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Literature summary for 2.8.1.8 extracted from

  • Bryant, P.; Kriek, M.; Wood, R.J.; Roach, P.L.
    The activity of a thermostable lipoyl synthase from Sulfolobus solfataricus with a synthetic octanoyl substrate (2006), Anal. Biochem., 351, 44-49.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Saccharolobus solfataricus

Organism

Organism UniProt Comment Textmining
Saccharolobus solfataricus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant Saccharolobus solfataricus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
60
-
-
Saccharolobus solfataricus