Evidence map›Paper›PMID 30843212›Full record

ArticleThe New phytologist2019

Promiscuous terpene synthases from Prunella vulgaris highlight the importance of substrate and compartment switching in terpene synthase evolution.

Sean R Johnson, Wajid Waheed Bhat, Radin Sadre, Garret P Miller, Alekzander Sky Garcia, Björn Hamberger

Open access · hybridAbstract read
In one paragraph

Article in The New phytologist, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
1.8field-weighted citation impact, top 15% 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

29 citing papers in PubMed, 54 citations in OpenAlex.

  1. Review
  2. Article
  3. Biosynthesis of the Red Algal Diterpene Peyssonnosol in Bacteria.Angewandte Chemie (International ed. in English) · 2025
    Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. Review
  11. EngineeringmLife · 2023
    Article
  12. Article
  13. Plant terpene specialized metabolism: complex networks or simple linear pathways?The Plant journal : for cell and molecular biology · 2023
    Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Functional Prediction ofInternational journal of molecular sciences · 2022
    Article
  19. Review
  20. 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 1 institution in 1 country.

Sean R JohnsonDepartment of Biochemistry and Molecular Biology, Michigan State University, East Lansing, MI, 48824, USA.ORCID 0000-0001-8261-9015
Wajid Waheed BhatDepartment of Biochemistry and Molecular Biology, Michigan State University, East Lansing, MI, 48824, USA.ORCID 0000-0002-7049-8671
Radin SadreDepartment of Biochemistry and Molecular Biology, Michigan State University, East Lansing, MI, 48824, USA.ORCID 0000-0002-8412-2579
Garret P MillerDepartment of Biochemistry and Molecular Biology, Michigan State University, East Lansing, MI, 48824, USA.
Alekzander Sky GarciaDepartment of Biochemistry and Molecular Biology, Michigan State University, East Lansing, MI, 48824, USA.
Björn HambergerDepartment of Biochemistry and Molecular Biology, Michigan State University, East Lansing, MI, 48824, USA.ORCID 0000-0003-1249-1807
Michigan State University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The mint family (Lamiaceae) is well documented as a rich source of terpene natural products. More than 200 diterpene skeletons have been reported from mints, but biosynthetic pathways are known for just a few of these. We crossreferenced chemotaxonomic data with publicly available transcriptomes to select common selfheal (Prunella vulgaris) and its highly unusual vulgarisin diterpenoids as a case study for exploring the origins of diterpene skeletal diversity in Lamiaceae. Four terpene synthases (TPS) from the TPS-a subfamily, including two localised to the plastid, were cloned and functionally characterised. Previous examples of TPS-a enzymes from Lamiaceae were cytosolic and reported to act on the 15-carbon farnesyl diphosphate. Plastidial TPS-a enzymes using the 20-carbon geranylgeranyl diphosphate are known from other plant families, having apparently arisen independently in each family. All four new enzymes were found to be active on multiple prenyl-diphosphate substrates with different chain lengths and stereochemistries. One of the new enzymes catalysed the cyclisation of geranylgeranyl diphosphate into 11-hydroxy vulgarisane, the likely biosynthetic precursor of the vulgarisins. We uncovered the pathway to a rare diterpene skeleton. Our results support an emerging paradigm of substrate and compartment switching as important aspects of TPS evolution and diversification.

Indexed as

Evolution, MolecularAlkyl and Aryl TransferasesGene Expression Regulation, PlantPeptidesPhylogenyPlant LeavesPlant RootsPolyisoprenyl PhosphatesPrunellaRecombinant Fusion ProteinsSubstrate SpecificityTerpenesTranscriptomeAlkyl and Aryl Transferasesgeranylgeranyl pyrophosphatePeptidesPolyisoprenyl PhosphatesRecombinant Fusion ProteinsTerpenesterpene synthasediterpenoidPrunella vulgaris (common selfheal)terpene synthasetranscriptometransit peptidevulgarisane

Identifiers

PMID30843212
PMCPMC6593445
OpenAlexW2921582610

What OpenQuestion holds

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LicenceCC BY
Read underepoch 390

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.