Evidence map›Paper›PMID 26187464›Full record

ArticleThe Journal of biological chemistry2015

Structure and Function of CutC Choline Lyase from Human Microbiota Bacterium Klebsiella pneumoniae.

Gints Kalnins, Janis Kuka, Solveiga Grinberga, Marina Makrecka-Kuka, Edgars Liepinsh, Maija Dambrova, Kaspars Tars

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 68 papers.

0numbers the graph read from it
0cells of the map it votes in
68citing papers in PubMed
5.6field-weighted citation impact, top 4% 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

68 citing papers in PubMed, 100 citations in OpenAlex.

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  16. Microbiome research reports · 2025
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8 more citing papers are in PubMed but not listed here.

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

7 authors at 3 institutions in 1 country.

Gints KalninsFrom the Latvian Biomedical Research and Study Center, LV-1067 Riga, gints@biomed.lu.lv.
Janis Kukathe Latvian Institute of Organic Synthesis, LV-1006 Riga, and.
Solveiga Grinbergathe Latvian Institute of Organic Synthesis, LV-1006 Riga, and.
Marina Makrecka-Kukathe Latvian Institute of Organic Synthesis, LV-1006 Riga, and.
Edgars Liepinshthe Latvian Institute of Organic Synthesis, LV-1006 Riga, and.
Maija Dambrovathe Latvian Institute of Organic Synthesis, LV-1006 Riga, and.
Kaspars TarsFrom the Latvian Biomedical Research and Study Center, LV-1067 Riga, the University of Latvia, LV-1586 Riga, Latvia.
Latvijas Organiskās Sintēzes Institūts · LVLatvian Biomedical Research and Study Centre · LVUniversity of Latvia · LV

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

CutC choline trimethylamine-lyase is an anaerobic bacterial glycyl radical enzyme (GRE) that cleaves choline to produce trimethylamine (TMA) and acetaldehyde. In humans, TMA is produced exclusively by the intestinal microbiota, and its metabolite, trimethylamine oxide, has been associated with a higher risk of cardiovascular diseases. Therefore, information about the three-dimensional structures of TMA-producing enzymes is important for microbiota-targeted drug discovery. We have cloned, expressed, and purified the CutC GRE and the activating enzyme CutD from Klebsiella pneumoniae, a representative of the human microbiota. We have determined the first crystal structures of both the choline-bound and choline-free forms of CutC and have discovered that binding of choline at the ligand-binding site triggers conformational changes in the enzyme structure, a feature that has not been observed for any other characterized GRE.

Indexed as

MicrobiotaBacterial ProteinsCatalytic DomainCholineChromatography, GelChymotrypsinElectrophoresis, Polyacrylamide GelHumansKlebsiella pneumoniaeLyasesModels, MolecularProtein MultimerizationProtein Structure, TertiarySpectrometry, Mass, Matrix-Assisted Laser Desorption-IonizationBacterial ProteinsCholineChymotrypsinLyasescholineconformational changeenzyme catalysisenzyme structureradical

Identifiers

PMID26187464
PMCPMC4571895
OpenAlexW2282235374

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.