23S rRNA (uracil1939-C5)-methyltransferase

23S rRNA (uracil-C)-methyltransferase (EC 2.1.1.190, RumA, RNA uridine methyltransferase A, YgcA) is an enzyme with systematic name S-adenosyl-L-methionine:23S rRNA (uracil-C)-methyltransferase. This enzyme catalyses the following chemical reaction

S-adenosyl-L-methionine + uracil in 23S rRNA

\rightleftharpoons

S-adenosyl-L-homocysteine + 5-methyluracil in 23S rRNA

The enzyme specifically methylates uracil at C in 23S rRNA.

References

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.
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.
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.
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.
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.
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.

External links

23S+rRNA+(uracil1939-C5)-methyltransferase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)

Transferase: one carbon transferases (EC 2.1)

2.1.1: Methyl-

N-	Histamine N-methyltransferase Phenylethanolamine N-methyltransferase Amine N-methyltransferase Phosphatidylethanolamine N-methyltransferase
O-	5-hydroxyindole-O-methyltransferase/Acetylserotonin O-methyltransferase Catechol-O-methyl transferase
Homocysteine	Betaine-homocysteine methyltransferase Homocysteine methyltransferase Methionine synthase
Other	Phosphatidyl ethanolamine methyltransferase DNMT3B Histone methyltransferase Thymidylate synthase DNA methyltransferase Thiopurine methyltransferase Cyclopropane-fatty-acyl-phospholipid synthase

2.1.2: Hydroxymethyl-,
Formyl- and Related

Hydroxymethyltransferase	Serine hydroxymethyltransferase 3-methyl-2-oxobutanoate hydroxymethyltransferase
Formyltransferase	Phosphoribosylglycinamide formyltransferase Inosine monophosphate synthase
Other	Glutamate formimidoyltransferase Aminomethyltransferase

2.1.3: Carboxy-
and Carbamoyl

Carboxy	methylmalonyl-CoA carboxytransferase
Carbamoyl	Aspartate carbamoyltransferase Ornithine carbamoyltransferase Oxamate carbamoyltransferase Putrescine carbamoyltransferase 3-hydroxymethylcephem carbamoyltransferase Lysine carbamoyltransferase N-acetylornithine carbamoyltransferase

2.1.4: Amidine

Arginine:glycine amidinotransferase

v t e Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Diffusion-limited enzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator
Classification	EC number Enzyme superfamily Enzyme family List of enzymes
Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics
Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list) EC7 Translocases (list)

Portal:

Biology

Category:

EC 2.1.1