Evidence map›Paper›PMID 22492439›Full record

ArticleApplied and environmental microbiology2012

Purification and characterization of the acetone carboxylase of Cupriavidus metallidurans strain CH34.

Caroline Rosier, Natalie Leys, Céline Henoumont, Max Mergeay, Ruddy Wattiez

Open access · bronzeAbstract read
In one paragraph

Article in Applied and environmental microbiology, 2012. 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
0.7field-weighted citation impact, top 32% 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, 19 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

5 authors at 2 institutions in 1 country.

Caroline RosierDepartment of Proteomics and Microbiology, Interdisciplinary Center of Mass Spectrometry (CISMa), University of Mons, Mons, Belgium.
Natalie Leys
Céline Henoumont
Max Mergeay
Ruddy Wattiez
University of Mons · BEBelgian Nuclear Research Centre · BE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Acetone carboxylase (Acx) is a key enzyme involved in the biodegradation of acetone by bacteria. Except for the Helicobacteraceae family, genome analyses revealed that bacteria that possess an Acx, such as Cupriavidus metallidurans strain CH34, are associated with soil. The Acx of CH34 forms the heterohexameric complex α(2)β(2)γ(2) and can carboxylate only acetone and 2-butanone in an ATP-dependent reaction to acetoacetate and 3-keto-2-methylbutyrate, respectively.

Indexed as

AcetoneButanonesCarboxy-LyasesCupriavidusElectrophoresis, Polyacrylamide GelEnzyme StabilityHydrogen-Ion ConcentrationProtein MultimerizationProtein SubunitsSubstrate SpecificityTemperatureAcetoneacetone carboxylaseButanonesCarboxy-Lyasesmethylethyl ketoneProtein Subunits

Identifiers

PMID22492439
PMCPMC3370517
OpenAlexW2006330843

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.