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Literature summary for 2.3.1.181 extracted from

  • Christensen, Q.H.; Martin, N.; Mansilla, M.C.; de Mendoza, D.; Cronan, J.E.
    A novel amidotransferase required for lipoic acid cofactor assembly in Bacillus subtilis (2011), Mol. Microbiol., 80, 350-363.
    View publication on PubMedView publication on EuropePMC

Activating Compound

Activating Compound Comment Organism Structure
LipL is essential for lipoic acid synthesis, but has no detectable octanoyltransferase or ligase activity either in vitro or in vivo. It catalyses the amidotransfer (transamidation) of the octanoyl moiety from octanoyl-GcvH to the E2 subunit of pyruvate dehydrogenase Bacillus subtilis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
an octanoyl-[acyl-carrier protein] + a protein Bacillus subtilis LipM specifically modifies the glycine cleavage system protein, GcvH a protein N6-(octanoyl)lysine + an [acyl-carrier protein]
-
?
an octanoyl-[acyl-carrier protein] + glycine cleavage system protein Bacillus subtilis
-
glycine cleavage system protein-N6-(octanoyl)lysine + an [acyl-carrier protein]
-
?

Organism

Organism UniProt Comment Textmining
Bacillus subtilis
-
gene lipM
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
an octanoyl-[acyl-carrier protein] + a protein
-
Bacillus subtilis a protein N6-(octanoyl)lysine + an [acyl-carrier protein]
-
?
an octanoyl-[acyl-carrier protein] + a protein LipM specifically modifies the glycine cleavage system protein, GcvH Bacillus subtilis a protein N6-(octanoyl)lysine + an [acyl-carrier protein]
-
?
an octanoyl-[acyl-carrier protein] + glycine cleavage system protein
-
Bacillus subtilis glycine cleavage system protein-N6-(octanoyl)lysine + an [acyl-carrier protein]
-
?

Synonyms

Synonyms Comment Organism
ACP: GcvH octanoyltransferase
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Bacillus subtilis
LipM
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Bacillus subtilis

General Information

General Information Comment Organism
evolution LipM and LipL phylogenetic tree analysis, overview Bacillus subtilis
physiological function LipM specifically modifies the glycine cleavage system protein, GcvH. GcvH is required in Bacillus subtilis lipoic acid biosynthesis, overview. LipM is an octanoyltransferase required for lipoic acid synthesis, and LipL is essential for lipoic acid synthesis, but has no detectable octanoyltransferase or ligase activity either in vitro or in vivo, it catalyses the amidotransfer (transamidation) of the octanoyl moiety from octanoyl-glycine cleavage system protein to the E2 subunit of pyruvate dehydrogenase Bacillus subtilis