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Literature summary for 2.1.1.229 extracted from

  • Kitamura, A.; Sengoku, T.; Nishimoto, M.; Yokoyama, S.; Bessho, Y.
    Crystal structure of the bifunctional tRNA modification enzyme MnmC from Escherichia coli (2011), Protein Sci., 20, 1105-1113.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
gene JW5380, expression of wild-type and selenomethinone-labeled MnmC in Escherichia coli strains Rosetta2(DE3) and B834(DE3), respectively Escherichia coli

Crystallization (Commentary)

Crystallization (Comment) Organism
purified MnmC containing FAD, sitting drop method, the optimal reservoir solution contains 100 mM Bis-Tris, pH 5.5, containing 25% w/v PEG3350, 250 mM ammonium sulfate, and 10 mM hexamine cobalt(III) chloride, 5 days, X-ray diffraction structure determination and analysis at 3.0 A resolution Escherichia coli

Protein Variants

Protein Variants Comment Organism
R618A the mutation abolishes the activity of MnmC Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Escherichia coli the bifunctional enzyme MnmC catalyzes the two consecutive reactions that convert 5-carboxymethylaminomethyl uridine to 5-methylaminomethyl uridine. The C-terminal domain of MnmC is responsible for the FAD-dependent deacetylation of cmnm5U to 5-aminomethyl uridine, whereas the N-terminal domain catalyzes the subsequent S-adenosyl-L-methionine-dependent methylation of 5-aminomethyl uridine, leading to the final product, 5-methylaminomethyl uridine, coordination of the two consecutive reactions, overview ?
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?
S-adenosyl-L-methionine + carboxymethyluridine34 in tRNA Escherichia coli
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S-adenosyl-L-homocysteine + 5-(2-methoxy-2-oxoethyl)uridine34 in tRNA
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?

Organism

Organism UniProt Comment Textmining
Escherichia coli P77182 gene JW5380
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Purification (Commentary)

Purification (Comment) Organism
recombinant wild-type and selenomethinone-labeled enzymes from Escherichia coli by ultracentrifugation, anion exchange and hydrophobic interaction chromatography, another step of anion exchange chromatography and gel filtration Escherichia coli

Reaction

Reaction Comment Organism Reaction ID
S-adenosyl-L-methionine + carboxymethyluridine34 in tRNA = S-adenosyl-L-homocysteine + 5-(2-methoxy-2-oxoethyl)uridine34 in tRNA aspects of substrate recognition and catalytic mechanism. overview Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information the bifunctional enzyme MnmC catalyzes the two consecutive reactions that convert 5-carboxymethylaminomethyl uridine to 5-methylaminomethyl uridine. The C-terminal domain of MnmC is responsible for the FAD-dependent deacetylation of cmnm5U to 5-aminomethyl uridine, whereas the N-terminal domain catalyzes the subsequent S-adenosyl-L-methionine-dependent methylation of 5-aminomethyl uridine, leading to the final product, 5-methylaminomethyl uridine, coordination of the two consecutive reactions, overview Escherichia coli ?
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S-adenosyl-L-methionine + carboxymethyluridine34 in tRNA
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Escherichia coli S-adenosyl-L-homocysteine + 5-(2-methoxy-2-oxoethyl)uridine34 in tRNA
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?
S-adenosyl-L-methionine + carboxymethyluridine34 in tRNA residue Arg567 os involved in tRNA substrate recognition Escherichia coli S-adenosyl-L-homocysteine + 5-(2-methoxy-2-oxoethyl)uridine34 in tRNA
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?

Subunits

Subunits Comment Organism
More methyltransferase domain MnmC2 domain adopts the canonical class I methyltransferase fold Escherichia coli

Synonyms

Synonyms Comment Organism
MnmC
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Escherichia coli

Cofactor

Cofactor Comment Organism Structure
S-adenosyl-L-methionine binding site structure, overview Escherichia coli

General Information

General Information Comment Organism
physiological function posttranscriptional modifications of bases within the tRNA anticodon significantly affect the decoding system, uridines at the wobble position U34 of some tRNAs are modified to 5-methyluridine derivatives. These xm5U34-containing tRNAs read codons ending with A or G, whereas tRNAs with the unmodified U34 are able to read all four synonymous codons of a family box Escherichia coli