Evidence map›Paper›PMID 39023782›Full record

ArticleApplied microbiology and biotechnology2024

Prenylation of aromatic amino acids and plant phenolics by an aromatic prenyltransferase from Rasamsonia emersonii.

Pimvisuth Chunkrua, Kai P Leschonski, Alejandro A Gran-Scheuch, Gijs J C Vreeke, Jean-Paul Vincken, Marco W Fraaije, Willem J H van Berkel, Wouter J C de Bruijn, Mirjam A Kabel

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Applied microbiology and biotechnology, 2024. 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

9 authors.

Pimvisuth ChunkruaLaboratory of Food Chemistry, Wageningen University, Bornse Weilanden 9, 6708 WG, Wageningen, The Netherlands.ORCID http://orcid.org/0000-0001-7432-5359
Kai P LeschonskiLaboratory of Food Chemistry, Wageningen University, Bornse Weilanden 9, 6708 WG, Wageningen, The Netherlands.ORCID http://orcid.org/0009-0009-3539-6213
Alejandro A Gran-ScheuchMolecular Enzymology Group, University of Groningen, Nijenborgh 4, 9747 AG, Groningen, The Netherlands.ORCID http://orcid.org/0000-0001-9979-0927
Gijs J C VreekeLaboratory of Food Chemistry, Wageningen University, Bornse Weilanden 9, 6708 WG, Wageningen, The Netherlands.ORCID http://orcid.org/0000-0002-8088-500X
Jean-Paul VinckenLaboratory of Food Chemistry, Wageningen University, Bornse Weilanden 9, 6708 WG, Wageningen, The Netherlands.ORCID http://orcid.org/0000-0001-8540-4327
Marco W FraaijeMolecular Enzymology Group, University of Groningen, Nijenborgh 4, 9747 AG, Groningen, The Netherlands.ORCID http://orcid.org/0000-0001-6346-5014
Willem J H van BerkelLaboratory of Food Chemistry, Wageningen University, Bornse Weilanden 9, 6708 WG, Wageningen, The Netherlands.ORCID http://orcid.org/0000-0002-6551-2782
Wouter J C de BruijnLaboratory of Food Chemistry, Wageningen University, Bornse Weilanden 9, 6708 WG, Wageningen, The Netherlands.ORCID http://orcid.org/0000-0003-0564-9848
Mirjam A KabelLaboratory of Food Chemistry, Wageningen University, Bornse Weilanden 9, 6708 WG, Wageningen, The Netherlands. mirjam.kabel@wur.nl.ORCID http://orcid.org/0000-0002-2787-7852

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Dimethylallyl tryptophan synthases (DMATSs) are aromatic prenyltransferases that catalyze the transfer of a prenyl moiety from a donor to an aromatic acceptor during the biosynthesis of microbial secondary metabolites. Due to their broad substrate scope, DMATSs are anticipated as biotechnological tools for producing bioactive prenylated aromatic compounds. Our study explored the substrate scope and product profile of a recombinant RePT, a novel DMATS from the thermophilic fungus Rasamsonia emersonii. Among a variety of aromatic substrates, RePT showed the highest substrate conversion for L-tryptophan and L-tyrosine (> 90%), yielding two mono-prenylated products in both cases. Nine phenolics from diverse phenolic subclasses were notably converted (> 10%), of which the stilbenes oxyresveratrol, piceatannol, pinostilbene, and resveratrol were the best acceptors (37-55% conversion). The position of prenylation was determined using NMR spectroscopy or annotated using MS

Indexed as

Amino Acids, AromaticDimethylallyltranstransferasePhenolsPrenylationRecombinant ProteinsStilbenesSubstrate SpecificityTryptophanAmino Acids, AromaticDimethylallyltranstransferasePhenolsRecombinant ProteinsStilbenesTryptophanAlkylationaPTBiocatalysisDMATSFungal PTTryptophan

Identifiers

PMID39023782
PMCPMC11258057

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.