The Enzyme Database

Your query returned 1 entry.    printer_iconPrintable version

EC 2.1.1.74     
Accepted name: methylenetetrahydrofolate—tRNA-(uracil54-C5)-methyltransferase (FADH2-oxidizing)
Reaction: 5,10-methylenetetrahydrofolate + uracil54 in tRNA + FADH2 = tetrahydrofolate + 5-methyluracil54 in tRNA + FAD
Glossary: Ψ = pseudouridine
T = ribothymidine = 5-methyluridine
Other name(s): folate-dependent ribothymidyl synthase; methylenetetrahydrofolate-transfer ribonucleate uracil 5-methyltransferase; 5,10-methylenetetrahydrofolate:tRNA-UΨC (uracil-5-)-methyl-transferase; 5,10-methylenetetrahydrofolate:tRNA (uracil-5-)-methyl-transferase; TrmFO; folate/FAD-dependent tRNA T54 methyltransferase
Systematic name: 5,10-methylenetetrahydrofolate:tRNA (uracil54-C5)-methyltransferase
Comments: Up to 25% of the bases in mature tRNA are post-translationally modified or hypermodified. One almost universal post-translational modification is the conversion of U54 into ribothymidine in the TΨC loop, and this modification is found in most species studied to date [2]. Unlike this enzyme, which uses 5,10-methylenetetrahydrofolate and FADH2 to supply the atoms for methylation of U54, EC 2.1.1.35, tRNA (uracil54-C5)-methyltransferase, uses S-adenosyl-L-methionine.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 56831-74-4
References:
1.  Delk, A.S., Nagle, D.P., Jr. and Rabinowitz, J.C. 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 (1980) 4387–4390. [PMID: 6768721]
2.  Becker, H.F., Motorin, Y., Sissler, M., Florentz, C. and Grosjean, H. Major identity determinants for enzymatic formation of ribothymidine and pseudouridine in the TΨ-loop of yeast tRNAs. J. Mol. Biol. 274 (1997) 505–518. [PMID: 9417931]
3.  Nishimasu, H., Ishitani, R., Yamashita, K., Iwashita, C., Hirata, A., Hori, H. and Nureki, O. Atomic structure of a folate/FAD-dependent tRNA T54 methyltransferase. Proc. Natl. Acad. Sci. USA 106 (2009) 8180–8185. [PMID: 19416846]
[EC 2.1.1.74 created 1983 as EC 2.1.2.12, transferred 1984 to EC 2.1.1.74, modified 2011]
 
 


Data © 2001–2016 IUBMB
Web site © 2005–2016 Andrew McDonald