Sequence around the active center cystine of lipoamide dehydrogenase from pig heart, comparison with the E. coli enzyme.

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.