Literature summary for 2.1.1.207 extracted from

Armengod, M.E.; Moukadiri, I.; Prado, S.; Ruiz-Partida, R.; Benitez-Paez, A.; Villarroya, M.; Lomas, R.; Garzon, M.J.; Martinez-Zamora, A.; Meseguer, S.; Navarro-Gonzalez, C.
Enzymology of tRNA modification in the bacterial MnmEG pathway (2012), Biochimie, 94, 1510-1520.

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Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
17700	-	x * 17700, TrmL	Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
S-adenosyl-L-methionine + 5-carboxymethylaminomethyluridine34 in tRNA	Escherichia coli	TrmL catalyzes the methyl transfer from SAM to the 2'-OH of the wobble nucleotide in tRNALeu cmnm5UmAA, which decodes codons UUA and UUG in the Phe/Leu mixed box, and tRNALeu CmAA, which reads the UUG codon included in the Leu family box	S-adenosyl-L-homocysteine + 5-carboxymethylaminomethyl-2'-O-methyluridine34 in tRNA	o.e. tRNALeucmnm5UmAA	?

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	-	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
additional information	in addition to a pyrimidine at position 34, the enzyme requires the presence of N6-(isopentenyl)-2-methylthioadenosine (ms2i6A) at position 37 as a positive identity determinant. Modification i6A, produced by MiaA, is enough to promote recognition of the substrate tRNAs by TrmL. Recognition of an amber codon by the supP suppressor, which is a mutant tRNALeu CmAA carrying the A35U change in the anticodon, is impaired if the suppressor lacks the 2'-O-methylation at the wobble position	Escherichia coli	?	-	?
S-adenosyl-L-methionine + 5-carboxymethylaminomethyluridine34 in tRNA	TrmL catalyzes the methyl transfer from SAM to the 2'-OH of the wobble nucleotide in tRNALeu cmnm5UmAA, which decodes codons UUA and UUG in the Phe/Leu mixed box, and tRNALeu CmAA, which reads the UUG codon included in the Leu family box	Escherichia coli	S-adenosyl-L-homocysteine + 5-carboxymethylaminomethyl-2'-O-methyluridine34 in tRNA	o.e. tRNALeucmnm5UmAA	?
S-adenosyl-L-methionine + 5-carboxymethylaminomethyluridine34 in tRNA	TrmL catalyzes the methyl transfer from SAM to the 2'-OH of the wobble nucleotide in tRNALeu cmnm5UmAA, which decodes codons UUA and UUG in the Phe/Leu mixed box, and tRNALeu CmAA, which reads the UUG codon included in the Leu family box. The wobble nucleoside in tRNALeu cmnm5UmAA and tRNALeuCmAA is not thiolated. Nevertheless methylation of the 2'-hydroxyl group favors the C3'-endo ribose conformation for all nucleosides, although the effect is more marked with pyrimidines	Escherichia coli	S-adenosyl-L-homocysteine + 5-carboxymethylaminomethyl-2'-O-methyluridine34 in tRNA	o.e. tRNALeucmnm5UmAA	?

Subunits

Subunits	Comment	Organism
?	x * 17700, TrmL	Escherichia coli

Synonyms

Synonyms	Comment	Organism
Trml	-	Escherichia coli
YibK	-	Escherichia coli

Cofactor

Cofactor	Comment	Organism	Structure
additional information	no requirement of other protein cofactors	Escherichia coli
S-adenosyl-L-methionine	-	Escherichia coli

General Information

General Information	Comment	Organism
evolution	TrmL is a representative protein of SPOUTenzymes, a class of S-adenosyl-L-methionine-dependent methyltransferases that exhibit an unusual fold with a very deep topological knot. TrmL is one of the smallest alpha/beta-knot proteins	Escherichia coli
metabolism	modifications at the wobble uridine, U34, of tRNAs reading two degenerate codons ending in purine are complex and result from the activity of two multi-enzyme pathways, the IscSeMnmA and MnmEG pathways, which independently work on positions 2 and 5 of the U34 pyrimidine ring, respectively, and from a third single-step pathway, controlled by TrmL, i.e. YibK, that modifies the 2'-hydroxyl group of the ribose. TrmL occurs as a late step in the maturation of the tRNALeu isoacceptors	Escherichia coli

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Release 2023.1 (January 2023)