23S rRNA (uracil1939-C5)-methyltransferase

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23S rRNA (uracil1939-C5)-methyltransferase
Identifiers
EC no. 2.1.1.190
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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 + uracil 1939 in 23S rRNA S-adenosyl-L-homocysteine + 5-methyluracil 1939 in 23S rRNA

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

Related Research Articles

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In enzymology, a rRNA (guanine-N2-)-methyltransferase (EC 2.1.1.52) is an enzyme that catalyzes the chemical reaction

In enzymology, a tRNA guanosine-2'-O-methyltransferase is an enzyme that catalyzes the chemical reaction

Radical SAMenzymes is a superfamily of enzymes that use a [4Fe-4S]+ cluster to reductively cleave S-adenosyl-L-methionine (SAM) to generate a radical, usually a 5′-deoxyadenosyl radical (5'-dAdo), as a critical intermediate. These enzymes utilize this radical intermediate to perform diverse transformations, often to functionalize unactivated C-H bonds. Radical SAM enzymes are involved in cofactor biosynthesis, enzyme activation, peptide modification, post-transcriptional and post-translational modifications, metalloprotein cluster formation, tRNA modification, lipid metabolism, biosynthesis of antibiotics and natural products etc. The vast majority of known radical SAM enzymes belong to the radical SAM superfamily, and have a cysteine-rich motif that matches or resembles CxxxCxxC. Radical SAM enzymes comprise the largest superfamily of metal-containing enzymes.

23S rRNA (uridine2552-2'-O)-methyltransferase is an enzyme with systematic name S-adenosyl-L-methionine:23S rRNA (uridine2552-2'-O-)-methyltransferase. This enzyme catalyses the following chemical reaction

16S rRNA (guanine1207-N2)-methyltransferase (EC 2.1.1.172, m2G1207 methyltransferase) is an enzyme with systematic name S-adenosyl-L-methionine:16S rRNA (guanine1207-N2)-methyltransferase. This enzyme catalyses the following chemical reaction

23S rRNA (guanine2445-N2)-methyltransferase (EC 2.1.1.173, ycbY (gene), rlmL (gene)) is an enzyme with systematic name S-adenosyl-L-methionine:23S rRNA (guanine2445-N2)-methyltransferase. This enzyme catalyses the following chemical reaction

23S rRNA (guanine1835-N2)-methyltransferase (EC 2.1.1.174, ygjO (gene), rlmG (gene), ribosomal RNA large subunit methyltransferase G) is an enzyme with systematic name S-adenosyl-L-methionine:23S rRNA (guanine1835-N2)-methyltransferase. This enzyme catalyses the following chemical reaction

16S rRNA (cytosine967-C5)-methyltransferase (EC 2.1.1.176, rsmB (gene), fmu (gene), 16S rRNA m5C967 methyltransferase) is an enzyme with systematic name S-adenosyl-L-methionine:16S rRNA (cytosine967-C5)-methyltransferase. This enzyme catalyses the following chemical reaction

23S rRNA (pseudouridine1915-N3)-methyltransferase (EC 2.1.1.177, YbeA, RlmH, pseudouridine methyltransferase, m3Psi methyltransferase, Psi1915-specific methyltransferase, rRNA large subunit methyltransferase H) is an enzyme with systematic name S-adenosyl-L-methionine:23S rRNA (pseudouridine1915-N3)-methyltransferase. This enzyme catalyses the following chemical reaction

16S rRNA (cytosine1407-C5)-methyltransferase (EC 2.1.1.178, RNA m5C methyltransferase YebU, RsmF, YebU) is an enzyme with systematic name S-adenosyl-L-methionine:16S rRNA (cytosine1407-C5)-methyltransferase. This enzyme catalyses the following chemical reaction

16S rRNA (adenine1408-N1)-methyltransferase (EC 2.1.1.180, kanamycin-apramycin resistance methylase, 16S rRNA:m1A1408 methyltransferase, KamB, NpmA, 16S rRNA m1A1408 methyltransferase) is an enzyme with systematic name S-adenosyl-L-methionine:16S rRNA (adenine1408-N1)-methyltransferase. This enzyme catalyses the following chemical reaction

23S rRNA (adenine1618-N6)-methyltransferase (EC 2.1.1.181, rRNA large subunit methyltransferase F, YbiN protein, rlmF (gene), m6A1618 methyltransferase) is an enzyme with systematic name S-adenosyl-L-methionine:23S rRNA (adenine1618-N6)-methyltransferase. This enzyme catalyses the following chemical reaction

16S rRNA (adenine1518-N6/adenine1519-N6)-dimethyltransferase (EC 2.1.1.182, S-adenosylmethionine-6-N',N'-adenosyl (rRNA) dimethyltransferase, KsgA, ksgA methyltransferase) is an enzyme with systematic name S-adenosyl-L-methionine:16S rRNA (adenine1518-N6/adenine1519-N6)-dimethyltransferase. This enzyme catalyses the following chemical reaction

23S rRNA (guanosine2251-2'-O)-methyltransferase is an enzyme with systematic name S-adenosyl-L-methionine:23S rRNA (guanosine2251-2'-O-)-methyltransferase. This enzyme catalyses the following chemical reaction

23S rRNA (guanine745-N1)-methyltransferase (EC 2.1.1.187, Rlma(I), Rlma1, 23S rRNA m1G745 methyltransferase, YebH, RlmAI methyltransferase, ribosomal RNA(m1G)-methylase, rRNA(m1G)methylase, RrmA, 23S rRNA:m1G745 methyltransferase) is an enzyme with systematic name S-adenosyl-L-methionine:23S rRNA (guanine745-N1)-methyltransferase. This enzyme catalyses the following chemical reaction

23S rRNA (uracil747-C5)-methyltransferase (EC 2.1.1.189, YbjF, RumB, RNA uridine methyltransferase B) is an enzyme with systematic name S-adenosyl-L-methionine:23S rRNA (uracil747-C5)-methyltransferase. This enzyme catalyses the following chemical reaction

23S rRNA (cytosine1962-C5)-methyltransferase (EC 2.1.1.191, RlmI, rRNA large subunit methyltransferase I, YccW) is an enzyme with systematic name S-adenosyl-L-methionine:23S rRNA (cytosine1962-C5)-methyltransferase. This enzyme catalyses the following chemical reaction

23S rRNA (adenosine1067-2'-O)-methyltransferase is an enzyme with systematic name S-adenosyl-L-methionine:23S rRNA (adenosine1067-2'-O)-methyltransferase. This enzyme catalyses the following chemical reaction

References

  1. Agarwalla S, Kealey JT, Santi DV, Stroud RM (March 2002). "Characterization of the 23 S ribosomal RNA m5U1939 methyltransferase from Escherichia coli". The Journal of Biological Chemistry. 277 (11): 8835–40. doi: 10.1074/jbc.M111825200 . PMID   11779873.
  2. Lee TT, Agarwalla S, Stroud RM (March 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 CT, Mengel-Jørgensen J, Kirpekar F, Douthwaite S (August 2003). "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. doi:10.1093/nar/gkg657. PMC   169892 . PMID   12907714.
  4. Persaud C, Lu Y, Vila-Sanjurjo A, Campbell JL, Finley J, O'Connor M (February 2010). "Mutagenesis of the modified bases, m(5)U1939 and psi2504, in Escherichia coli 23S rRNA". Biochemical and Biophysical Research Communications. 392 (2): 223–7. doi:10.1016/j.bbrc.2010.01.021. PMID   20067766.
  5. Agarwalla S, Stroud RM, Gaffney BJ (August 2004). "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. doi: 10.1074/jbc.M405702200 . PMC   1237038 . PMID   15181002.
  6. Lee TT, Agarwalla S, Stroud RM (March 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.