12029065 | doi = 10.1126/science.1072113 | issue = 5578 }}

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