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Literature summary for 2.3.1.181 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
Search for more literature for 2.3.1.181

Cloned(Commentary)

Cloned (Comment) Organism
-
 Escherichia coli

Protein Variants

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

Molecular Weight [Da]

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

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
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]
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 ?

Organism

Organism UniProt Comment Textmining
Escherichia coli
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-
-

Purification (Commentary)

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

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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]
-
 ?
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]
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 ?

Synonyms

Synonyms Comment Organism
LipB
-
 Escherichia coli

General Information

General Information Comment Organism
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