Evidence map›Paper›PMID 32694223›Full record

ArticleThe Journal of biological chemistry2020

Carnitine metabolism in the human gut: characterization of the two-component carnitine monooxygenase CntAB from

Marco Massmig, Edward Reijerse, Joern Krausze, Christoph Laurich, Wolfgang Lubitz, Dieter Jahn, Jürgen Moser

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
2.4field-weighted citation impact, top 11% 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

15 citing papers in PubMed, 28 citations in OpenAlex.

  1. Trimethylamine-N-oxide: the microbial cue in immune-mediated disorders.Trends in endocrinology and metabolism: TEM · 2026
    Review
  2. Review
  3. Amino acid metabolism in diabetic kidney disease.Clinical and experimental nephrology · 2026
    Review
  4. Metabolic versatility ofFrontiers in microbiology · 2026
    Article
  5. Review
  6. Article
  7. Roles of DJ41_1407 and DJ41_1408 inInternational journal of molecular sciences · 2024
    Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. 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

7 authors at 2 institutions in 1 country.

Marco MassmigInstitute of Microbiology, Technical University Braunschweig, Braunschweig, Germany.
Edward ReijerseMax-Planck-Institute for Chemical Energy Conversion, Mülheim an der Ruhr, Germany.
Joern KrauszeInstitute of Plant Biology, Technical University Braunschweig, Braunschweig, Germany.
Christoph LaurichMax-Planck-Institute for Chemical Energy Conversion, Mülheim an der Ruhr, Germany.
Wolfgang LubitzMax-Planck-Institute for Chemical Energy Conversion, Mülheim an der Ruhr, Germany.
Dieter JahnBraunschweig Centre of Integrated Systems Biology, Braunschweig, Germany.
Jürgen MoserInstitute of Microbiology, Technical University Braunschweig, Braunschweig, Germany. Electronic address: j.moser@tu-bs.de.
Max Planck Institute for Chemical Energy Conversion · DETechnische Universität Braunschweig · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Bacterial formation of trimethylamine (TMA) from carnitine in the gut microbiome has been linked to cardiovascular disease. During this process, the two-component carnitine monooxygenase (CntAB) catalyzes the oxygen-dependent cleavage of carnitine to TMA and malic semialdehyde. Individual redox states of the reductase CntB and the catalytic component CntA were investigated based on mutagenesis and electron paramagnetic resonance (EPR) spectroscopic approaches. Protein ligands of the flavin mononucleotide (FMN) and the plant-type [2Fe-2S] cluster of CntB and also of the Rieske-type [2Fe-2S] cluster and the mononuclear [Fe] center of CntA were identified. EPR spectroscopy of variant CntA proteins suggested a hierarchical metallocenter maturation, Rieske [2Fe-2S] followed by the mononuclear [Fe] center. NADH-dependent electron transfer

Indexed as

Acinetobacter baumanniiBacterial ProteinsGastrointestinal MicrobiomeHumansIntestinesMixed Function OxygenasesBacterial ProteinsMixed Function Oxygenasescarnitine monooxygenaseCntABelectron paramagnetic resonanceelectron paramagnetic resonance (EPR)enzyme mechanismgut microbiotairon-sulfur proteinl-carnitinemetalloenzymeRieske-type oxygenasesite-directed mutagenesistrimethylamine

Identifiers

PMID32694223
PMCPMC7489909
OpenAlexW3044501025

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.