Evidence map›Paper›PMID 33597725›Full record

ArticleCommunications biology2021

Bioinformatics-aided identification, characterization and applications of mushroom linalool synthases.

Congqiang Zhang, Xixian Chen, Raphael Tze Chuen Lee, Rehka T, Sebastian Maurer-Stroh, Martin Rühl

Open access · goldAbstract read
In one paragraph

Article in Communications biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
1.9field-weighted citation impact, top 13% 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

16 citing papers in PubMed, 35 citations in OpenAlex.

  1. Article
  2. Review
  3. Clade III Synthases Add Cyclic and Linear Terpenoids to the Psilocybe Metabolome.Chembiochem : a European journal of chemical biology · 2025
    Article
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  5. Article
  6. Article
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  8. Article
  9. Article
  10. Review
  11. Article
  12. Article
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  14. Review
  15. Bioproduction of Linalool From Paper Mill Waste.Frontiers in bioengineering and biotechnology · 2022
    Article
  16. 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

6 authors at 2 institutions in 2 countries.

Congqiang ZhangSingapore Institute of Food and Biotechnology Innovation (SIFBI), Agency for Science, Technology and Research (A*STAR), Singapore, Singapore. congqiang_zhang@sifbi.a-star.edu.sg.ORCID 0000-0003-1070-8806
Xixian ChenSingapore Institute of Food and Biotechnology Innovation (SIFBI), Agency for Science, Technology and Research (A*STAR), Singapore, Singapore.
Raphael Tze Chuen LeeBioinformatics Institute (BII), Agency for Science Technology and Research (A*STAR), Singapore, Singapore.
Rehka TSingapore Institute of Food and Biotechnology Innovation (SIFBI), Agency for Science, Technology and Research (A*STAR), Singapore, Singapore.
Sebastian Maurer-Stroh *Bioinformatics Institute (BII), Agency for Science Technology and Research (A*STAR), Singapore, Singapore.ORCID 0000-0003-0813-9640
Martin Rühl *Institute of Food Chemistry and Food Biotechnology, Justus Liebig University Giessen, Giessen, Germany.
Agency for Science, Technology and Research · SGJustus-Liebig-Universität Gießen · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Enzymes empower chemical industries and are the keystone for metabolic engineering. For example, linalool synthases are indispensable for the biosynthesis of linalool, an important fragrance used in 60-80% cosmetic and personal care products. However, plant linalool synthases have low activities while expressed in microbes. Aided by bioinformatics analysis, four linalool/nerolidol synthases (LNSs) from various Agaricomycetes were accurately predicted and validated experimentally. Furthermore, we discovered a linalool synthase (Ap.LS) with exceptionally high levels of selectivity and activity from Agrocybe pediades, ideal for linalool bioproduction. It effectively converted glucose into enantiopure (R)-linalool in Escherichia coli, 44-fold and 287-fold more efficient than its bacterial and plant counterparts, respectively. Phylogenetic analysis indicated the divergent evolution paths for plant, bacterial and fungal linalool synthases. More critically, structural comparison provided catalytic insights into Ap.LS superior specificity and activity, and mutational experiments validated the key residues responsible for the specificity.

Indexed as

Computational BiologyIndustrial MicrobiologyAcyclic MonoterpenesAgaricalesEvolution, MolecularFungal ProteinsHydro-LyasesKineticsPhylogenyProtein ConformationStructure-Activity RelationshipAcyclic MonoterpenesFungal ProteinsHydro-LyaseslinaloolS-linalool synthase

Identifiers

PMID33597725
PMCPMC7890063
OpenAlexW3132726232

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.