Evidence map›Paper›PMID 20099870›Full record

ArticleBiochemistry2010

Structural insights into the prereaction state of pyruvate decarboxylase from Zymomonas mobilis .

Xue-Yuan Pei, Karl M Erixon, Ben F Luisi, Finian J Leeper

Open access · bronzeAbstract read
In one paragraph

Article in Biochemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
1.9field-weighted citation impact, top 16% 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

15 citing papers in PubMed, 47 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. New Role of Water in Transketolase Catalysis.International journal of molecular sciences · 2023
    Article
  7. Enzymes for Efficient COThe protein journal · 2021
    Review
  8. Crystal structure of an inferred ancestral bacterial pyruvate decarboxylase.Acta crystallographica. Section F, Structural biology communications · 2018
    Article
  9. Article
  10. Crystal structure of pyruvate decarboxylase from Zymobacter palmae.Acta crystallographica. Section F, Structural biology communications · 2016
    Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Review
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

4 authors at 1 institution in 1 country.

Xue-Yuan PeiDepartment of Biochemistry, University of Cambridge, Tennis Court Road, Cambridge CB2 1QA, UK.
Karl M Erixon
Ben F Luisi
Finian J Leeper
University of Cambridge · GB

Funding

Wellcome Trust
6 · The paper itself

Abstract

Pyruvate decarboxylase (PDC) uses thiamine diphosphate as an essential cofactor to catalyze the formation of acetaldehyde on the pathway of ethanol synthesis. Here we report the crystallographic image of a prereaction intermediate of a bacterial pyruvate decarboxylase prepared by cocrystallizing the enzyme with pyruvate and a stable analogue of the cofactor's activated ylid form. A second crystal structure of PDC in complex with fluoride shows that the ion organizes a water molecule that occludes the pyruvate binding site, accounting for the inhibitory effect of the halide. Also reported is a structure of the cofactor-free apo form, which when compared to the structure of the holo form indicates how thiamine diphosphate organizes the active site pocket of pyruvate decarboxylase to support catalysis. Guided by the structural and enzymatic data, we propose roles for several key residues in the catalytic mechanism.

Indexed as

Bacterial ProteinsBinding SitesCatalytic DomainCrystallography, X-RayFluoridesProtein Structure, SecondaryPyruvate DecarboxylasePyruvic AcidZymomonasBacterial ProteinsFluoridesPyruvate DecarboxylasePyruvic Acid

Identifiers

PMID20099870
PMCPMC2855724
OpenAlexW2032422364

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.