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Literature summary for 2.8.1.8 extracted from

  • Cicchillo, R.M.; Iwig, D.F.; Jones, A.D.; Nesbitt, N.M.; Baleanu-Gogonea, C.; Souder, M.G.; Tu, L.; Booker, S.J.
    Lipoyl synthase requires two equivalents of S-adenosyl-L-methionine to synthesize one equivalent of lipoic acid (2004), Biochemistry, 43, 6378-6386.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
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Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
protein N6-(octanoyl)lysine + sulfur + S-adenosyl-L-methionine lipoyl-bearing subunit of the glycine cleavage system (H-protein) is a substrate for LipA. 5'-deoxyadenosyl radical acts directly on the octanoyl substrate. 2 equivalents of S-adenosyl-L-methionine are cleaved irreversibly in forming 1 equivalent of [lipoyl]H-protein and are consistent with a model in which two LipA proteins are required to synthesize one lipoyl group Escherichia coli protein N6-(lipoyl)lysine + L-methionine + 5'-deoxyadenosyl radicals
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ir

Synonyms

Synonyms Comment Organism
LipA
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Escherichia coli