tRNA (uracil-5-)-methyltransferase

In enzymology, a tRNA (uracil-5-)-methyltransferase (EC 2.1.1.35) is an enzyme that catalyzes the chemical reaction

S-adenosyl-L-methionine + tRNA containing uridine at position 54 S-adenosyl-L-homocysteine + tRNA containing ribothymidine at position 54
tRNA (uracil-5-)-methyltransferase
Identifiers
EC no.2.1.1.35
CAS no.37257-02-6
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
Search
PMCarticles
PubMedarticles
NCBIproteins

Thus, the two substrates of this enzyme are S-adenosyl methionine and tRNA containing uridine at position 54, whereas its two products are S-adenosylhomocysteine and tRNA containing ribothymidine at position 54.

This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is S-adenosyl-L-methionine:tRNA (uracil-5-)-methyltransferase. Other names in common use include ribothymidyl synthase, transfer RNA uracil 5-methyltransferase, transfer RNA uracil methylase, tRNA uracil 5-methyltransferase, m5U-methyltransferase, tRNA:m5U54-methyltransferase, and RUMT.

References

    • Hurwitz J, Gold M, Anders M (1964). "The Enzymatic Methylation of Ribonucleic Acid and Deoxyribonucleic Acid. 3. Purification of Soluble Ribonucleic Acid-Methylating Enzymes". J. Biol. Chem. 239: 3462–3473. PMID 14245404.
    • Bjork GR, Svensson I (1969). "Studies on microbial RNA. Fractionation of tRNA methylases from Saccharomyces cerevisiae". Eur. J. Biochem. 9 (2): 207–15. doi:10.1111/j.1432-1033.1969.tb00596.x. PMID 4896260.
    • Greenberg R, Dudock B (1980). "Isolation and characterization of m5U-methyltransferase from Escherichia coli". J. Biol. Chem. 255 (17): 8296–302. PMID 6997293.
    • 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.
    • Kealey JT, Gu X, Santi DV (1994). "Enzymatic mechanism of tRNA (m5U54)methyltransferase". Biochimie. 76 (12): 1133–42. doi:10.1016/0300-9084(94)90042-6. PMID 7748948.
    • Gu X, Ivanetich KM, Santi DV (1996). "Recognition of the T-arm of tRNA by tRNA (m5U54)-methyltransferase is not sequence specific". Biochemistry. 35 (36): 11652–9. doi:10.1021/bi9612125. PMID 8794745.
    • 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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