The pyruvate dehydrogenase complexes: Structure-based function and regulation

Mulchand S. Patel, Natalia S. Nemeria, William Furey, Frank Jordan

Research output: Contribution to journalShort surveypeer-review

182 Scopus citations


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.

Original languageEnglish (US)
Pages (from-to)16615-16623
Number of pages9
JournalJournal of Biological Chemistry
Issue number24
StatePublished - Jun 13 2014

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Fingerprint Dive into the research topics of 'The pyruvate dehydrogenase complexes: Structure-based function and regulation'. Together they form a unique fingerprint.

Cite this