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Literature summary for 2.1.1.35 extracted from
- Specificity shifts in the rRNA and tRNA nucleotide targets of archaeal and bacterial m5U methyltransferases (2011), RNA, 17, 45-53.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expressed in Escherichia coli as a His-tagged fusion protein | Pyrococcus abyssi |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Mg2+ | stimulating effect | Pyrococcus abyssi |  |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Pyrococcus abyssi | - |
the genome of the hyperthermophilic archaeon Pyrococcus abyssi contains two open reading frames, PAB0719 and PAB0760,which are shownby comparative phylogenetic analyses to belong to the COG2265 m5U methyltransferases | - |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| using Ni-NTA chromatography | Pyrococcus abyssi |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | recombinant PAB0719 is shown to function like TrmA from Escherichia coli and catalyzes m5U formation at position 54 in Pyrococcus abyssi tRNAs | Pyrococcus abyssi | ? | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| PAB0719 | - |
Pyrococcus abyssi |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 80 | - |
kinetics of m5U formation by PAB0760 proceed faster at 80°C than at 50°C | Pyrococcus abyssi |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.5 | - |
assay at | Pyrococcus abyssi |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| S-adenosyl-L-methionine | - |
Pyrococcus abyssi | |
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Release 2023.1 (January 2023)
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