Literature summary for 2.1.1.B122 extracted from

Benitez-Paez, A.; Villarroya, M.; Armengod, M.-A.
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 .

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Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	P36979	-	-

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	?	-	-
S-adenosyl-L-methionine + adenine37 in tRNAChimeraUUG	-	Escherichia coli	S-adenosyl-L-homocysteine + 2-methyladenine37 in tRNAChimeraUUG	-	?
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	-	?

Synonyms

Synonyms	Comment	Organism
NlmA	-	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

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Release 2023.1 (January 2023)