BRENDA - Enzyme Database

Mechanistic investigations of lipoic acid biosynthesis in Escherichia coli: both sulfur atoms in lipoic acid are contributed by the same lipoyl synthase polypeptide

Cicchillo, R.M.; Booker, S.J.; J. Am. Chem. Soc. 127, 2860-2861 (2005) View publication on PubMed

Data extracted from this reference:

Organism
EC Number
Organism
UniProt
Commentary
Textmining
2.8.1.8
Escherichia coli
-
-
-
Substrates and Products (Substrate)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
Substrate Product ID
2.8.1.8
protein N6-(octanoyl)lysine + sulfur + S-adenosyl-L-methionine
both sulfur atoms in lipoic acid are contributed by the same lipoyl synthase polypeptide
661945
Escherichia coli
protein N6-(lipoyl)lysine + 2 L-methionine + 2 5'-deoxyadenosyl radicals
-
-
-
?
Substrates and Products (Substrate) (protein specific)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ID
2.8.1.8
protein N6-(octanoyl)lysine + sulfur + S-adenosyl-L-methionine
both sulfur atoms in lipoic acid are contributed by the same lipoyl synthase polypeptide
661945
Escherichia coli
protein N6-(lipoyl)lysine + 2 L-methionine + 2 5'-deoxyadenosyl radicals
-
-
-
?