Evidence map›Paper›PMID 40804552›Full record

ArticlePlanta2025

Discovery of corynanthe synthases in Camptotheca acuminata: medium-chain dehydrogenase/reductase-based gateway to corynanthe-type compound diversification.

Van-Hung Bui, Tuan-Anh Minh Nguyen, Truc Kim, Shenyu Liu, Benedikt Seligmann, Parandis Daneshgar, Trinh-Don Nguyen, Wesley F Zandberg, Jakob Franke, Thu-Thuy T Dang

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Article in Planta, 2025. 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. Article
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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.

Van-Hung BuiDepartment of Chemistry, Irving K. Barber Faculty of Science, University of British Columbia, 3247 University Way, Kelowna, BC, Canada.
Tuan-Anh Minh NguyenDepartment of Chemistry, Irving K. Barber Faculty of Science, University of British Columbia, 3247 University Way, Kelowna, BC, Canada.
Truc KimDepartment of Chemistry, Irving K. Barber Faculty of Science, University of British Columbia, 3247 University Way, Kelowna, BC, Canada.
Shenyu LiuInstitute of Botany, Leibniz University Hannover, Herrenhäuser Straße 2, 30419, Hannover, Germany.
Benedikt SeligmannInstitute of Botany, Leibniz University Hannover, Herrenhäuser Straße 2, 30419, Hannover, Germany.
Parandis DaneshgarDepartment of Chemistry, Irving K. Barber Faculty of Science, University of British Columbia, 3247 University Way, Kelowna, BC, Canada.
Trinh-Don NguyenDepartment of Chemistry, Irving K. Barber Faculty of Science, University of British Columbia, 3247 University Way, Kelowna, BC, Canada.
Wesley F ZandbergDepartment of Chemistry, Irving K. Barber Faculty of Science, University of British Columbia, 3247 University Way, Kelowna, BC, Canada.
Jakob FrankeInstitute of Botany, Leibniz University Hannover, Herrenhäuser Straße 2, 30419, Hannover, Germany.
Thu-Thuy T DangDepartment of Chemistry, Irving K. Barber Faculty of Science, University of British Columbia, 3247 University Way, Kelowna, BC, Canada. thuy.dang@ubc.ca.ORCID http://orcid.org/0000-0002-6459-3664

Funding

Bundesministerium für Bildung, Wissenschaft, Forschung und Technologie 031B1208CFI JELF 35426CFI JELF 38167Michael Smith Health Research BC 2020-40NSERC ALLRP 571673 - 21
6 · The paper itself

Abstract

MAIN

conclusionWe combined bioinformatic analysis with in vitro biochemical assays to identify and characterize six medium-chain dehydrogenase/reductase (MDR) enzymes involved in corynanthe alkaloid biosynthesis in Camptotheca acuminata. Camptotheca acuminata, commonly known as the happy tree, is a medicinal plant from the monoterpenoid indole alkaloids (MIAs)-rich Nyssaceae family. In this study, we combined bioinformatic analysis and biochemical investigations to identify new enzymes involved in the biosynthesis of corynanthe alkaloids, an MIA subgroup, in C. acuminata. We identified six medium-chain dehydrogenase/reductase (MDR) enzymes, four of which catalyze the formation of diverse simple corynanthe alkaloids. Structural modeling of the two newly identified enzymes, namely CaMDR1 and CaMDR2, revealed key active-site residues Ser52 and Ser55/His55, crucial for their product profiles. The identification of these new corynanthe synthases further advances our understanding of the formation and diversification of corynanthe alkaloids and MIAs in happy tree and related species.

Indexed as

CamptothecaIndole AlkaloidsOxidoreductasesPlant ProteinsComputational BiologyModels, MolecularPhylogenySecologanin Tryptamine AlkaloidsIndole AlkaloidsOxidoreductasesPlant ProteinsSecologanin Tryptamine AlkaloidsBiosynthesisCamptotheca acuminataCorynanthe alkaloidHeteroyohimbaneMedium-chain dehydrogenase/reductaseMonoterpenoid indole alkaloidNatural productYohimbane

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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.