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Literature summary for 2.1.1.74 extracted from
- A catalytic intermediate and several flavin redox states stabilized by folate-dependent tRNA methyltransferase from Bacillus subtilis (2011), Biochemistry, 50, 5208-5219.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expressed in Escherichia coli as a His-tagged fusion protein | Bacillus subtilis |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Bacillus subtilis | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| using Ni-NTA chromatography | Bacillus subtilis |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 5,10-methylenetetrahydrofolate + tRNA UpsiC + FADH2 | - |
Bacillus subtilis | tetrahydrofolate + tRNA TpsiC + FAD | - |
? |  |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| folate-dependent tRNA methyltransferase | - |
Bacillus subtilis |
| TRMFO | - |
Bacillus subtilis |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 37 | - |
assay at | Bacillus subtilis |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.5 | - |
assay at | Bacillus subtilis |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| FADH2 | using spectroscopic characterization it is shown that TrmFO stabilizes the protonated semiquinone FADH and a catalytic intermediate containing most likely both methylenetetrahydrofolate and an FAD reduced form. TrmFO, in the absence of tRNA, maintains an insulated active site that locks up the methyl donor and protects the reduced forms of the flavin from deleterious oxidative reactions | Bacillus subtilis | |
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Release 2023.1 (January 2023)
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