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Literature summary for 2.3.1.181 extracted from

  • Hermes, F.A.; Cronan, J.E.
    Scavenging of cytosolic octanoic acid by mutant LplA lipoate ligases allows growth of Escherichia coli strains lacking the LipB octanoyltransferase of lipoic acid synthesis (2009), J. Bacteriol., 191, 6796-6803.
    View publication on PubMedView publication on EuropePMC

Protein Variants

Protein Variants Comment Organism
additional information Escherichia coli wild type strain and several spontaneous LipB knockout strains are used Escherichia coli

Localization

Localization Comment Organism GeneOntology No. Textmining

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
wild type and several LipB knockout strains
-

Synonyms

Synonyms Comment Organism
LipB octanoyltransferase
-
Escherichia coli
octanoyl-[acyl carrier protein {ACP}]:protein N-octanoyltransferase
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Escherichia coli

General Information

General Information Comment Organism
metabolism The LipB octanoyltransferase catalyzes the first step of lipoic acid synthesis in Escherichia coli, transfer of the octanoyl moiety from octanoyl-acyl carrier protein to the lipoyl domains of the E2 subunits of the 2-oxoacid dehydrogenases of aerobic metabolism. Escherichia coli