EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
2.1.1.74 | C193A | mutant is nearly as active as the wild-type enzyme | Bacillus subtilis |
2.1.1.74 | C226A | mutant loses both the tRNA methylation activity and the capacity to form a covalent complex with the 5-FU-mini-RNA | Bacillus subtilis |
2.1.1.74 | C53A | mutant is inactive but like the wild-type enzyme, mutant C53A is capable of forming a covalent complex with a 5-fluorouridine-containing mini-RNA. Mutation of Cys-53 changes the accessibility of the FAD-binding site and impairs the conformational stability of TrmFO | Bacillus subtilis |
2.1.1.74 | C53A/C226A | as for the single C226A mutant, no protein-RNA covalent complex is detectable with the double mutant | Bacillus subtilis |
2.1.1.74 | S54A | mutant is nearly as active as the wild-type enzyme | Bacillus subtilis |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
2.1.1.74 | Bacillus subtilis | - |
- |
- |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
2.1.1.74 | 5,10-methylenetetrahydrofolate + tRNA UpsiC + FADH2 | - |
Bacillus subtilis | tetrahydrofolate + tRNA TpsiC + FAD | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
2.1.1.74 | folate-dependent tRNA methyltransferase | - |
Bacillus subtilis |
2.1.1.74 | TRMFO | - |
Bacillus subtilis |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
2.1.1.74 | 25 | - |
assay at | Bacillus subtilis |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
2.1.1.74 | 8 | - |
assay at | Bacillus subtilis |