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 (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 | Comment | Organism |
---|---|---|
R618A | the mutation abolishes the activity of MnmC | Escherichia coli |
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 | ? | - |
? | |
S-adenosyl-L-methionine + carboxymethyluridine34 in tRNA | Escherichia coli | - |
S-adenosyl-L-homocysteine + 5-(2-methoxy-2-oxoethyl)uridine34 in tRNA | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | P77182 | gene JW5380 | - |
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 | 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 | 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 | ? | - |
? | |
S-adenosyl-L-methionine + carboxymethyluridine34 in tRNA | - |
Escherichia coli | S-adenosyl-L-homocysteine + 5-(2-methoxy-2-oxoethyl)uridine34 in tRNA | - |
? | |
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 | - |
? |
Subunits | Comment | Organism |
---|---|---|
More | methyltransferase domain MnmC2 domain adopts the canonical class I methyltransferase fold | Escherichia coli |
Synonyms | Comment | Organism |
---|---|---|
MnmC | - |
Escherichia coli |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
S-adenosyl-L-methionine | binding site structure, overview | Escherichia coli |
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 |