From Wikipedia, the free encyclopedia
Class of enzymes
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
⇌
{\displaystyle \rightleftharpoons }
S-adenosyl-L-homocysteine +
5-methyluracil 1939 in 23S rRNA
The enzyme specifically methylates uracil1939 at C5 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
Activity Regulation Classification Kinetics Types