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Literature summary for 2.3.1.181 extracted from

  • vanden Boom, T.J.; Reed, K.E.; Cronan, J.E.
    Lipoic acid metabolism in Escherichia coli: isolation of null mutants defective in lipoic acid biosynthesis, molecular cloning and characterization of the E. coli lip locus, and identification of the lipoylated protein of the glycine cleavage system (1991), J. Bacteriol., 173, 6411-6420.
    View publication on PubMedView publication on EuropePMC

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
octanoyl-[acyl-carrier protein] + protein Escherichia coli first committed step in the biosynthesis of lipoyl cofactor. The lipoyl cofactor is essential for the function of glycine cleavage system (H protein) protein N6-(octanoyl)lysine + acyl-carrier protein
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Organism

Organism UniProt Comment Textmining
Escherichia coli
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
octanoyl-[acyl-carrier protein] + protein first committed step in the biosynthesis of lipoyl cofactor. The lipoyl cofactor is essential for the function of glycine cleavage system (H protein) Escherichia coli protein N6-(octanoyl)lysine + acyl-carrier protein
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?