Structure and Function of the Catalytic Domain of the Dihydrolipoyl Acetyltransferase Component in Escherichia coli Pyruvate Dehydrogenase Complex*
Identifieur interne : 001143 ( Main/Exploration ); précédent : 001142; suivant : 001144Structure and Function of the Catalytic Domain of the Dihydrolipoyl Acetyltransferase Component in Escherichia coli Pyruvate Dehydrogenase Complex*
Auteurs : Junjie Wang ; Natalia S. Nemeria ; Krishnamoorthy Chandrasekhar ; Sowmini Kumaran ; Palaniappa Arjunan ; Shelley Reynolds ; Guillermo Calero ; Roman Brukh ; Lazaros Kakalis ; William Furey ; Frank JordanSource :
- The Journal of Biological Chemistry [ 0021-9258 ] ; 2014.
Descripteurs français
- KwdFr :
- Acide pyruvique (métabolisme), Activation enzymatique (physiologie), Acétyl coenzyme A (biosynthèse), Acétylation, Complexe du pyruvate déshydrogénase (), Complexe du pyruvate déshydrogénase (génétique), Complexe du pyruvate déshydrogénase (métabolisme), Cristallographie aux rayons X, Dihydrolipoyllysine-residue acetyltransferase (), Dihydrolipoyllysine-residue acetyltransferase (génétique), Dihydrolipoyllysine-residue acetyltransferase (métabolisme), Domaine catalytique, Données de séquences moléculaires, Escherichia coli (enzymologie), Escherichia coli (génétique), Mesure d'échange de deutérium, Métabolisme des glucides (physiologie), Plasmides, Protéines Escherichia coli (), Protéines Escherichia coli (génétique), Protéines Escherichia coli (métabolisme), Séquence d'acides aminés.
- MESH :
- biosynthèse : Acétyl coenzyme A.
- enzymologie : Escherichia coli.
- génétique : Complexe du pyruvate déshydrogénase, Dihydrolipoyllysine-residue acetyltransferase, Escherichia coli, Protéines Escherichia coli.
- métabolisme : Acide pyruvique, Complexe du pyruvate déshydrogénase, Dihydrolipoyllysine-residue acetyltransferase, Protéines Escherichia coli.
- physiologie : Activation enzymatique, Métabolisme des glucides.
- Acétylation, Complexe du pyruvate déshydrogénase, Cristallographie aux rayons X, Dihydrolipoyllysine-residue acetyltransferase, Domaine catalytique, Données de séquences moléculaires, Mesure d'échange de deutérium, Plasmides, Protéines Escherichia coli, Séquence d'acides aminés.
English descriptors
- KwdEn :
- Acetyl Coenzyme A (biosynthesis), Acetylation, Amino Acid Sequence, Carbohydrate Metabolism (physiology), Catalytic Domain, Crystallography, X-Ray, Deuterium Exchange Measurement, Dihydrolipoyllysine-Residue Acetyltransferase (chemistry), Dihydrolipoyllysine-Residue Acetyltransferase (genetics), Dihydrolipoyllysine-Residue Acetyltransferase (metabolism), Enzyme Activation (physiology), Escherichia coli (enzymology), Escherichia coli (genetics), Escherichia coli Proteins (chemistry), Escherichia coli Proteins (genetics), Escherichia coli Proteins (metabolism), Molecular Sequence Data, Plasmids, Pyruvate Dehydrogenase Complex (chemistry), Pyruvate Dehydrogenase Complex (genetics), Pyruvate Dehydrogenase Complex (metabolism), Pyruvic Acid (metabolism).
- MESH :
- chemical , biosynthesis : Acetyl Coenzyme A.
- chemical , chemistry : Dihydrolipoyllysine-Residue Acetyltransferase, Escherichia coli Proteins, Pyruvate Dehydrogenase Complex.
- chemical , genetics : Dihydrolipoyllysine-Residue Acetyltransferase, Escherichia coli Proteins, Pyruvate Dehydrogenase Complex.
- chemical , metabolism : Dihydrolipoyllysine-Residue Acetyltransferase, Escherichia coli Proteins, Pyruvate Dehydrogenase Complex, Pyruvic Acid.
- enzymology : Escherichia coli.
- genetics : Escherichia coli.
- physiology : Carbohydrate Metabolism, Enzyme Activation.
- Acetylation, Amino Acid Sequence, Catalytic Domain, Crystallography, X-Ray, Deuterium Exchange Measurement, Molecular Sequence Data, Plasmids.
Abstract
Url:
DOI: 10.1074/jbc.M113.544080
PubMed: 24742683
PubMed Central: 4140881
Affiliations:
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Le document en format XML
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Nemeria</name><affiliation><nlm:aff id="aff1"></nlm:aff></affiliation></author><author><name sortKey="Chandrasekhar, Krishnamoorthy" sort="Chandrasekhar, Krishnamoorthy" uniqKey="Chandrasekhar K" first="Krishnamoorthy" last="Chandrasekhar">Krishnamoorthy Chandrasekhar</name><affiliation><nlm:aff id="aff2"></nlm:aff></affiliation></author><author><name sortKey="Kumaran, Sowmini" sort="Kumaran, Sowmini" uniqKey="Kumaran S" first="Sowmini" last="Kumaran">Sowmini Kumaran</name><affiliation><nlm:aff id="aff1"></nlm:aff></affiliation></author><author><name sortKey="Arjunan, Palaniappa" sort="Arjunan, Palaniappa" uniqKey="Arjunan P" first="Palaniappa" last="Arjunan">Palaniappa Arjunan</name><affiliation><nlm:aff id="aff2"></nlm:aff></affiliation></author><author><name sortKey="Reynolds, Shelley" sort="Reynolds, Shelley" uniqKey="Reynolds S" first="Shelley" last="Reynolds">Shelley Reynolds</name><affiliation><nlm:aff id="aff4"></nlm:aff></affiliation></author><author><name sortKey="Calero, Guillermo" sort="Calero, Guillermo" uniqKey="Calero G" first="Guillermo" last="Calero">Guillermo Calero</name><affiliation><nlm:aff id="aff4"></nlm:aff></affiliation></author><author><name sortKey="Brukh, Roman" sort="Brukh, Roman" uniqKey="Brukh R" first="Roman" last="Brukh">Roman Brukh</name><affiliation><nlm:aff id="aff1"></nlm:aff></affiliation></author><author><name sortKey="Kakalis, Lazaros" sort="Kakalis, Lazaros" uniqKey="Kakalis L" first="Lazaros" last="Kakalis">Lazaros Kakalis</name><affiliation><nlm:aff id="aff1"></nlm:aff></affiliation></author><author><name sortKey="Furey, William" sort="Furey, William" uniqKey="Furey W" first="William" last="Furey">William Furey</name><affiliation><nlm:aff id="aff2"></nlm:aff></affiliation><affiliation><nlm:aff id="aff3"></nlm:aff></affiliation></author><author><name sortKey="Jordan, Frank" sort="Jordan, Frank" uniqKey="Jordan F" first="Frank" last="Jordan">Frank Jordan</name><affiliation><nlm:aff id="aff1"></nlm:aff></affiliation></author></analytic><series><title level="j">The Journal of Biological Chemistry</title><idno type="ISSN">0021-9258</idno><idno type="eISSN">1083-351X</idno><imprint><date when="2014">2014</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Acetyl Coenzyme A (biosynthesis)</term><term>Acetylation</term><term>Amino Acid Sequence</term><term>Carbohydrate Metabolism (physiology)</term><term>Catalytic Domain</term><term>Crystallography, X-Ray</term><term>Deuterium Exchange Measurement</term><term>Dihydrolipoyllysine-Residue Acetyltransferase (chemistry)</term><term>Dihydrolipoyllysine-Residue Acetyltransferase (genetics)</term><term>Dihydrolipoyllysine-Residue Acetyltransferase (metabolism)</term><term>Enzyme Activation (physiology)</term><term>Escherichia coli (enzymology)</term><term>Escherichia coli (genetics)</term><term>Escherichia coli Proteins (chemistry)</term><term>Escherichia coli Proteins (genetics)</term><term>Escherichia coli Proteins (metabolism)</term><term>Molecular Sequence Data</term><term>Plasmids</term><term>Pyruvate Dehydrogenase Complex (chemistry)</term><term>Pyruvate Dehydrogenase Complex (genetics)</term><term>Pyruvate Dehydrogenase Complex (metabolism)</term><term>Pyruvic Acid (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Acide pyruvique (métabolisme)</term><term>Activation enzymatique (physiologie)</term><term>Acétyl coenzyme A (biosynthèse)</term><term>Acétylation</term><term>Complexe du pyruvate déshydrogénase ()</term><term>Complexe du pyruvate déshydrogénase (génétique)</term><term>Complexe du pyruvate déshydrogénase (métabolisme)</term><term>Cristallographie aux rayons X</term><term>Dihydrolipoyllysine-residue acetyltransferase ()</term><term>Dihydrolipoyllysine-residue acetyltransferase (génétique)</term><term>Dihydrolipoyllysine-residue acetyltransferase (métabolisme)</term><term>Domaine catalytique</term><term>Données de séquences moléculaires</term><term>Escherichia coli (enzymologie)</term><term>Escherichia coli (génétique)</term><term>Mesure d'échange de deutérium</term><term>Métabolisme des glucides (physiologie)</term><term>Plasmides</term><term>Protéines Escherichia coli ()</term><term>Protéines Escherichia coli (génétique)</term><term>Protéines Escherichia coli (métabolisme)</term><term>Séquence d'acides aminés</term></keywords><keywords scheme="MESH" type="chemical" qualifier="biosynthesis" xml:lang="en"><term>Acetyl Coenzyme A</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Dihydrolipoyllysine-Residue Acetyltransferase</term><term>Escherichia coli Proteins</term><term>Pyruvate Dehydrogenase Complex</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Dihydrolipoyllysine-Residue Acetyltransferase</term><term>Escherichia coli Proteins</term><term>Pyruvate Dehydrogenase Complex</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Dihydrolipoyllysine-Residue Acetyltransferase</term><term>Escherichia coli Proteins</term><term>Pyruvate Dehydrogenase Complex</term><term>Pyruvic Acid</term></keywords><keywords scheme="MESH" qualifier="biosynthèse" xml:lang="fr"><term>Acétyl coenzyme A</term></keywords><keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Escherichia coli</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Escherichia coli</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Escherichia coli</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Complexe du pyruvate déshydrogénase</term><term>Dihydrolipoyllysine-residue acetyltransferase</term><term>Escherichia coli</term><term>Protéines Escherichia coli</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Acide pyruvique</term><term>Complexe du pyruvate déshydrogénase</term><term>Dihydrolipoyllysine-residue acetyltransferase</term><term>Protéines Escherichia coli</term></keywords><keywords scheme="MESH" qualifier="physiologie" xml:lang="fr"><term>Activation enzymatique</term><term>Métabolisme des glucides</term></keywords><keywords scheme="MESH" qualifier="physiology" xml:lang="en"><term>Carbohydrate Metabolism</term><term>Enzyme Activation</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Acetylation</term><term>Amino Acid Sequence</term><term>Catalytic Domain</term><term>Crystallography, X-Ray</term><term>Deuterium Exchange Measurement</term><term>Molecular Sequence Data</term><term>Plasmids</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Acétylation</term><term>Complexe du pyruvate déshydrogénase</term><term>Cristallographie aux rayons X</term><term>Dihydrolipoyllysine-residue acetyltransferase</term><term>Domaine catalytique</term><term>Données de séquences moléculaires</term><term>Mesure d'échange de deutérium</term><term>Plasmides</term><term>Protéines Escherichia coli</term><term>Séquence d'acides aminés</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><p><bold>Background:</bold> The <italic>E. coli</italic> pyruvate dehydrogenase complex catalyzes conversion of pyruvate to acetyl-CoA and comprises E1p, E2p, and E3 components.</p><p><bold>Results:</bold> The structure of the E2 core domain was solved and shown to efficiently catalyze acetyl transfer between domains.</p><p><bold>Conclusion:</bold> Mass spectrometry revealed hitherto unrecognized domain-induced interactions between E1 and E2 core domain.</p><p><bold>Significance:</bold> A multifaceted approach is required to understand communication between intact multidomain components.</p></div></front></TEI><affiliations><list></list><tree><noCountry><name sortKey="Arjunan, Palaniappa" sort="Arjunan, Palaniappa" uniqKey="Arjunan P" first="Palaniappa" last="Arjunan">Palaniappa Arjunan</name><name sortKey="Brukh, Roman" sort="Brukh, Roman" uniqKey="Brukh R" first="Roman" last="Brukh">Roman Brukh</name><name sortKey="Calero, Guillermo" sort="Calero, Guillermo" uniqKey="Calero G" first="Guillermo" last="Calero">Guillermo Calero</name><name sortKey="Chandrasekhar, Krishnamoorthy" sort="Chandrasekhar, Krishnamoorthy" uniqKey="Chandrasekhar K" first="Krishnamoorthy" last="Chandrasekhar">Krishnamoorthy Chandrasekhar</name><name sortKey="Furey, William" sort="Furey, William" uniqKey="Furey W" first="William" last="Furey">William Furey</name><name sortKey="Jordan, Frank" sort="Jordan, Frank" uniqKey="Jordan F" first="Frank" last="Jordan">Frank Jordan</name><name sortKey="Kakalis, Lazaros" sort="Kakalis, Lazaros" uniqKey="Kakalis L" first="Lazaros" last="Kakalis">Lazaros Kakalis</name><name sortKey="Kumaran, Sowmini" sort="Kumaran, Sowmini" uniqKey="Kumaran S" first="Sowmini" last="Kumaran">Sowmini Kumaran</name><name sortKey="Nemeria, Natalia S" sort="Nemeria, Natalia S" uniqKey="Nemeria N" first="Natalia S." last="Nemeria">Natalia S. Nemeria</name><name sortKey="Reynolds, Shelley" sort="Reynolds, Shelley" uniqKey="Reynolds S" first="Shelley" last="Reynolds">Shelley Reynolds</name><name sortKey="Wang, Junjie" sort="Wang, Junjie" uniqKey="Wang J" first="Junjie" last="Wang">Junjie Wang</name></noCountry></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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