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Literature summary 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

EC Number Activating Compound Comment Organism Structure
2.3.1.181 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

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.3.1.200 expressed in Escherichia coli strain QC143 Bacillus subtilis
2.3.1.204 expressed in Escherichia coli Bacillus subtilis

Protein Variants

EC Number Protein Variants Comment Organism
2.3.1.200 C150A the mutation results in loss of enzymatic activity and the inability to form an acyl-enzyme intermediate Bacillus subtilis
2.3.1.200 C150S the mutation results in loss of enzymatic activity and the inability to form an acyl-enzyme intermediate Bacillus subtilis

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.3.1.204 31420
-
calculated from amino acid sequence Bacillus subtilis

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.3.1.181 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]
-
?
2.3.1.181 an octanoyl-[acyl-carrier protein] + glycine cleavage system protein Bacillus subtilis
-
glycine cleavage system protein-N6-(octanoyl)lysine + an [acyl-carrier protein]
-
?
2.3.1.204 [glycine cleavage system H]-N6-octanoyl-L-lysine + a [lipoyl-carrier protein] Bacillus subtilis
-
glycine cleavage system H + a [lipoyl-carrier protein]-N6-octanoyl-L-lysine
-
r
2.3.1.204 [glycine cleavage system H]-N6-octanoyl-L-lysine + a [lipoyl-carrier protein] Bacillus subtilis 168
-
glycine cleavage system H + a [lipoyl-carrier protein]-N6-octanoyl-L-lysine
-
r

Organism

EC Number Organism UniProt Comment Textmining
2.3.1.181 Bacillus subtilis
-
gene lipM
-
2.3.1.200 Bacillus subtilis
-
-
-
2.3.1.204 Bacillus subtilis P39648
-
-
2.3.1.204 Bacillus subtilis 168 P39648
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.3.1.200 Ni-NTA resin column chromatography Bacillus subtilis
2.3.1.204
-
Bacillus subtilis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.3.1.181 an octanoyl-[acyl-carrier protein] + a protein
-
Bacillus subtilis a protein N6-(octanoyl)lysine + an [acyl-carrier protein]
-
?
2.3.1.181 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]
-
?
2.3.1.181 an octanoyl-[acyl-carrier protein] + glycine cleavage system protein
-
Bacillus subtilis glycine cleavage system protein-N6-(octanoyl)lysine + an [acyl-carrier protein]
-
?
2.3.1.200 octanoyl-glycine cleavage system H protein + pyruvate dehydrogenase subunit E2
-
Bacillus subtilis glycine cleavage system H protein + pyruvate dehydrogenase subunit E2-octanoyl
-
r
2.3.1.204 [glycine cleavage system H]-N6-octanoyl-L-lysine + a [lipoyl-carrier protein]
-
Bacillus subtilis glycine cleavage system H + a [lipoyl-carrier protein]-N6-octanoyl-L-lysine
-
r
2.3.1.204 [glycine cleavage system H]-N6-octanoyl-L-lysine + a [lipoyl-carrier protein]
-
Bacillus subtilis 168 glycine cleavage system H + a [lipoyl-carrier protein]-N6-octanoyl-L-lysine
-
r

Synonyms

EC Number Synonyms Comment Organism
2.3.1.181 ACP: GcvH octanoyltransferase
-
Bacillus subtilis
2.3.1.181 LipM
-
Bacillus subtilis
2.3.1.200 GcvH:E2 amidotransferase
-
Bacillus subtilis
2.3.1.200 GcvH:[lipoyl domain] amidotransferase
-
Bacillus subtilis
2.3.1.200 LIPL
-
Bacillus subtilis
2.3.1.200 ywfL
-
Bacillus subtilis
2.3.1.204 LIPL
-
Bacillus subtilis
2.3.1.204 octanoyl-[GcvH]:E2 amidotransferase
-
Bacillus subtilis

General Information

EC Number General Information Comment Organism
2.3.1.181 evolution LipM and LipL phylogenetic tree analysis, overview Bacillus subtilis
2.3.1.181 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
2.3.1.200 metabolism the enzyme is essential for lipoic acid synthesis, but has no detectable octanoyltransferase or ligase activity either in vitro or in vivo. The enzyme is required for PdhC modification Bacillus subtilis