Biology:Methylenetetrahydrofolate—tRNA-(uracil-5-)-methyltransferase
| methylenetetrahydrofolate-tRNA-(uracil-5-)-methyltransferase (FADH2-oxidizing) | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 2.1.1.74 | ||||||||
| CAS number | 74665-78-4 | ||||||||
| 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 / QuickGO | ||||||||
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In enzymology, a methylenetetrahydrofolate-tRNA-(uracil-5-)-methyltransferase (EC 2.1.1.74) is an enzyme that catalyzes the chemical reaction
- 5,10-methylenetetrahydrofolate + tRNA containing uridine at position 54 + FADH2 [math]\displaystyle{ \rightleftharpoons }[/math] tetrahydrofolate + tRNA containing ribothymidine at position 54 + FAD
The 3 substrates of this enzyme are 5,10-methylenetetrahydrofolate, tRNA containing uridine at position 54, and FADH2, whereas its 3 products are tetrahydrofolate, tRNA containing ribothymidine at position 54, 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:tRNA (uracil-5-)-methyl-transferase. Other names in common use include (FADH2-oxidizing), folate-dependent ribothymidyl synthase, methylenetetrahydrofolate-transfer ribonucleate uracil, 5-methyltransferase, 5,10-methylenetetrahydrofolate:tRNA-UPsiC, and (uracil-5-)-methyl-transferase.
References
- "Methylenetetrahydrofolate-dependent biosynthesis of ribothymidine in transfer RNA of Streptococcus faecalis. Evidence for reduction of the 1-carbon unit by FADH2". J. Biol. Chem. 255 (10): 4387–90. 1980. PMID 6768721.
- "Major identity determinants for enzymatic formation of ribothymidine and pseudouridine in the T psi-loop of yeast tRNAs". J. Mol. Biol. 274 (4): 505–18. 1997. doi:10.1006/jmbi.1997.1417. PMID 9417931. https://univoak.eu/islandora/object/islandora%3A69893.
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