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Literature summary extracted from
- The activity of a thermostable lipoyl synthase from Sulfolobus solfataricus with a synthetic octanoyl substrate (2006), Anal. Biochem., 351, 44-49.
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 2.8.1.8 | expression in Escherichia coli | Saccharolobus solfataricus |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 2.8.1.8 | Saccharolobus solfataricus | - |
- |
- |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 2.8.1.8 | recombinant | Saccharolobus solfataricus |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 2.8.1.8 | protein N6-(octanoyl)lysine + sulfur + S-adenosyl-L-methionine | tetrapeptide substrate, containing an Nepsilon-octanoyl lysine residue, corresponding in sequence to the lipoyl binding domain of the E2 subunit of pyruvate dehydrogenase | Saccharolobus solfataricus | protein N6-(lipoyl)lysine + L-methionine + 5'-deoxyadenosyl radicals | - |
? |  |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 2.8.1.8 | 60 | - |
- |
Saccharolobus solfataricus |
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Release 2023.1 (January 2023)
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