Lipoyl synthase requires two equivalents of S-adenosyl-L-methionine to synthesize one equivalent of lipoic acid.

@article{Cicchillo2004LipoylSR,
  title={Lipoyl synthase requires two equivalents of S-adenosyl-L-methionine to synthesize one equivalent of lipoic acid.},
  author={Robert M. Cicchillo and David F Iwig and A. Daniel Jones and Natasha M Nesbitt and Camelia Baleanu-Gogonea and Matthew G Souder and Loretta Tu and Squire J Booker},
  journal={Biochemistry},
  year={2004},
  volume={43 21},
  pages={6378-86}
}
Lipoyl synthase (LipA) catalyzes the formation of the lipoyl cofactor, which is employed by several multienzyme complexes for the oxidative decarboxylation of various alpha-keto acids, as well as the cleavage of glycine into CO(2) and NH(3), with concomitant transfer of its alpha-carbon to tetrahydrofolate, generating N(5),N(10)-methylenetetrahydrofolate. In each case, the lipoyl cofactor is tethered covalently in an amide linkage to a conserved lysine residue located on a designated lipoyl… CONTINUE READING
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