Literature summary for 2.1.1.224 extracted from

Grove, T.L.; Benner, J.S.; Radle, M.I.; Ahlum, J.H.; Landgraf, B.J.; Krebs, C.; Booker, S.J.
A radically different mechanism for S-adenosylmethionine-dependent methyltransferases (2011), Science, 332, 604-607.

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Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	-	-	-

Reaction

Reaction	Comment	Organism	Reaction ID
2 S-adenosyl-L-methionine + adenine2503 in 23S rRNA + 2 reduced [2Fe-2S] ferredoxin = S-adenosyl-L-homocysteine + L-methionine + 5'-deoxyadenosine + 8-methyladenine2503 in 23S rRNA + 2 oxidized [2Fe-2S] ferredoxin	the methyl group is not transferred directly from S-adenosyl-L-methionine to the RNA. Reaction proceeds by a ping-pong mechanism involving intermediate methylation of a conserved cysteine residue	Escherichia coli	a

Synonyms

Synonyms	Comment	Organism
Cfr	-	Escherichia coli

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Release 2023.1 (January 2023)