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Literature summary extracted from

  • Hassan, B.H.; Cronan, J.E.
    Protein-protein interactions in assembly of lipoic acid on the 2-oxoacid dehydrogenases of aerobic metabolism (2011), J. Biol. Chem., 286, 8263-8276.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.3.1.181
-
 Escherichia coli

Protein Variants

EC Number Protein Variants Comment Organism
2.3.1.181 C169S the hydrolyzed C169S mutant protein shows higher methyl octanoate levels than those of the wild type protein preparations Escherichia coli

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.3.1.181 26220
-
 MALDI mass spectrometry Escherichia coli

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.3.1.181 octanoyl-[acyl-carrier protein] + a protein Escherichia coli LipB (EC 2.3.11.181) is responsible for octanoylation of the E2 components of 2-oxoacid dehydrogenases to provide the substrates of LipA (EC 2.7.7.63), an S-adenosyl-L-methionine radical enzyme that inserts two sulfur atoms into the octanoyl moiety to give the active lipoylated dehydrogenase complexes. LipB accumulates an octanoyl-enzyme intermediate with no sign of a lipoyl-enzyme intermediate a protein N6-(octanoyl)lysine + an [acyl-carrier protein]
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.3.1.181 Escherichia coli
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.3.1.181 isolation and properties of a very stable complex between LipB and acyl cyrrier protein Escherichia coli

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.3.1.181 octanoyl-[acyl-carrier protein] + a protein LipB (EC 2.3.11.181) is responsible for octanoylation of the E2 components of 2-oxoacid dehydrogenases to provide the substrates of LipA (EC 2.7.7.63), an S-adenosyl-L-methionine radical enzyme that inserts two sulfur atoms into the octanoyl moiety to give the active lipoylated dehydrogenase complexes. LipB accumulates an octanoyl-enzyme intermediate with no sign of a lipoyl-enzyme intermediate Escherichia coli a protein N6-(octanoyl)lysine + an [acyl-carrier protein]
-
 ?
2.3.1.181 octanoyl-[acyl-carrier protein] + a protein LipB (EC 2.3.11.181) is responsible for octanoylation of the E2 components of 2-oxoacid dehydrogenases to provide the substrates of LipA (EC 2.7.7.63), an S-adenosyl-L-methionine radical enzyme that inserts two sulfur atoms into the octanoyl moiety to give the active lipoylated dehydrogenase complexes. The binding sites for LipB reside both in the lipoyl domain and catalytic core sequences Escherichia coli a protein N6-(octanoyl)lysine + an [acyl-carrier protein]
-
 ?

Synonyms

EC Number Synonyms Comment Organism
2.3.1.181 LipB
-
 Escherichia coli

General Information

EC Number General Information Comment Organism
2.3.1.181 physiological function LipB (EC 2.3.11.181) is responsible for octanoylation of the E2 components of 2-oxoacid dehydrogenases to provide the substrates of LipA (EC 2.7.7.63), an S-adenosyl-L-methionine radical enzyme that inserts two sulfur atoms into the octanoyl moiety to give the active lipoylated dehydrogenase complexes Escherichia coli