Thymidylate synthase (FAD) explained

thymidylate synthase (FAD)
Ec Number:	2.1.1.148
Go Code:	0050797
Width:	270

In enzymology, a thymidylate synthase (FAD) is an enzyme that catalyzes the chemical reaction

5,10-methylenetetrahydrofolate + dUMP + FADH₂

\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.^[1]

Structural studies

As of late 2007, 3 structures have been solved for this class of enzymes, with PDB accession codes,, and .

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 . 105 - 7 . 12029065 . 10.1126/science.1072113 . 5578 . 2002Sci...297..105M . 12592540 . free .

Notes and References

1. 10.1073/pnas.1206077109. free. Folate binding site of flavin-dependent thymidylate synthase. 2012. Koehn. E. M.. Perissinotti. L. L.. Moghram. S.. Prabhakar. A.. Lesley. S. A.. Mathews. I. I.. Kohen. A.. Proceedings of the National Academy of Sciences. 109. 39. 15722–15727. 23019356. 3465422. 2012PNAS..10915722K.