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Literature summary for 2.1.1.207 extracted from

  • Zhou, M.; Long, T.; Fang, Z.P.; Zhou, X.L.; Liu, R.J.; Wang, E.D.
    Identification of determinants for tRNA substrate recognition by Escherichia coli C/U34 2-O-methyltransferase (2015), RNA Biol., 12, 900-911.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.1.1.207

Cloned(Commentary)

Cloned (Comment) Organism
gene rmL, recombinant expression of wild-type and mutant enzymes Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.00182 0.00537 cytidine34 in tRNALeuCAA wild-type tRNALeuCAA and diverse mutants thereof, pH 7.5, 37°C Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
S-adenosyl-L-methionine + cytidine34 in tRNALeuCAA Escherichia coli
-
 S-adenosyl-L-homocysteine + 2'-O-methylcytidine34 in tRNALeuCAA
-
 ?
S-adenosyl-L-methionine + cytidine34 in tRNALeuUAA Escherichia coli
-
 S-adenosyl-L-homocysteine + 2'-O-methylcytidine34 in tRNALeuUAA
-
 ?

Organism

Organism UniProt Comment Textmining
Escherichia coli P0AGJ7
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information anticodon stem-loop minihelices with an extension of 2 base pairs are the minimal substrate for EcTrmL methylation. A35 is a key residue for TrmL recognition, while A36-A37-A38 are important either via direct interaction with TrmL or due to the necessity for prior isopentenylation (i6) at A37. In addition, TrmL only methylates pyrimidines but not purine residues at the wobble position, and the 20-O-methylation relies on prior N6-isopentenyladenosine modification at position 37. tRNALeuCAA and tRNALeuUAA isoacceptors are the only two RNA substrates of TrmL. i6A37 is sufficient to restore 20-O-methylation at C34 of EctRNALeuCAA transcripts in vitro. TrmL activity is sensitive to the modified base at position 37, a defect in synthesis of ms2i6A37 at position 37, leads to the loss of 20-O-methylation at C/U 34 at tRNALeuCAA and tRNALeuUAA isoacceptors.16 The isopentenyl modification at position 37 of transcribed tRNALeu is sufficient to recruit TrmL for methylation of nucleotides C34/U34. Although the affinity of i6A-Ts-tRNALeu CAA to EcTrmL is lower than for wild-type EctRNALeuCAA, the i6A modification has a consequent effect on the binding strength of tRNA transcripts for EcTrmL Escherichia coli ?
-
 ?
S-adenosyl-L-methionine + cytidine34 in tRNALeuCAA
-
 Escherichia coli S-adenosyl-L-homocysteine + 2'-O-methylcytidine34 in tRNALeuCAA
-
 ?
S-adenosyl-L-methionine + cytidine34 in tRNALeuCAA diverse mutant variants of tRNALeuCAA, overview Escherichia coli S-adenosyl-L-homocysteine + 2'-O-methylcytidine34 in tRNALeuCAA
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 ?
S-adenosyl-L-methionine + cytidine34 in tRNALeuUAA
-
 Escherichia coli S-adenosyl-L-homocysteine + 2'-O-methylcytidine34 in tRNALeuUAA
-
 ?

Subunits

Subunits Comment Organism
More TrmL-catalyzed 2'-O-methylation requires its homodimerization Escherichia coli

Synonyms

Synonyms Comment Organism
C/U34 2-O-methyltransferase
-
 Escherichia coli
Trml
-
 Escherichia coli

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
 assay at Escherichia coli

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.0073 0.2 cytidine34 in tRNALeuCAA wild-type tRNALeuCAA and diverse mutants thereof, pH 7.5, 37°C Escherichia coli

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
 assay at Escherichia coli

Cofactor

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

General Information

General Information Comment Organism
evolution the enzyme belongs to the SPOUT tRNA MTase superfamily Escherichia coli
additional information TrmL-catalyzed 2'-O-methylation requires its homodimerization. TrmL exhibits a fine-tuned tRNA substrate recognition mechanism. The variable arm of tRNA is not a recognition element for EcTrmL. The anticodon stem of tRNA does not contain recognition elements for EcTrmL Escherichia coli
physiological function TrmL is the prokaryotic methyltransferase that catalyzes the transfer of the methyl group from S-adenosyl-L-methionine to the wobble base of tRNALeuCAA and tRNALeuUAA isoacceptors. This Cm34/Um34 modification affects codon-anticodon interactions and is essential for translational fidelity Escherichia coli