Biology:tRNA (uracil-5-)-methyltransferase
| tRNA (uracil-5-)-methyltransferase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 2.1.1.35 | ||||||||
| CAS number | 37257-02-6 | ||||||||
| 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 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 [math]\displaystyle{ \rightleftharpoons }[/math] S-adenosyl-L-homocysteine + tRNA containing ribothymidine at position 54
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
- "The Enzymatic Methylation of Ribonucleic Acid and Deoxyribonucleic Acid. 3. Purification of Soluble Ribonucleic Acid-Methylating Enzymes". J. Biol. Chem. 239: 3462–3473. 1964. PMID 14245404.
- "Studies on microbial RNA. Fractionation of tRNA methylases from Saccharomyces cerevisiae". Eur. J. Biochem. 9 (2): 207–15. 1969. doi:10.1111/j.1432-1033.1969.tb00596.x. PMID 4896260.
- "Isolation and characterization of m5U-methyltransferase from Escherichia coli". J. Biol. Chem. 255 (17): 8296–302. 1980. PMID 6997293.
- "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.
- "Enzymatic mechanism of tRNA (m5U54)methyltransferase". Biochimie 76 (12): 1133–42. 1994. doi:10.1016/0300-9084(94)90042-6. PMID 7748948.
- "Recognition of the T-arm of tRNA by tRNA (m5U54)-methyltransferase is not sequence specific". Biochemistry 35 (36): 11652–9. 1996. doi:10.1021/bi9612125. PMID 8794745.
- "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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