thymidylate synthase (FAD) | |||||||
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Identifiers | |||||||
EC number | 2.1.1.148 | ||||||
Databases | |||||||
IntEnz | IntEnz view | ||||||
BRENDA | BRENDA entry | ||||||
ExPASy | NiceZyme view | ||||||
KEGG | KEGG entry | ||||||
MetaCyc | metabolic pathway | ||||||
PRIAM | profile | ||||||
PDB structures | RCSB PDB PDBe PDBsum | ||||||
Gene Ontology | AmiGO / EGO | ||||||
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In enzymology, a thymidylate synthase (FAD) (EC 2.1.1.148) is an enzyme that catalyzes the chemical reaction
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, specifically 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.
As of late 2007, 3 structures have been solved for this class of enzymes, with PDB accession codes 2AF6, 2CFA, and 2GQ2.
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