Evidence map›Paper›PMID 40067141›Full record

ArticleChemistry (Weinheim an der Bergstrasse, Germany)2025

Enzyme-Catalysed Formation of Hydrocarbon Scaffolds from Geranylgeranyl Diphosphate Analogs with Shifted Double Bonds.

Heng Li, Bernd Goldfuss, Jeroen S Dickschat

Abstract read
In one paragraph

Article in Chemistry (Weinheim an der Bergstrasse, Germany), 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

1 citing paper in PubMed.

  1. 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

3 authors.

Heng LiKekulé-Institute for Organic Chemistry and Biochemistry, University of Bonn, Gerhard-Domagk-Straße 1, 53121, Bonn, Germany.
Bernd GoldfussDepartment for Chemistry, University of Cologne, Greinstraße 4, 50939, Cologne, Germany.
Jeroen S DickschatKekulé-Institute for Organic Chemistry and Biochemistry, University of Bonn, Gerhard-Domagk-Straße 1, 53121, Bonn, Germany.ORCID https://orcid.org/0000-0002-0102-0631

Funding

Deutsche Forschungsgemeinschaft 513548540
6 · The paper itself

Abstract

Four analogs of geranylgeranyl diphosphate (GGPP) with shifted double bonds were synthesised and enzymatically converted with 14 diterpene synthases of previously reported function, including two newly characterised homologs of the benditerpe-2,6,15-triene synthase Bnd4 and the venezuelaene synthase VenA. In successful cases the products were isolated and structurally characterised by NMR spectroscopy, revealing the formation of various diterpenoids with skeletons that have not been reported from natural sources. Isotopic labelling experiments in conjunction with DFT calculations were performed to give insights into hydride migrations in the biosynthesis of the non-natural diterpenes benditerpe-2,7(19),15-triene and venezuelaxenene and their natural counterparts from GGPP.

Indexed as

Alkyl and Aryl TransferasesDiterpenesHydrocarbonsPolyisoprenyl PhosphatesBiocatalysisMagnetic Resonance SpectroscopyAlkyl and Aryl TransferasesDiterpenesgeranylgeranyl pyrophosphateHydrocarbonsPolyisoprenyl Phosphatesbiosynthesisenzyme mechanismsisotopessubstrate analogsterpenes

Identifiers

PMID40067141
PMCPMC12015392

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.