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Literature summary extracted from

  • Douthwaite, S.; Jakobsen, L.; Yoshizawa, S.; Fourmy, D.
    Interaction of the tylosin-resistance methyltransferase RlmA II at its rRNA target differs from the orthologue RlmA I (2008), J. Mol. Biol., 378, 969-975.
    View publication on PubMed

Organism

EC Number Organism UniProt Comment Textmining
2.1.1.188 Streptococcus pneumoniae
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Purification (Commentary)

EC Number Purification (Comment) Organism
2.1.1.188
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 Streptococcus pneumoniae

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.1.1.188 S-adenosyl-L-methionine + guanine748 in 23S rRNA RlmAII makes multiple footprint contacts with nucleotides in stem–loops 33, 34 and 35, and does not interact elsewhere in the rRNA. Binding of RlmAII to the rRNA is dependent on the cofactor S-adenosylmethionine (or S-adenosylhomocysteine). RlmAII interacts with the same rRNA region as the orthologous enzyme RlmAI that methylates at nucleotide G745 Streptococcus pneumoniae S-adenosyl-L-homocysteine + N1-methylguanine748 in 23S rRNA
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 ?

Synonyms

EC Number Synonyms Comment Organism
2.1.1.188 RlmA II
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 Streptococcus pneumoniae
2.1.1.188 RlmA(II)
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 Streptococcus pneumoniae