Evidence map›Paper›PMID 40920486›Full record

ArticleThe journal of physical chemistry. B2025

All Roads Lead to Carbinolamine: QM/MM Study of Enzymatic C-N Bond Cleavage in Anaerobic Glycyl Radical Enzyme Choline Trimethylamine-Lyase (CutC).

Marko Hanzevacki, J Jasmin Güven, Philip Hinchliffe, John Shaw, Antonia S J S Mey, Natalie Fey, James Spencer, Adrian J Mulholland

Abstract read
In one paragraph

Article in The journal of physical chemistry. B, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
–field-weighted citation impact
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

2 citing papers in PubMed.

  1. Review
  2. 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

8 authors.

Marko HanzevackiCentre for Computational Chemistry, School of Chemistry, University of Bristol, Bristol BS8 1TS, U.K.ORCID 0000-0002-0834-871X
J Jasmin GüvenEaStCHEM School of Chemistry, University of Edinburgh, Edinburgh EH9 3FJ, U.K.ORCID 0000-0003-1555-0075
Philip HinchliffeSchool of Cellular and Molecular Medicine, University of Bristol, Bristol BS8 1TD, U.K.ORCID 0000-0001-8611-4743
John ShawSchool of Cellular and Molecular Medicine, University of Bristol, Bristol BS8 1TD, U.K.
Antonia S J S MeyEaStCHEM School of Chemistry, University of Edinburgh, Edinburgh EH9 3FJ, U.K.ORCID 0000-0001-7512-5252
Natalie FeyCentre for Computational Chemistry, School of Chemistry, University of Bristol, Bristol BS8 1TS, U.K.ORCID 0000-0003-0609-475X
James SpencerSchool of Cellular and Molecular Medicine, University of Bristol, Bristol BS8 1TD, U.K.ORCID 0000-0002-4602-0571
Adrian J MulhollandCentre for Computational Chemistry, School of Chemistry, University of Bristol, Bristol BS8 1TS, U.K.ORCID 0000-0003-1015-4567

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The anaerobic glycyl radical enzyme choline trimethylamine-lyase (CutC) is produced by multiple bacterial species in the human gut microbiome and catalyzes the conversion of choline to trimethylamine (TMA) and acetaldehyde. CutC has emerged as a promising therapeutic target due to its role in producing TMA, which is subsequently oxidized in the liver to form trimethylamine-

Indexed as

LyasesMolecular Dynamics SimulationQuantum TheoryCatalytic DomainCholineDensity Functional TheoryFree RadicalsHydrogen BondingMethylaminesCholineFree RadicalsLyasesMethylaminestrimethylaminetrimethyloxamine

Identifiers

PMID40920486
PMCPMC12451663

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.