EC Number   |
Substrates |
Organism |
Products |
Reversibility |
|---|
   2.1.1.229 | more |
alternative mechanisms in formation of the 5-carboxymethyluridine34 side chain at wobble position, overview |
Saccharomyces cerevisiae |
? |
- |
? |
| 2.1.1.229 | more |
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 |
? |
- |
? |
| 2.1.1.229 | more |
methylaminomethyl modification of uridine or 2-thiouridine (mnm5U34 or mnm5s2U34) at the wobble position of tRNAs specific for glutamate, lysine and arginine are observed in Escherichia coli and allow for specific recognition of codons ending in A or G. In the biosynthetic pathway responsible for this posttranscriptional modification, the bifunctional enzyme MnmC catalyzes the conversion of its hypermodified substrate carboxymethylaminomethyl uridine (cmnm5U34) to mnm5U34. MnmC catalyzes the FAD-dependent oxidative cleavage of carboxymethyl group from cmnm5U34 via an imine intermediate to generate aminomethyl uridine (nm5U34), which is subsequently methylated by S-adenosyl-L-methionine to yield methylaminomethyl uridine (mnm5U34) |
Escherichia coli |
? |
- |
? |
| 2.1.1.229 | more |
methylaminomethyl modification of uridine or 2-thiouridine (mnm5U34 or mnm5s2U34) at the wobble position of tRNAs specific for glutamate, lysine and arginine are observed in Escherichia coli and allow for specific recognition of codons ending in A or G. In the biosynthetic pathway responsible for this posttranscriptional modification, the bifunctional enzyme MnmC catalyzes the conversion of its hypermodified substrate carboxymethylaminomethyl uridine (cmnm5U34) to mnm5U34. MnmC catalyzes the FAD-dependent oxidative cleavage of carboxymethyl group from cmnm5U34 via an imine intermediate to generate aminomethyl uridine (nm5U34), which is subsequently methylated by S-adenosyl-L-methionine to yield methylaminomethyl uridine (mnm5U34) |
Yersinia pestis |
? |
- |
? |
| 2.1.1.229 | more |
recombinant tagged Sc Trm9 protein purified from yeast methylates a saponified tRNA extract, demonstrating that Sc Trm9 is required for formation of the terminal methyl group of mcm5U |
Saccharomyces cerevisiae |
? |
- |
? |
| 2.1.1.229 | more |
methylaminomethyl modification of uridine or 2-thiouridine (mnm5U34 or mnm5s2U34) at the wobble position of tRNAs specific for glutamate, lysine and arginine are observed in Escherichia coli and allow for specific recognition of codons ending in A or G. In the biosynthetic pathway responsible for this posttranscriptional modification, the bifunctional enzyme MnmC catalyzes the conversion of its hypermodified substrate carboxymethylaminomethyl uridine (cmnm5U34) to mnm5U34. MnmC catalyzes the FAD-dependent oxidative cleavage of carboxymethyl group from cmnm5U34 via an imine intermediate to generate aminomethyl uridine (nm5U34), which is subsequently methylated by S-adenosyl-L-methionine to yield methylaminomethyl uridine (mnm5U34) |
Yersinia pestis Kim |
? |
- |
? |
| 2.1.1.229 | S-adenosyl-L-methionine + carboxymethyl-2-thiouridine34 in tRNA |
Trm9-Trm112, subunit Trm112 is required for the activity, but role of Sc Trm112 in the complex is not for catalysis |
Saccharomyces cerevisiae |
S-adenosyl-L-homocysteine + 5-(2-methoxy-2-oxoethyl)-2-thiouridine34 in tRNA |
- |
? |
| 2.1.1.229 | S-adenosyl-L-methionine + carboxymethylaminomethyl 2-thiouridine34 in tRNAGlu |
- |
Escherichia coli |
S-adenosyl-L-homocysteine + methylaminomethyl 2-thiouridine34 in tRNAGlu + hydroxyacetate |
- |
? |
| 2.1.1.229 | S-adenosyl-L-methionine + carboxymethylaminomethyl 2-thiouridine34 in tRNAGlu |
- |
Yersinia pestis |
S-adenosyl-L-homocysteine + methylaminomethyl 2-thiouridine34 in tRNAGlu + hydroxyacetate |
- |
? |
| 2.1.1.229 | S-adenosyl-L-methionine + carboxymethylaminomethyl 2-thiouridine34 in tRNAGlu |
- |
Yersinia pestis Kim |
S-adenosyl-L-homocysteine + methylaminomethyl 2-thiouridine34 in tRNAGlu + hydroxyacetate |
- |
? |
