Evidence map›Paper›PMID 27642758›Full record

ArticlePloS one2016

Linkage between Fitness of Yeast Cells and Adenylate Kinase Catalysis.

Hasan Tükenmez, Helge Magnus Magnussen, Michael Kovermann, Anders Byström, Magnus Wolf-Watz

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
0.9field-weighted citation impact, top 23% 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

14 citing papers in PubMed, 17 citations in OpenAlex.

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  7. Protein dynamics: The future is bright and complicated!Structural dynamics (Melville, N.Y.) · 2023
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  12. Article
  13. Molecular mechanism of ATP versus GTP selectivity of adenylate kinase.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  14. The Effect of Fermented Lingonberry Juice onInternational journal of dentistry · 2017
    Article
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

5 authors at 1 institution in 1 country.

Hasan TükenmezDepartment of Molecular Biology, Umeå University, SE-901 87, Umeå, Sweden.
Helge Magnus MagnussenDepartment of Chemistry, Umeå University, SE-901 87, Umeå, Sweden.
Michael KovermannDepartment of Chemistry, Umeå University, SE-901 87, Umeå, Sweden.
Anders ByströmDepartment of Molecular Biology, Umeå University, SE-901 87, Umeå, Sweden.
Magnus Wolf-WatzDepartment of Chemistry, Umeå University, SE-901 87, Umeå, Sweden.
Umeå University · SE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Enzymes have evolved with highly specific values of their catalytic parameters kcat and KM. This poses fundamental biological questions about the selection pressures responsible for evolutionary tuning of these parameters. Here we are address these questions for the enzyme adenylate kinase (Adk) in eukaryotic yeast cells. A plasmid shuffling system was developed to allow quantification of relative fitness (calculated from growth rates) of yeast in response to perturbations of Adk activity introduced through mutations. Biophysical characterization verified that all variants studied were properly folded and that the mutations did not cause any substantial differences to thermal stability. We found that cytosolic Adk is essential for yeast viability in our strain background and that viability could not be restored with a catalytically dead, although properly folded Adk variant. There exist a massive overcapacity of Adk catalytic activity and only 12% of the wild type kcat is required for optimal growth at the stress condition 20°C. In summary, the approach developed here has provided new insights into the evolutionary tuning of kcat for Adk in a eukaryotic organism. The developed methodology may also become useful for uncovering new aspects of active site dynamics and also in enzyme design since a large library of enzyme variants can be screened rapidly by identifying viable colonies.

Indexed as

Genetic LinkageAdenylate KinaseCatalysisPlasmidsYeastsAdenylate Kinase

Identifiers

PMID27642758
PMCPMC5028032
OpenAlexW2522558972

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.