Lipoyl dehydrogenase functions

Chen, G., Wang, L., Liu, S., Chuang, C. and Roche, T.E. (1996) Activated function of the pyruvate dehydrogenase phosphatase through Ca2+-facilitated binding to the inner lipoyl domain of the dihydrolipoyl acetyltransferase. Journal of Biological Chemistry 271,28064-28070. 

Recent studies with bovine heart mitochondrial matrix preparations indicate that one of the major products of this pathway is octanoyl-ACP and these newly synthesized octanoyl moieties can be translocated directly to the lipoylation site of the glycine cleavage apo-H protein (S. Smith, 2007). Octanoylated mitochondrial proteins are the substrates for the enzyme lipoic acid synthase, which inserts two sulfur atoms at the C6 and C8 positions of the octanoyl moiety. These results are consistent with the hypothesis that one of the major roles of the mitochondrial FAS pathway in all eukaryotes is to ensure that an adequate supply of lipoyl moieties is always available to service the glycine cleavage enzyme and the alpha-ketoacid dehydrogenases that are essential to mitochondrial function. 

Cronan JE Jr (2002) Interchangeable enzyme modules. Functional replacement of the essential linker of the biotinylated subunit of acetyl-CoA carboxylase with a Unker from the lipoylated subunit of pyruvate dehydrogenase. Journal of Biological Chemistry 22520-22527. 

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