Evidence map›Paper›PMID 38416537›Full record

ArticleChembiochem : a European journal of chemical biology2024

Ether Bond Cleavage of a Phenylcoumaran β-5 Lignin Model Compound and Polymeric Lignin Catalysed by a LigE-type Etherase from Agrobacterium sp.

Goran M M Rashid, Guillaume N Rivière, Betty Cottyn-Boitte, Amel Majira, Laurent Cézard, Victoria Sodré, Richard Lam, Julia A Fairbairn, Stéphanie Baumberger, Timothy D H Bugg

Open access · hybridAbstract read
In one paragraph

Article in Chembiochem : a European journal of chemical biology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
0.7field-weighted citation impact, top 35% 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

4 citing papers in PubMed, 4 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. 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

10 authors at 2 institutions in 2 countries.

Goran M M RashidDepartment of Chemistry, University of Warwick, Gibbet Hill Road, Coventry, CV4 7AL, United Kingdom.
Guillaume N RivièreUniversité Paris-Saclay, INRAE, AgroParisTech, Institute Jean-Pierre Bourgin (IJPB), 78000, Versailles, France.
Betty Cottyn-BoitteUniversité Paris-Saclay, INRAE, AgroParisTech, Institute Jean-Pierre Bourgin (IJPB), 78000, Versailles, France.
Amel MajiraUniversité Paris-Saclay, INRAE, AgroParisTech, Institute Jean-Pierre Bourgin (IJPB), 78000, Versailles, France.
Laurent CézardUniversité Paris-Saclay, INRAE, AgroParisTech, Institute Jean-Pierre Bourgin (IJPB), 78000, Versailles, France.
Victoria SodréDepartment of Chemistry, University of Warwick, Gibbet Hill Road, Coventry, CV4 7AL, United Kingdom.
Richard LamDepartment of Chemistry, University of Warwick, Gibbet Hill Road, Coventry, CV4 7AL, United Kingdom.
Julia A FairbairnDepartment of Chemistry, University of Warwick, Gibbet Hill Road, Coventry, CV4 7AL, United Kingdom.
Stéphanie BaumbergerUniversité Paris-Saclay, INRAE, AgroParisTech, Institute Jean-Pierre Bourgin (IJPB), 78000, Versailles, France.
Timothy D H BuggDepartment of Chemistry, University of Warwick, Gibbet Hill Road, Coventry, CV4 7AL, United Kingdom.ORCID 0000-0003-3964-4498
AgroParisTech · FRUniversity of Warwick · GB

Funding

BBSRC BB/T010622/1MRC-DTPUniversity of Warwick
6 · The paper itself

Abstract

A LigE-type beta-etherase enzyme from lignin-degrading Agrobacterium sp. has been identified, which assists degradation of polymeric lignins. Testing against lignin dimer model compounds revealed that it does not catalyse the previously reported reaction of Sphingobium SYK-6 LigE, but instead shows activity for a β-5 phenylcoumaran lignin dimer. The reaction products did not contain glutathione, indicating a catalytic role for reduced glutathione in this enzyme. Three reaction products were identified: the major product was a cis-stilbene arising from C-C fragmentation involving loss of formaldehyde; two minor products were an alkene arising from elimination of glutathione, and an oxidised ketone, proposed to arise from reaction of an intermediate with molecular oxygen. Testing of the recombinant enzyme against a soda lignin revealed the formation of new signals by two-dimensional NMR analysis, whose chemical shifts are consistent with the formation of a stilbene unit in polymeric lignin.

Indexed as

LigninStilbenesAgrobacteriumEtherEthersEthyl EthersGlutathioneEtherEthersEthyl EthersGlutathioneLigninStilbenesAgrobacteriumbeta-etheraseLigElignin degradationphenylcoumaran

Identifiers

PMID38416537
PMCPMC11497285
OpenAlexW4392242287

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.