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Literature summary for 2.1.1.187 extracted from

  • Hansen, L.H.; Kirpekar, F.; Douthwaite, S.
    Recognition of nucleotide G745 in 23 S ribosomal RNA by the RrmA methyltransferase (2001), J. Mol. Biol., 310, 1001-1010.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
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Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
S-adenosyl-L-methionine + guanine745 in 23S rRNA Escherichia coli
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S-adenosyl-L-homocysteine + N1-methylguanine745 in 23S rRNA
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Organism

Organism UniProt Comment Textmining
Escherichia coli P36999
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Purification (Commentary)

Purification (Comment) Organism
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Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
S-adenosyl-L-methionine + guanine745 in 23S rRNA
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Escherichia coli S-adenosyl-L-homocysteine + N1-methylguanine745 in 23S rRNA
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S-adenosyl-L-methionine + guanine745 in 23S rRNA methylation of the N1 position of nucleotide G745 in hairpin 35 of Escherichia coli 23S ribosomal RNA. Progressive truncation of the rRNA substrate shows that structures in stem-loops 33, 34 and 35 are required for methylation by RrmA. Multiple contacts between nucleotides in these stem-loops and RrmA are confirmed in footprinting experiments. No other RrmA contact is evident elsewhere in the rRNA. The RrmA contact sites on the rRNA are inaccessible in ribosomal particles and, consistent with this, 50S subunits or 70S ribosomes are not substrates for RrmA methylation. Methylate their target nucleotides only in the free RNA Escherichia coli S-adenosyl-L-homocysteine + N1-methylguanine745 in 23S rRNA
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General Information

General Information Comment Organism
malfunction lack of G745 methylation results in reduced rates of protein synthesis and growth. Addition of recombinant plasmid-encoded rrmA to an rrmA-defficient strain remedies these defects Escherichia coli