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Literature summary for 2.1.1.192 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 PubMedView publication on EuropePMC
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Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2 S-adenosyl-L-methionine + adenine2503 in 23S rRNA Escherichia coli
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 S-adenosyl-L-homocysteine + L-methionine + 5'-deoxyadenosine + 2-methyladenine2503 in 23S rRNA
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 ?
additional information Escherichia coli RlmN introduces m2A at position 2503 in the peptidyl transferase center of 23S RNA. RlmN is a dual-specificity enzyme that catalyzes methylation of both rRNA and tRNA, see for EC 2.1.1.66, substrate specificity analysis, overview ?
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Organism

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

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2 S-adenosyl-L-methionine + adenine2503 in 23S rRNA
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 Escherichia coli S-adenosyl-L-homocysteine + L-methionine + 5'-deoxyadenosine + 2-methyladenine2503 in 23S rRNA
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 ?
additional information RlmN introduces m2A at position 2503 in the peptidyl transferase center of 23S RNA. RlmN is a dual-specificity enzyme that catalyzes methylation of both rRNA and tRNA, see for EC 2.1.1.66, substrate specificity analysis, overview Escherichia coli ?
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additional information recombinant His-RlmN protein is able to catalyze the synthesis of m2A in a SAM-dependent manner on tRNAchimera UUG purified from DELTArlmN cells Escherichia coli ?
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Synonyms

Synonyms Comment Organism
radical S-adenosyl-L-methionine enzyme
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 Escherichia coli
radical SAM enzyme
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 Escherichia coli
RlmN
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 Escherichia coli
RlmN methyltransferase
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 Escherichia coli

Cofactor

Cofactor Comment Organism Structure
S-adenosyl-L-methionine dependent on Escherichia coli

General Information

General Information Comment Organism
malfunction the DrlmN mutant lacks m2A in both RNA types, whereas the expression of recombinant RlmN from a plasmid introduced into this mutant restores tRNA modification. RlmN inactivation increases the misreading of a UAG stop codon. Since loss of m2A37 from tRNA is expected to produce a hyperaccurate phenotype, the error-prone phenotype exhibited by the DrlmN mutant is due to loss of m2A from 23S rRNA Escherichia coli
physiological function RlmN introduces m2A at position 2503 in the peptidyl transferase center of 23S RNA. RlmN is a dual-specificity enzyme that catalyzes methylation of both rRNA and tRNA. RlmN works in a late step during tRNA maturation by recognizing a precise 3D structure of tRNA, see for EC 2.1.1.66. The m2A2503 modification plays a crucial role in the proofreading step occurring at the peptidyl transferase center Escherichia coli