Sequence around the Active Center Cystine of Lipoamide Dehydrogenase from Pig Heart, Comparison with the E. coli Enzyme

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Abstract
Catalysis by lipoamide dehydrogenase involves the concerted action of the flavin and a cystine residue. Peptides containing this cystine residue have been previously isolated from E. coli and now from pig heart. The sequences of amino acid residues reveal a high degree of homology indicating a strict conservation of the region around the active site cystine during the long evolutionary period between these two species. The peptide sequences suggest a likely conformation of the polypeptide chain in the region of the flavin as well as the forces involved in substrate and flavin binding.

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