23S rRNA (uracil1939-C5)-methyltransferase

23S rRNA (uracil1939-C5)-methyltransferase
Identifiers
EC number 2.1.1.190
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum

23S rRNA (uracil1939-C5)-methyltransferase (EC 2.1.1.190, RumA, RNA uridine methyltransferase A, YgcA) is an enzyme with systematic name S-adenosyl-L-methionine:23S rRNA (uracil1939-C5)-methyltransferase.[1][2][3][4][5][6] This enzyme catalyses the following chemical reaction

S-adenosyl-L-methionine + uracil1939 in 23S rRNA S-adenosyl-L-homocysteine + 5-methyluracil1939 in 23S rRNA

The enzyme specifically methylates uracil1939 at C5 in 23S rRNA.

References

  1. ↑ Agarwalla, S.; Kealey, J.T.; Santi, D.V.; Stroud, R.M. (2002). "Characterization of the 23 S ribosomal RNA m5U1939 methyltransferase from Escherichia coli". J. Biol. Chem. 277 (11): 8835–8840. doi:10.1074/jbc.M111825200. PMID 11779873.
  2. ↑ Lee, T.T.; Agarwalla, S.; Stroud, R.M. (2004). "Crystal structure of RumA, an iron-sulfur cluster containing E. coli ribosomal RNA 5-methyluridine methyltransferase". Structure. 12 (3): 397–407. doi:10.1016/j.str.2004.02.009. PMID 15016356.
  3. ↑ Madsen, C.T.; Mengel-Jorgensen, J.; Kirpekar, F.; Douthwaite, S. (2003). "Identifying the methyltransferases for m5U747 and m5U1939 in 23S rRNA using MALDI mass spectrometry". Nucleic Acids Res. 31: 4738–4746. doi:10.1093/nar/gkg657. PMC 169892. PMID 12907714.
  4. ↑ Persaud, C.; Lu, Y.; Vila-Sanjurjo, A.; Campbell, J.L.; Finley, J.; O'Connor, M. (2010). "Mutagenesis of the modified bases, m5U1939 and Ψ2504, in Escherichia coli 23S rRNA". Biochem. Biophys. Res. Commun. 392 (2): 223–227. doi:10.1016/j.bbrc.2010.01.021. PMID 20067766.
  5. ↑ Agarwalla, S.; Stroud, R.M.; Gaffney, B.J. (2004). "Redox reactions of the iron-sulfur cluster in a ribosomal RNA methyltransferase, RumA: optical and EPR studies". J. Biol. Chem. 279 (33): 34123–34129. doi:10.1074/jbc.M405702200. PMC 1237038. PMID 15181002.
  6. ↑ Lee, T.T.; Agarwalla, S.; Stroud, R.M. (2005). "A unique RNA Fold in the RumA-RNA-cofactor ternary complex contributes to substrate selectivity and enzymatic function". Cell. 120 (5): 599–611. doi:10.1016/j.cell.2004.12.037. PMID 15766524.
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