Evidence map›Paper›PMID 35535733›Full record

ArticleChemistry (Weinheim an der Bergstrasse, Germany)2022

Dihydroxy-Acid Dehydratases From Pathogenic Bacteria: Emerging Drug Targets to Combat Antibiotic Resistance.

Tenuun Bayaraa, Jose Gaete, Samuel Sutiono, Julia Kurz, Thierry Lonhienne, Jeffrey R Harmer, Paul V Bernhardt, Volker Sieber, Luke Guddat, Gerhard Schenk

Open access · hybridAbstract read
In one paragraph

Article in Chemistry (Weinheim an der Bergstrasse, Germany), 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
0.9field-weighted citation impact, top 31% 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

8 citing papers in PubMed, 13 citations in OpenAlex.

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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

10 authors at 2 institutions in 2 countries.

Tenuun BayaraaSchool of Chemistry and Molecular Biosciences, The University of Queensland, Brisbane, 4072, Australia.
Jose GaeteSchool of Chemistry and Molecular Biosciences, The University of Queensland, Brisbane, 4072, Australia.
Samuel SutionoChair of Chemistry of Biogenic resources, Campus Straubing for Biotechnology and Sustainability, Technical University of Munich, Schulgasse 16, 94315, Straubing, Germany.
Julia KurzSchool of Chemistry and Molecular Biosciences, The University of Queensland, Brisbane, 4072, Australia.
Thierry LonhienneSchool of Chemistry and Molecular Biosciences, The University of Queensland, Brisbane, 4072, Australia.
Jeffrey R HarmerCentre for Advanced Imaging, The University of Queensland, Brisbane, 4072, Australia.
Paul V BernhardtSchool of Chemistry and Molecular Biosciences, The University of Queensland, Brisbane, 4072, Australia.
Volker SieberSchool of Chemistry and Molecular Biosciences, The University of Queensland, Brisbane, 4072, Australia.
Luke GuddatSchool of Chemistry and Molecular Biosciences, The University of Queensland, Brisbane, 4072, Australia.
Gerhard SchenkSchool of Chemistry and Molecular Biosciences, The University of Queensland, Brisbane, 4072, Australia.ORCID http://orcid.org/0000-0001-8619-0631
The University of Queensland · AUTechnical University of Munich · DE

Funding

Australian Research Council DP210101802National Health and Medical Research Council, Australia 2003946
6 · The paper itself

Abstract

There is an urgent global need for the development of novel therapeutics to combat the rise of various antibiotic-resistant superbugs. Enzymes of the branched-chain amino acid (BCAA) biosynthesis pathway are an attractive target for novel anti-microbial drug development. Dihydroxy-acid dehydratase (DHAD) is the third enzyme in the BCAA biosynthesis pathway. It relies on an Fe-S cluster for catalytic activity and has recently also gained attention as a catalyst in cell-free enzyme cascades. Two types of Fe-S clusters have been identified in DHADs, i.e. [2Fe-2S] and [4Fe-4S], with the latter being more prone to degradation in the presence of oxygen. Here, we characterise two DHADs from bacterial human pathogens, Staphylococcus aureus and Campylobacter jejuni (SaDHAD and CjDHAD). Purified SaDHAD and CjDHAD are virtually inactive, but activity could be reversibly reconstituted in vitro (up to ∼19,000-fold increase with k

Indexed as

Drug Resistance, BacterialHydro-LyasesBacterial ProteinsCampylobacter jejuniCatalysisIron-Sulfur ProteinsStaphylococcus aureusBacterial ProteinsHydro-LyasesIron-Sulfur Proteinsantibioticsdihydroxy-acid dehydrataseenzyme activationFe−S clustersustainable chemistry

Identifiers

PMID35535733
PMCPMC9543379
OpenAlexW4229442744

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.