The pyruvate dehydrogenase complexes: structure-based function and regulation

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...

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Veröffentlicht in:The Journal of biological chemistry Jg. 289; H. 24; S. 16615
Hauptverfasser: Patel, Mulchand S, Nemeria, Natalia S, Furey, William, Jordan, Frank
Format: Journal Article
Sprache:Englisch
Veröffentlicht: United States 13.06.2014
Schlagworte:
Amino Acid Sequence
Animals
Catalytic Domain
Escherichia coli - enzymology
Humans
Molecular Sequence Data
Protein Binding
Pyruvate Dehydrogenase Complex - chemistry
Pyruvate Dehydrogenase Complex - metabolism
Pyruvate Dehydrogenase Complex (PDC)
Pyruvate Dehydrogenase Kinase (PDC Kinase)
Covalent Regulation
Enzyme Catalysis
Protein-Protein Interaction
ISSN:1083-351X, 1083-351X
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Zusammenfassung: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.
Bibliographie:ObjectType-Article-1
SourceType-Scholarly Journals-1
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ISSN:1083-351X
1083-351X
DOI:10.1074/jbc.R114.563148