Information on EC - lipoyl(octanoyl) transferase

for references in articles please use BRENDA:EC2.3.1.181
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IUBMB Comments
This is the first committed step in the biosynthesis of lipoyl cofactor. Lipoylation is essential for the function of several key enzymes involved in oxidative metabolism, as it converts apoprotein into the biologically active holoprotein. Examples of such lipoylated proteins include pyruvate dehydrogenase (E2 domain), 2-oxoglutarate dehydrogenase (E2 domain), the branched-chain 2-oxoacid dehydrogenases and the glycine cleavage system (H protein) [2,3]. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the true substrate . The other enzyme involved in the biosynthesis of lipoyl cofactor is EC, lipoyl synthase. An alternative lipoylation pathway involves EC, lipoate---protein ligase, which can lipoylate apoproteins using exogenous lipoic acid (or its analogues).
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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
ACP: GcvH octanoyltransferase, ACP:protein-N-octanoyltransferase, At1g47578, At4G31050, AtLIP2p2, bLT, LIP2, LIP2P1, Lip2p2, LIP3, more
an octanoyl-[acyl-carrier protein] + a protein = a protein N6-(octanoyl)lysine + an [acyl-carrier protein]
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