Evidence map›Paper›PMID 24742683›Full record

ArticleThe Journal of biological chemistry2014

Structure and function of the catalytic domain of the dihydrolipoyl acetyltransferase component in Escherichia coli pyruvate dehydrogenase complex.

Junjie Wang, Natalia S Nemeria, Krishnamoorthy Chandrasekhar, Sowmini Kumaran, Palaniappa Arjunan, Shelley Reynolds, Guillermo Calero, Roman Brukh, Lazaros Kakalis, William Furey and 1 more

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
3.3field-weighted citation impact, top 9% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

27 citing papers in PubMed, 47 citations in OpenAlex.

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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

11 authors at 3 institutions in 1 country.

Junjie WangFrom the Department of Chemistry, Rutgers University, Newark, New Jersey 07102.
Natalia S NemeriaFrom the Department of Chemistry, Rutgers University, Newark, New Jersey 07102.
Krishnamoorthy Chandrasekharthe Department of Pharmacology and Chemical Biology, University of Pittsburgh School of Medicine, Pittsburgh, Pennsylvania 15261.
Sowmini KumaranFrom the Department of Chemistry, Rutgers University, Newark, New Jersey 07102.
Palaniappa Arjunanthe Department of Pharmacology and Chemical Biology, University of Pittsburgh School of Medicine, Pittsburgh, Pennsylvania 15261.
Shelley Reynoldsthe Department of Structural Biology, University of Pittsburgh School of Medicine, Pittsburgh, Pennsylvania 15261.
Guillermo Calerothe Department of Structural Biology, University of Pittsburgh School of Medicine, Pittsburgh, Pennsylvania 15261.
Roman BrukhFrom the Department of Chemistry, Rutgers University, Newark, New Jersey 07102.
Lazaros KakalisFrom the Department of Chemistry, Rutgers University, Newark, New Jersey 07102.
William Fureythe Department of Pharmacology and Chemical Biology, University of Pittsburgh School of Medicine, Pittsburgh, Pennsylvania 15261, the Veterans Affairs Medical Center, Pittsburgh, Pennsylvania 15240, and fureyw@pitt.edu.
Frank JordanFrom the Department of Chemistry, Rutgers University, Newark, New Jersey 07102, frjordan@rutgers.edu.
Rutgers, The State University of New Jersey · USUniversity of Pittsburgh · USVeterans Health Administration · US

Funding

STRUCTURE AND MECHANISM OF YEAST PYRUVATE DECARBOXYLASER01GM050380 · NIGMS · RUTGERS THE STATE UNIV OF NJ NEWARK · PI JORDAN, FRANK · 1993 to 2013
$3.0M
Pyruvate Dehydrogenase E1: Structure-Function StudiesR01GM061791 · NIGMS · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI FUREY, WILLIAM F · 2000 to 2012
$2.7M
NIGMS NIH HHS GM050380NIGMS NIH HHS GM061791NIGMS NIH HHS R01 GM050380NIGMS NIH HHS R01 GM061791
6 · The paper itself

Abstract

The Escherichia coli pyruvate dehydrogenase complex (PDHc) catalyzing conversion of pyruvate to acetyl-CoA comprises three components: E1p, E2p, and E3. The E2p is the five-domain core component, consisting of three tandem lipoyl domains (LDs), a peripheral subunit binding domain (PSBD), and a catalytic domain (E2pCD). Herein are reported the following. 1) The x-ray structure of E2pCD revealed both intra- and intertrimer interactions, similar to those reported for other E2pCDs. 2) Reconstitution of recombinant LD and E2pCD with E1p and E3p into PDHc could maintain at least 6.4% activity (NADH production), confirming the functional competence of the E2pCD and active center coupling among E1p, LD, E2pCD, and E3 even in the absence of PSBD and of a covalent link between domains within E2p. 3) Direct acetyl transfer between LD and coenzyme A catalyzed by E2pCD was observed with a rate constant of 199 s(-1), comparable with the rate of NADH production in the PDHc reaction. Hence, neither reductive acetylation of E2p nor acetyl transfer within E2p is rate-limiting. 4) An unprecedented finding is that although no interaction could be detected between E1p and E2pCD by itself, a domain-induced interaction was identified on E1p active centers upon assembly with E2p and C-terminally truncated E2p proteins by hydrogen/deuterium exchange mass spectrometry. The inclusion of each additional domain of E2p strengthened the interaction with E1p, and the interaction was strongest with intact E2p. E2p domain-induced changes at the E1p active site were also manifested by the appearance of a circular dichroism band characteristic of the canonical 4'-aminopyrimidine tautomer of bound thiamin diphosphate (AP).

Indexed as

AcetylationAcetyl Coenzyme AAmino Acid SequenceCarbohydrate MetabolismCatalytic DomainCrystallography, X-RayDeuterium Exchange MeasurementDihydrolipoyllysine-Residue AcetyltransferaseEnzyme ActivationEscherichia coliEscherichia coli ProteinsMolecular Sequence DataPlasmidsPyruvate Dehydrogenase ComplexPyruvic AcidAcetyl Coenzyme ADihydrolipoyllysine-Residue AcetyltransferaseEscherichia coli ProteinsPyruvate Dehydrogenase ComplexPyruvic AcidCarbohydrate MetabolismEnzyme CatalysisHD ExchangeMass Spectrometry (MS)Nuclear Magnetic Resonance (NMR)Pyruvate Dehydrogenase Complex (PDC)X-ray Crystallography

Identifiers

PMID24742683
PMCPMC4140881
OpenAlexW2020661893

What OpenQuestion holds

Textmetadata
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Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.