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thymidylate synthase (FAD)
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| Identifiers | ||||||
| EC number | 2.1.1.148 | |||||
| IntEnz | IntEnz view | |||||
| BRENDA | BRENDA entry | |||||
| ExPASy | NiceZyme view | |||||
| KEGG | KEGG entry | |||||
| MetaCyc | metabolic pathway | |||||
| PRIAM | profile | |||||
| PDB | structures | |||||
| 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
- 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, 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.
Structural studies
As of late 2007, 3 structures have been solved for this class of enzymes, with PDB accession codes 2AF6, 2CFA, and 2GQ2.
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. doi:. PMID 12029065.
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