Evidence map›Paper›PMID 36385513›Full record

ArticleChemistry (Weinheim an der Bergstrasse, Germany)2023

Structural and Functional Insight into the Mechanism of the Fe-S Cluster-Dependent Dehydratase from Paralcaligenes ureilyticus.

Tenuun Bayaraa, Thierry Lonhienne, Samuel Sutiono, Okke Melse, Thomas B Brück, Esteban Marcellin, Paul V Bernhardt, Mikael Boden, Jeffrey R Harmer, Volker Sieber and 2 more

Open access · hybridAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Chemistry (Weinheim an der Bergstrasse, Germany), 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
0.3field-weighted citation impact, top 55% 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

1 citing paper in PubMed, 6 citations in OpenAlex.

  1. 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

12 authors at 3 institutions in 2 countries.

Tenuun BayaraaSchool of Chemistry and Molecular Biosciences, The University of Queensland, 4072, Brisbane, Australia.
Thierry LonhienneSchool of Chemistry and Molecular Biosciences, The University of Queensland, 4072, Brisbane, Australia.
Samuel SutionoChair of Chemistry of Biogenic resources, Campus Straubing for Biotechnology and Sustainability, Technical University of Munich, 94315, Straubing, Germany.
Okke MelseChair of Chemistry of Biogenic resources, Campus Straubing for Biotechnology and Sustainability, Technical University of Munich, 94315, Straubing, Germany.
Thomas B BrückWerner Siemens Chair of Synthetic Biotechnology, Department of Chemistry, Technical University of Munich, 85748, Garching, Germany.
Esteban MarcellinAustralian Institute for Bioengineering and Nanotechnology, The University of Queensland, 4072, Brisbane, Australia.
Paul V BernhardtSchool of Chemistry and Molecular Biosciences, The University of Queensland, 4072, Brisbane, Australia.
Mikael BodenSchool of Chemistry and Molecular Biosciences, The University of Queensland, 4072, Brisbane, Australia.
Jeffrey R HarmerCentre for Advanced Imaging, The University of Queensland, 4072, Brisbane, Australia.
Volker SieberSchool of Chemistry and Molecular Biosciences, The University of Queensland, 4072, Brisbane, Australia.
Luke W GuddatSchool of Chemistry and Molecular Biosciences, The University of Queensland, 4072, Brisbane, Australia.
Gerhard SchenkSchool of Chemistry and Molecular Biosciences, The University of Queensland, 4072, Brisbane, Australia.ORCID http://orcid.org/0000-0001-8619-0631
The University of Queensland · AUStadtwerke Straubing (Germany) · DESiemens (Germany) · DE

Funding

Australian Research Council DP210101802National Health and Medical Research Centre (AU) 2003946)
6 · The paper itself

Abstract

Enzyme-catalyzed reaction cascades play an increasingly important role for the sustainable manufacture of diverse chemicals from renewable feedstocks. For instance, dehydratases from the ilvD/EDD superfamily have been embedded into a cascade to convert glucose via pyruvate to isobutanol, a platform chemical for the production of aviation fuels and other valuable materials. These dehydratases depend on the presence of both a Fe-S cluster and a divalent metal ion for their function. However, they also represent the rate-limiting step in the cascade. Here, catalytic parameters and the crystal structure of the dehydratase from Paralcaligenes ureilyticus (PuDHT, both in presence of Mg

Indexed as

Hydro-LyasesAlcaligenaceaeAmino Acid SequenceBinding SitesCatalysisHydro-Lyasesbiomanufacturingbranched-chain amino acid biosynthesiscell-free enzyme cascadesdehydrataseFe−S clusterisobutanol

Identifiers

PMID36385513
PMCPMC10107998
OpenAlexW4309244559

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.