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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Vydané v:	The Journal of biological chemistry Ročník 289; číslo 24; s. 16615
Hlavní autori:	Patel, Mulchand S, Nemeria, Natalia S, Furey, William, Jordan, Frank
Médium:	Journal Article
Jazyk:	English
Vydavateľské údaje:	United States 13.06.2014
Predmet:	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
On-line prístup:	Zistit podrobnosti o prístupe
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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.
AbstractList	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.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. 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.
Author	Jordan, Frank Nemeria, Natalia S Patel, Mulchand S Furey, William
Author_xml	– sequence: 1 givenname: Mulchand S surname: Patel fullname: Patel, Mulchand S email: mspatel@buffalo.edu organization: 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 – sequence: 2 givenname: Natalia S surname: Nemeria fullname: Nemeria, Natalia S organization: the Department of Chemistry, Rutgers, the State University of New Jersey, Newark, New Jersey 07102 – sequence: 3 givenname: William surname: Furey fullname: Furey, William organization: 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 – sequence: 4 givenname: Frank surname: Jordan fullname: Jordan, Frank email: frjordan@rutgers.edu organization: the Department of Chemistry, Rutgers, the State University of New Jersey, Newark, New Jersey 07102, frjordan@rutgers.edu
BackLink	https://www.ncbi.nlm.nih.gov/pubmed/24798336$$D View this record in MEDLINE/PubMed
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Keywords	Pyruvate Dehydrogenase Complex (PDC) Pyruvate Dehydrogenase Kinase (PDC Kinase) Covalent Regulation Enzyme Catalysis Protein-Protein Interaction
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SubjectTerms	Amino Acid Sequence Animals Catalytic Domain Escherichia coli - enzymology Humans Molecular Sequence Data Protein Binding Pyruvate Dehydrogenase Complex - chemistry Pyruvate Dehydrogenase Complex - metabolism
Title	The pyruvate dehydrogenase complexes: structure-based function and regulation
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