Evidence map›Paper›PMID 29531083›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2018

Archaeal acetoacetyl-CoA thiolase/HMG-CoA synthase complex channels the intermediate via a fused CoA-binding site.

Bastian Vögeli, Sylvain Engilberge, Eric Girard, François Riobé, Olivier Maury, Tobias J Erb, Seigo Shima, Tristan Wagner

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
2.2field-weighted citation impact, top 11% 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

24 citing papers in PubMed, 68 citations in OpenAlex.

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  13. Intrinsic Ability of the β-Oxidation Pathway To Produce Bioactive Styrylpyrones.Angewandte Chemie (International ed. in English) · 2022
    Article
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  16. Review
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  20. Biochemistry · 2019
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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

8 authors at 3 institutions in 2 countries.

Bastian VögeliBiochemistry and Synthetic Metabolism, Max Planck Institute for Terrestrial Microbiology, 35043 Marburg, Germany.
Sylvain EngilbergeInstitut de Biologie Structurale (IBS), University of Grenoble Alpes (UGA), Commissariat à l'énergie atomique et aux énergies alternatives (CEA), Centre National de la Recherche Scientifique (CNRS), F-38000 Grenoble, France.
Eric GirardInstitut de Biologie Structurale (IBS), University of Grenoble Alpes (UGA), Commissariat à l'énergie atomique et aux énergies alternatives (CEA), Centre National de la Recherche Scientifique (CNRS), F-38000 Grenoble, France.
François RiobéLaboratoire de Chimie, UMR 5182 CNRS, École normale supérieure de Lyon, Université Lyon 1, 69364 Lyon Cedex 07, France.ORCID 0000-0001-6746-8132
Olivier MauryLaboratoire de Chimie, UMR 5182 CNRS, École normale supérieure de Lyon, Université Lyon 1, 69364 Lyon Cedex 07, France.
Tobias J ErbBiochemistry and Synthetic Metabolism, Max Planck Institute for Terrestrial Microbiology, 35043 Marburg, Germany.
Seigo ShimaMicrobial Protein Structure Group, Max Planck Institute for Terrestrial Microbiology, 35043 Marburg, Germany.
Tristan WagnerMicrobial Protein Structure Group, Max Planck Institute for Terrestrial Microbiology, 35043 Marburg, Germany tristan.wagner@mpi-marburg.mpg.de.
Max Planck Institute for Terrestrial Microbiology · DECentre National de la Recherche Scientifique · FRUniversité Claude Bernard Lyon 1 · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Many reactions within a cell are thermodynamically unfavorable. To efficiently run some of those endergonic reactions, nature evolved intermediate-channeling enzyme complexes, in which the products of the first endergonic reactions are immediately consumed by the second exergonic reactions. Based on this concept, we studied how archaea overcome the unfavorable first reaction of isoprenoid biosynthesis-the condensation of two molecules of acetyl-CoA to acetoacetyl-CoA catalyzed by acetoacetyl-CoA thiolases (thiolases). We natively isolated an enzyme complex comprising the thiolase and 3-hydroxy-3-methylglutaryl (HMG)-CoA synthase (HMGCS) from a fast-growing methanogenic archaeon,

Indexed as

Acetyl-CoA C-AcetyltransferaseAcetyl Coenzyme AAcyl Coenzyme AArchaeaBinding SitesCatalysisCatalytic DomainCrystallography, X-RayHydroxymethylglutaryl-CoA SynthaseProtein Conformationacetoacetyl CoAAcetyl-CoA C-AcetyltransferaseAcetyl Coenzyme AAcyl Coenzyme AHydroxymethylglutaryl-CoA Synthasearchaeaenzymatic channelingisoprenoid synthesismevalonate productionX-ray crystallography

Identifiers

PMID29531083
PMCPMC5879682
OpenAlexW2790748531

What OpenQuestion holds

Textmetadata
Read underepoch 390

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.