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Antibodies against an inter‐domain segment of polypeptide chain inhibit active‐site coupling in the pyruvate dehydrogenase multienzyme complex
Author(s) -
Radford Sheena E.,
Perham Richard N.,
Ullrich Stephen J.,
Appella Ettore
Publication year - 1989
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(89)80750-1
Subject(s) - immunogen , pyruvate dehydrogenase complex , dihydrolipoamide dehydrogenase , biochemistry , peptide , dihydrolipoyl transacetylase , enzyme , peptide sequence , chemistry , branched chain alpha keto acid dehydrogenase complex , escherichia coli , dehydrogenase , active site , biology , stereochemistry , antibody , pyruvate dehydrogenase phosphatase , monoclonal antibody , gene , immunology
A synthetic peptide, AAPAAAPAKQEAAAPAPAAKAEAPAAAPAAKA, proved to be an efficient and specific immunogen in rabbits. The amino acid sequence of the peptide is identical to that of the inter‐domain region (PEP3) linking the innermost of the three lipoyl domains to the dihydrolipoamide dehydrogenase‐binding domain in the dihydrolipoamide acetyltransferase chain of the pyruvate dehydrogenase complex of Escherichia coli . Fab fragments from anti‐PEP3 antibodies selectively inhibited active‐site coupling in the complex without affecting the individual activities of the three component enzymes, highlighting the role of the inter‐domain regions as flexible linkers in catalysis.