Biology:23S rRNA (uracil1939-C5)-methyltransferase

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Short description: Class of enzymes
23S rRNA (uracil1939-C5)-methyltransferase
Identifiers
EC number2.1.1.190
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB 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 [math]\displaystyle{ \rightleftharpoons }[/math] S-adenosyl-L-homocysteine + 5-methyluracil1939 in 23S rRNA

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

References

  1. "Characterization of the 23 S ribosomal RNA m5U1939 methyltransferase from Escherichia coli". The Journal of Biological Chemistry 277 (11): 8835–40. March 2002. doi:10.1074/jbc.M111825200. PMID 11779873. 
  2. "Crystal structure of RumA, an iron-sulfur cluster containing E. coli ribosomal RNA 5-methyluridine methyltransferase". Structure 12 (3): 397–407. March 2004. doi:10.1016/j.str.2004.02.009. PMID 15016356. 
  3. "Identifying the methyltransferases for m(5)U747 and m(5)U1939 in 23S rRNA using MALDI mass spectrometry". Nucleic Acids Research 31 (16): 4738–46. August 2003. doi:10.1093/nar/gkg657. PMID 12907714. 
  4. "Mutagenesis of the modified bases, m(5)U1939 and psi2504, in Escherichia coli 23S rRNA". Biochemical and Biophysical Research Communications 392 (2): 223–7. February 2010. doi:10.1016/j.bbrc.2010.01.021. PMID 20067766. 
  5. "Redox reactions of the iron-sulfur cluster in a ribosomal RNA methyltransferase, RumA: optical and EPR studies". The Journal of Biological Chemistry 279 (33): 34123–9. August 2004. doi:10.1074/jbc.M405702200. PMID 15181002. 
  6. "A unique RNA Fold in the RumA-RNA-cofactor ternary complex contributes to substrate selectivity and enzymatic function". Cell 120 (5): 599–611. March 2005. doi:10.1016/j.cell.2004.12.037. PMID 15766524. 

External links