Antibodies against an inter-domain segment of polypeptide chain inhibit active-site coupling in the pyruvate dehydrogenase multienzyme complex

FEBS Lett. 1989 Jul 3;250(2):336-40. doi: 10.1016/0014-5793(89)80750-1.

Abstract

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.

Publication types

  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Antibodies / immunology*
  • Binding Sites
  • Binding Sites, Antibody
  • Cross-Linking Reagents
  • Peptides / immunology*
  • Pyruvate Dehydrogenase Complex / antagonists & inhibitors*

Substances

  • Antibodies
  • Cross-Linking Reagents
  • Peptides
  • Pyruvate Dehydrogenase Complex