Evidence map›Paper›PMID 39152907›Full record

ArticleBiochemistry2024

Enzyme Catalyzed Formation of CoA Adducts of Fluorinated Hexanoic Acid Analogues using a Long-Chain acyl-CoA Synthetase from

Robert G Mothersole, Mina K Mothersole, Hannah G Goddard, Jinxia Liu, Jonathan D Van Hamme

Abstract read
In one paragraph

Article in Biochemistry, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing 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

6 citing papers in PubMed.

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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.

Robert G MothersoleDepartment of Chemistry, Thompson Rivers University, 805 TRU Way, Kamloops, British Columbia V2C 0C8, Canada.ORCID 0000-0001-7889-0988
Mina K MothersoleDepartment of Biological Sciences, Thompson Rivers University, 805 TRU Way, Kamloops, British Columbia V2C 0C8, Canada.ORCID 0000-0002-2929-7296
Hannah G GoddardDepartment of Biological Sciences, Thompson Rivers University, 805 TRU Way, Kamloops, British Columbia V2C 0C8, Canada.
Jinxia LiuDepartment of Civil Engineering, McGill University, 817 Sherbrooke Street West, Montreal, Québec H3A 0C3, Canada.ORCID 0000-0003-2505-9642
Jonathan D Van HammeDepartment of Biological Sciences, Thompson Rivers University, 805 TRU Way, Kamloops, British Columbia V2C 0C8, Canada.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Per and polyfluoroalkyl substances (PFAS) are a large family of anthropogenic fluorinated chemicals of increasing environmental concern. Over recent years, numerous microbial communities have been found to be capable of metabolizing some polyfluoroalkyl substances, generating a range of low-molecular-weight PFAS metabolites. One proposed pathway for the microbial breakdown of fluorinated carboxylates includes β-oxidation, this pathway is initiated by the formation of a CoA adduct. However, until recently no PFAS-CoA adducts had been reported. In a previous study, we were able to use a bacterial medium-chain acyl-CoA synthetase (mACS) to form CoA adducts of fluorinated adducts of propanoic acid and pentanoic acid but were not able to detect any products of fluorinated hexanoic acid analogues. Herein, we expressed and purified a long-chain acyl-CoA synthetase (lACS) and a A461K variant of mACS from the soil bacterium

Indexed as

CaproatesCoenzyme A LigasesAcyl Coenzyme ABacterial ProteinsCoenzyme AGordonia BacteriumHalogenationKineticsLong-Chain-Fatty-Acid-CoA LigaseSubstrate SpecificityAcyl Coenzyme ABacterial ProteinsCaproatesCoenzyme ACoenzyme A Ligaseshexanoic acidLong-Chain-Fatty-Acid-CoA Ligase

Identifiers

PMID39152907
PMCPMC11376266

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Registered trials

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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.