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

The pyruvate dehydrogenase complexes: structure-based function and regulation.

Author information

1
From the Department of Biochemistry, School of Medicine and Biomedical Sciences, University at Buffalo, the State University of New York, Buffalo, New York 14214, mspatel@buffalo.edu.
2
the Department of Chemistry, Rutgers, the State University of New Jersey, Newark, New Jersey 07102.
3
the Department of Pharmacology and Chemical Biology, University of Pittsburgh School of Medicine, Pittsburgh, Pennsylvania 15261, and the Veterans Affairs Medical Center, Pittsburgh, Pennsylvania 15240.
4
the Department of Chemistry, Rutgers, the State University of New Jersey, Newark, New Jersey 07102, frjordan@rutgers.edu.

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)

PMID:
24798336
PMCID:
PMC4059105
DOI:
10.1074/jbc.R114.563148
[Indexed for MEDLINE]
Free PMC Article

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