Evidence map›Paper›PMID 27884109›Full record

ArticleBMC microbiology2016

Cloning, functional expression and characterization of a bifunctional 3-hydroxybutanal dehydrogenase /reductase involved in acetone metabolism by Desulfococcus biacutus.

Jasmin Frey, Hendrik Rusche, Bernhard Schink, David Schleheck

Open access · goldAbstract read
In one paragraph

Article in BMC microbiology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
0.7field-weighted citation impact, top 25% 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

3 citing papers in PubMed, 10 citations in OpenAlex.

  1. 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

4 authors at 1 institution in 1 country.

Jasmin FreyDepartment of Biology, University of Konstanz, Postbox 649, D-78457, Konstanz, Germany.
Hendrik RuscheDepartment of Biology, University of Konstanz, Postbox 649, D-78457, Konstanz, Germany.
Bernhard SchinkDepartment of Biology, University of Konstanz, Postbox 649, D-78457, Konstanz, Germany.
David SchleheckDepartment of Biology, University of Konstanz, Postbox 649, D-78457, Konstanz, Germany. david.schleheck@uni-konstanz.de.
University of Konstanz · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundThe strictly anaerobic, sulfate-reducing bacterium Desulfococcus biacutus can utilize acetone as sole carbon and energy source for growth. Whereas in aerobic and nitrate-reducing bacteria acetone is activated by carboxylation with CO

resultsThe MDR gene DebiaDRAFT_04514 was cloned and overexpressed in E. coli. The purified recombinant protein required zinc as cofactor, and accepted NADH/NAD

conclusionThe enzyme might play a key role in acetone degradation by D. biacutus, for example as a bifunctional 3-hydroxybutanal dehydrogenase/reductase. Its recombinant production may represent an important step in the elucidation of the complete degradation pathway.

Indexed as

Cloning, OrganismAcetaldehydeAcetoneAlcohol DehydrogenaseAldehydesBacteria, AnaerobicBacterial ProteinsButanolsButylene GlycolsCarbon MonoxideCoenzymesDeltaproteobacteriaEnzyme ActivationEnzyme AssaysEscherichia coliGene Expression Regulation, Bacterial1,3-butylene glycol3-hydroxybutanalAcetaldehydeacetoacetaldehydeAcetoneAlcohol DehydrogenaseAldehydesBacterial ProteinsButanolsButylene GlycolsbutyraldehydeCarbon MonoxideCoenzymesNADNADPOxidoreductasesPropanolspropionaldehydeRecombinant ProteinsZincAcetone activationBifunctional MDR superfamily oxidoreductaseCarbonylationSulfate-reducing bacteria

Identifiers

PMID27884109
PMCPMC5123277
OpenAlexW2550419195

What OpenQuestion holds

Textmetadata
LicenceCC BY
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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.