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Thymidylate synthase (FAD)

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thymidylate synthase (FAD)
Flavin-dependent thymidylate synthase tetramer, Thermotoga maritima
Identifiers
EC no.2.1.1.148
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
Search
PMCarticles
PubMedarticles
NCBIproteins

In enzymology, a thymidylate synthase (FAD) (EC 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

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

See also

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References

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  1. ^ Koehn, E. M.; Perissinotti, L. L.; Moghram, S.; Prabhakar, A.; Lesley, S. A.; Mathews, I. I.; Kohen, A. (2012). "Folate binding site of flavin-dependent thymidylate synthase". Proceedings of the National Academy of Sciences. 109 (39): 15722–15727. Bibcode:2012PNAS..10915722K. doi:10.1073/pnas.1206077109. PMC 3465422. PMID 23019356.