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S-adenosyl-L-methionine + uracil1939 in 23S rRNA
S-adenosyl-L-homocysteine + 5-methyluracil1939 in 23S rRNA
additional information
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S-adenosyl-L-methionine + uracil1939 in 23S rRNA
S-adenosyl-L-homocysteine + 5-methyluracil1939 in 23S rRNA
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S-adenosyl-L-methionine + uracil1939 in 23S rRNA
S-adenosyl-L-homocysteine + 5-methyluracil1939 in 23S rRNA
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S-adenosyl-L-methionine + uracil1939 in 23S rRNA
S-adenosyl-L-homocysteine + 5-methyluracil1939 in 23S rRNA
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S-adenosyl-L-methionine + uracil1939 in 23S rRNA
S-adenosyl-L-homocysteine + 5-methyluracil1939 in 23S rRNA
a purified recombinant version of YgcA retains its activity and specificity, and methylates U1939 in an RNA transcript in vitro
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S-adenosyl-L-methionine + uracil1939 in 23S rRNA
S-adenosyl-L-homocysteine + 5-methyluracil1939 in 23S rRNA
the enzymatic activity of RumA is measured for a 37-mer 23 RNA segment (19321968) and for a 12-mer 5' segment (19321943) lacking the 3' hairpin
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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. A 40-nucleotide 23 S rRNA fragment (nucleotide 19301969) also serves as an efficient substrate for the enzyme
identification of C5-uracil1939 as reaction product
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S-adenosyl-L-methionine + uracil1939 in 23S rRNA
S-adenosyl-L-homocysteine + 5-methyluracil1939 in 23S rRNA
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rRNA substrate structure, overview
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S-adenosyl-L-methionine + uracil1939 in 23S rRNA
S-adenosyl-L-homocysteine + 5-methyluracil1939 in 23S rRNA
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S-adenosyl-L-methionine + uracil1939 in 23S rRNA
S-adenosyl-L-homocysteine + 5-methyluracil1939 in 23S rRNA
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S-adenosyl-L-methionine + uracil1939 in 23S rRNA
S-adenosyl-L-homocysteine + 5-methyluracil1939 in 23S rRNA
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S-adenosyl-L-methionine + uracil1939 in 23S rRNA
S-adenosyl-L-homocysteine + 5-methyluracil1939 in 23S rRNA
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additional information
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methylation of U747 and U1939 in Bacillus subtilis rRNA is catalysed by a single enzyme, YefA, MALDI mass spectrometry product identification. YefA is not involved in tRNA methylation, or in 23S rRNA m554 methylation
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the enzyme also methylates uracil747 in 23S rRNA
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enzyme introduces C5 methylation at both U747 and U1939 of the 23S ribosomal RNA, i. e. catalyzes both the reactions of EC 2.1.1.189 and 2.1.1.190
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additional information
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enzyme introduces C5 methylation at both U747 and U1939 of the 23S ribosomal RNA, i. e. catalyzes both the reactions of EC 2.1.1.189 and 2.1.1.190
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additional information
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the enzyme also methylates uracil747 in 23S rRNA
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Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
S-adenosyl-L-methionine + uracil1939 in 23S rRNA
S-adenosyl-L-homocysteine + 5-methyluracil1939 in 23S rRNA
additional information
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S-adenosyl-L-methionine + uracil1939 in 23S rRNA
S-adenosyl-L-homocysteine + 5-methyluracil1939 in 23S rRNA
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S-adenosyl-L-methionine + uracil1939 in 23S rRNA
S-adenosyl-L-homocysteine + 5-methyluracil1939 in 23S rRNA
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S-adenosyl-L-methionine + uracil1939 in 23S rRNA
S-adenosyl-L-homocysteine + 5-methyluracil1939 in 23S rRNA
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S-adenosyl-L-methionine + uracil1939 in 23S rRNA
S-adenosyl-L-homocysteine + 5-methyluracil1939 in 23S rRNA
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S-adenosyl-L-methionine + uracil1939 in 23S rRNA
S-adenosyl-L-homocysteine + 5-methyluracil1939 in 23S rRNA
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S-adenosyl-L-methionine + uracil1939 in 23S rRNA
S-adenosyl-L-homocysteine + 5-methyluracil1939 in 23S rRNA
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additional information
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methylation of U747 and U1939 in Bacillus subtilis rRNA is catalysed by a single enzyme, YefA, MALDI mass spectrometry product identification. YefA is not involved in tRNA methylation, or in 23S rRNA m554 methylation
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additional information
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the enzyme also methylates uracil747 in 23S rRNA
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additional information
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the enzyme also methylates uracil747 in 23S rRNA
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Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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D265A
the specific activity of the mutant enzyme is 830fold lower than that of the wild-type enzyme
D265E
mutant enzyme has no activity
D363A
mutation results in complete loss of activity
D363N
the specific activity of the mutant enzyme is 2fold lower than that of the wild-type enzyme
E424Q
the mutant enzyme displays a biphasic reaction profile with an initial burst phase followed by a slow second phase, mutation results in at least 350fold reduction in the rate of proton abstraction
D381A
2% residual activity towards U747 RNA substrate, reaction of EC 2.11.189, 40% residual activity towards U1939 RNA substrate
F145A
5% residual activity towards U747 RNA substrate, reaction of EC 2.11.189, 120% activity towards U1939 RNA substrate
H151A
5% residual activity towards U747 RNA substrate,reaction of EC 2.11.189, 55% activity towards U1939 RNA substrate
N249A
35% residual activity towards U747 RNA substrate, reaction of EC 2.11.189, 55% residual activity towards U1939 RNA substrate
Q162A
18% residual activity towards U747 RNA substrate, reaction of EC 2.11.189, 160% activity towards U1939 RNA substrate
Q283A
8% residual activity towards U747 RNA substrate, reaction of EC 2.11.189, 50% residual activity towards U1939 RNA substrate
R127A
8% residual activity towards U747 RNA substrate, reaction of EC 2.11.189, 2% residual activity towards U1939 RNA substrate
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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Persaud, C.; Lu, Y.; Vila-Sanjurjo, A.; Campbell, J.L.; Finley, J.; O'Connor, M.
Mutagenesis of the modified bases, m(5)U1939 and psi2504, in Escherichia coli 23S rRNA
Biochem. Biophys. Res. Commun.
392
223-227
2010
Escherichia coli (P55135)
brenda
Lee, T.T.; Agarwalla, S.; Stroud, R.M.
A unique RNA fold in the RumA-RNA-cofactor ternary complex contributes to substrate selectivity and enzymatic function
Cell
120
599-611
2005
Escherichia coli (P55135)
brenda
Agarwalla, S.; Kealey, J.T.; Santi, D.V.; Stroud, R.M.
Characterization of the 23 S ribosomal RNA m5U1939 methyltransferase from Escherichia coli
J. Biol. Chem.
277
8835-8840
2002
Escherichia coli (P55135)
brenda
Agarwalla, S.; Stroud, R.M.; Gaffney, B.J.
Redox reactions of the iron-sulfur cluster in a ribosomal RNA methyltransferase, RumA: optical and EPR studies
J. Biol. Chem.
279
34123-34129
2004
Escherichia coli (P55135)
brenda
Madsen, C.T.; Mengel-Jorgensen, J.; Kirpekar, F.; Douthwaite, S.
Identifying the methyltransferases for m(5)U747 and m(5)U1939 in 23S rRNA using MALDI mass spectrometry
Nucleic Acids Res.
31
4738-4746
2003
Escherichia coli (P55135)
brenda
Lee, T.T.; Agarwalla, S.; Stroud, R.M.
Crystal structure of RumA, an iron-sulfur cluster containing E. coli ribosomal RNA 5-methyluridine methyltransferase
Structure
12
397-407
2004
Escherichia coli (P55135)
brenda
Desmolaize, B.; Fabret, C.; Bregeon, D.; Rose, S.; Grosjean, H.; Douthwaite, S.
A single methyltransferase YefA (RlmCD) catalyses both m5U747 and m5U1939 modifications in Bacillus subtilis 23S rRNA
Nucleic Acids Res.
39
9368-9375
2011
Bacillus subtilis
brenda
Auxilien, S.; Rasmussen, A.; Rose, S.; Brochier-Armanet, C.; Husson, C.; Fourmy, D.; Grosjean, H.; Douthwaite, S.
Specificity shifts in the rRNA and tRNA nucleotide targets of archaeal and bacterial m5U methyltransferases
RNA
17
45-53
2011
Escherichia coli
brenda
Lartigue, C.; Lebaudy, A.; Blanchard, A.; El Yacoubi, B.; Rose, S.; Grosjean, H.; Douthwaite, S.
The flavoprotein Mcap0476 (RlmFO) catalyzes m5U1939 modification in Mycoplasma capricolum 23SrRNA
Nucleic Acids Res.
42
8073-8082
2014
Mycoplasma capricolum (Q2SS13), Mycoplasma capricolum
brenda
Shoji, T.; Takaya, A.; Sato, Y.; Kimura, S.; Suzuki, T.; Yamamoto, T.
RlmCD-mediated U747 methylation promotes efficient G748 methylation by methyltransferase RlmAII in 23S rRNA in Streptococcus pneumoniae; interplay between two rRNA methylations responsible for telithromycin susceptibility
Nucleic Acids Res.
43
8964-8972
2015
Streptococcus pneumoniae, Streptococcus pneumoniae S1
brenda
Jiang, Y.; Li, F.; Wu, J.; Shi, Y.; Gong, Q.
Structural insights into substrate selectivity of ribosomal RNA methyltransferase RlmCD
PLoS ONE
12
e0185226
2017
Streptococcus pneumoniae (Q97R12)
brenda
Jiang, Y.; Yu, H.; Li, F.; Cheng, L.; Zhu, L.; Shi, Y.; Gong, Q.
Unveiling the structural features that determine the dual methyltransferase activities of Streptococcus pneumoniae RlmCD
PLoS Pathog.
14
e1007379
2018
Streptococcus pneumoniae (Q97R12)
brenda