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Literature summary for 2.1.1.228 extracted from
- Stabilization of tRNA (mG37) methyltransferase [TrmD] from Aquifex aeolicus by an intersubunit disulfide bond formation (2008), Genes Cells, 13, 807-816.
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| C20S | the C20S mutant protein forms a dimer structure even though it is missing the Cys20Cys20 disulfide bond between its two subunits. Incubation at 85°C for 20 min causes the precipitation of more than half of the C20S protein, while more than 70% of the wild-type enzyme is soluble at that temperature. Methyl-transfer activity of the C20S mutant protein is slightly less than that of the wild-type enzyme at 70°C. Comparison of the CD-spectra of wild-type and C20S proteins reveals that some of the alpha-helices in the C20S mutant protein are less tightly packed than the alpha-helices of the wild-type enzyme at 70°C | Aquifex aeolicus |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Aquifex aeolicus | O67463 | - |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant enzyme | Aquifex aeolicus |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| TrmD | - |
Aquifex aeolicus |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| additional information | - |
the Cys20Cys20 disulfide bond between its two subunits enhances the protein stability at 85°C | Aquifex aeolicus |
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