Primary structure around the lipoate-attachment site on the E2 component of bovine heart pyruvate dehydrogenase complex

Biochem J. 1987 Aug 1;245(3):919-22. doi: 10.1042/bj2450919.


Bovine heart pyruvate dehydrogenase complex was acetylated by using [3-14C]pyruvate in the presence of N-ethylmaleimide, with approx. 1 mol of acetyl groups being incorporated per mol of E2 polypeptide. After peptic digestion, lipoate-containing peptides were purified by high-voltage electrophoresis and ion-exchange and reverse-phase h.p.l.c. The amino acid sequence around the lipoic acid-attachment site of E2 was determined by automated Edman degradation. Acetylation of a lipoate cofactor bound to a lysine residue was verified by fast-atom-bombardment m.s.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Acetylation
  • Amino Acid Sequence
  • Animals
  • Cattle
  • Ethylmaleimide / pharmacology
  • Mass Spectrometry
  • Molecular Sequence Data
  • Myocardium / enzymology*
  • Peptide Fragments / analysis
  • Pyruvate Dehydrogenase (Lipoamide)
  • Pyruvate Dehydrogenase Complex* / metabolism
  • Pyruvates / metabolism
  • Pyruvic Acid
  • Thioctic Acid / analysis*


  • Peptide Fragments
  • Pyruvate Dehydrogenase Complex
  • Pyruvates
  • Thioctic Acid
  • Pyruvic Acid
  • Pyruvate Dehydrogenase (Lipoamide)
  • Ethylmaleimide