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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 ${\displaystyle \rightleftharpoons }$ 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

• Delk AS, Nagle DP, Rabinowitz JC (1980). "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. PMID 6768721.
• Becker HF, Motorin Y, Sissler M, Florentz C, Grosjean H (1997). "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. doi:10.1006/jmbi.1997.1417. PMID 9417931.

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