The Pyruvate Dehydrogenase Complexes: Structure-Based Function and Regulation

J Biol Chem. 2014 Jun 13;289(24):16615-23. doi: 10.1074/jbc.R114.563148. Epub 2014 May 5.

Abstract

The pyruvate dehydrogenase complexes (PDCs) from all known living organisms comprise three principal catalytic components for their mission: E1 and E2 generate acetyl-coenzyme A, whereas the FAD/NAD(+)-dependent E3 performs redox recycling. Here we compare bacterial (Escherichia coli) and human PDCs, as they represent the two major classes of the superfamily of 2-oxo acid dehydrogenase complexes with different assembly of, and interactions among components. The human PDC is subject to inactivation at E1 by serine phosphorylation by four kinases, an inactivation reversed by the action of two phosphatases. Progress in our understanding of these complexes important in metabolism is reviewed.

Keywords: Covalent Regulation; Enzyme Catalysis; Protein-Protein Interaction; Pyruvate Dehydrogenase Complex (PDC); Pyruvate Dehydrogenase Kinase (PDC Kinase).

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, U.S. Gov't, Non-P.H.S.
  • Review

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Catalytic Domain*
  • Escherichia coli / enzymology
  • Humans
  • Molecular Sequence Data
  • Protein Binding
  • Pyruvate Dehydrogenase Complex / chemistry*
  • Pyruvate Dehydrogenase Complex / metabolism

Substances

  • Pyruvate Dehydrogenase Complex