Evidence map›Paper›PMID 19246454›Full record

ArticleThe Journal of biological chemistry2009

Covalently bound substrate at the regulatory site of yeast pyruvate decarboxylases triggers allosteric enzyme activation.

Steffen Kutter, Manfred S Weiss, Georg Wille, Ralph Golbik, Michael Spinka, Stephan König

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
2.6field-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

18 citing papers in PubMed, 46 citations in OpenAlex.

  1. Potent Inhibition ofACS infectious diseases · 2024
    Article
  2. Article
  3. Allosteric inhibition ofPhilosophical transactions of the Royal Society of London. Series B, Biological sciences · 2023
    Article
  4. Article
  5. Enzymes for Efficient COThe protein journal · 2021
    Review
  6. Article
  7. Allosteric regulation of menaquinone (vitamin KThe Journal of biological chemistry · 2020
    Article
  8. Article
  9. Article
  10. Article
  11. PolyprOnline: polyproline helix II and secondary structure assignment database.Database : the journal of biological databases and curation · 2014
    Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
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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

6 authors at 2 institutions in 1 country.

Steffen KutterInstitute for Biochemistry and Biotechnology, Faculty of Biological Sciences, Martin-Luther-University Halle-Wittenberg, Kurt-Mothes-Str. 3, 06120 Halle (Saale), Germany.
Manfred S Weiss
Georg Wille
Ralph Golbik
Michael Spinka
Stephan König
Martin Luther University Halle-Wittenberg · DEEuropean Molecular Biology Laboratory · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The mechanism by which the enzyme pyruvate decarboxylase from two yeast species is activated allosterically has been elucidated. A total of seven three-dimensional structures of the enzyme, of enzyme variants, or of enzyme complexes from two yeast species, three of them reported here for the first time, provide detailed atomic resolution snapshots along the activation coordinate. The prime event is the covalent binding of the substrate pyruvate to the side chain of cysteine 221, thus forming a thiohemiketal. This reaction causes the shift of a neighboring amino acid, which eventually leads to the rigidification of two otherwise flexible loops, one of which provides two histidine residues necessary to complete the enzymatically competent active site architecture. The structural data are complemented and supported by kinetic investigations and binding studies, providing a consistent picture of the structural changes occurring upon enzyme activation.

Indexed as

Allosteric RegulationEnzyme ActivationFungal ProteinsKineticsKluyveromycesProtein Structure, TertiaryPyruvate DecarboxylasePyruvic AcidFungal ProteinsPyruvate DecarboxylasePyruvic Acid

Identifiers

PMID19246454
PMCPMC2673282
OpenAlexW2106471781

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.