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Literature summary for 2.1.1.B122 extracted from

  • Benitez-Paez, A.; Villarroya, M.; Armengod, M.E.
    The Escherichia coli RlmN methyltransferase is a dual-specificity enzyme that modifies both rRNA and tRNA and controls translational accuracy (2012), RNA, 18, 1783-1795.
    View publication on PubMed
Search for more literature for 2.1.1.B122

Organism

Organism UniProt Comment Textmining
Escherichia coli P36979
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information residue U35 and G36 are imprtant for recognition by NmlA Escherichia coli ?
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 ?
S-adenosyl-L-methionine + adenine37 in tRNAChimeraUUG the anticodon stem-loop of the tRNA scaffold in the substrate is replaced with the anticodon stem-loop of tRNAGlncmnm5s2UUG Escherichia coli S-adenosyl-L-homocysteine + 2-methyladenine37 in tRNAChimeraUUG
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 ?
S-adenosyl-L-methionine + adenine37 in tRNAChimeraUUG
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 Escherichia coli S-adenosyl-L-homocysteine + 2-methyladenine37 in tRNAChimeraUUG
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 ?

Synonyms

Synonyms Comment Organism
NlmA
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 Escherichia coli

General Information

General Information Comment Organism
physiological function RlmN is a dual-specificity enzyme that catalyzes methylation of both rRNA and tRNA. The RlmN mutant lacks 2-methyladenine in both tRNA set and in the peptidyl transferase center of 23S RNA. RlmN works in a late step during tRNA maturation by recognizing a precise 3D structure of tRNA. RlmN inactivation increases the misreading of a UAG stop codon Escherichia coli