Evidence map›Paper›PMID 27412861›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2016

A conserved amino acid residue critical for product and substrate specificity in plant triterpene synthases.

Melissa Salmon, Ramesha B Thimmappa, Robert E Minto, Rachel E Melton, Richard K Hughes, Paul E O'Maille, Andrew M Hemmings, Anne Osbourn

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
4.0field-weighted citation impact, top 6% 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

31 citing papers in PubMed, 66 citations in OpenAlex.

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  7. Comprehensive mutant chemotyping reveals embedding of a lineage-specific biosynthetic gene cluster in wider plant metabolism.Proceedings of the National Academy of Sciences of the United States of America · 2025
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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

8 authors at 3 institutions in 2 countries.

Melissa SalmonJohn Innes Centre, Norwich Research Park, Norwich NR4 7UH, United Kingdom;
Ramesha B ThimmappaJohn Innes Centre, Norwich Research Park, Norwich NR4 7UH, United Kingdom;
Robert E MintoDepartment of Chemistry and Chemical Biology, Indiana University-Purdue University, Indianapolis, IN 46202;
Rachel E MeltonJohn Innes Centre, Norwich Research Park, Norwich NR4 7UH, United Kingdom;
Richard K HughesJohn Innes Centre, Norwich Research Park, Norwich NR4 7UH, United Kingdom;ORCID 0000-0001-9910-6566
Paul E O'MailleJohn Innes Centre, Norwich Research Park, Norwich NR4 7UH, United Kingdom; Food & Health Programme, Institute of Food Research, Norwich Research Park, Norwich NR4 7UH, United Kingdom;
Andrew M HemmingsSchool of Chemistry, University of East Anglia, Norwich NR4 7TJ, United Kingdom; School of Biological Sciences, University of East Anglia, Norwich NR4 7TJ, United Kingdom.
Anne OsbournJohn Innes Centre, Norwich Research Park, Norwich NR4 7UH, United Kingdom; anne.osbourn@jic.ac.uk.
John Innes Centre · GBIndiana University – Purdue University Indianapolis · USUniversity of East Anglia · GB

Funding

Biotechnology and Biological Sciences Research Council BB/L014130/1Biotechnology and Biological Sciences Research Council BBS/E/J/00000614
6 · The paper itself

Abstract

Triterpenes are structurally complex plant natural products with numerous medicinal applications. They are synthesized through an origami-like process that involves cyclization of the linear 30 carbon precursor 2,3-oxidosqualene into different triterpene scaffolds. Here, through a forward genetic screen in planta, we identify a conserved amino acid residue that determines product specificity in triterpene synthases from diverse plant species. Mutation of this residue results in a major change in triterpene cyclization, with production of tetracyclic rather than pentacyclic products. The mutated enzymes also use the more highly oxygenated substrate dioxidosqualene in preference to 2,3-oxidosqualene when expressed in yeast. Our discoveries provide new insights into triterpene cyclization, revealing hidden functional diversity within triterpene synthases. They further open up opportunities to engineer novel oxygenated triterpene scaffolds by manipulating the precursor supply.

Indexed as

Amino AcidsAmino Acid SequenceAvenaConserved SequenceCyclizationIntramolecular TransferasesModels, MolecularMolecular StructureMutationPlant ProteinsProtein DomainsSequence Homology, Amino AcidSubstrate SpecificityTriterpenes2,3-oxidosqualene-beta-amyrin-cyclaseAmino AcidsIntramolecular TransferasesPlant ProteinsTriterpenescyclizationmutantsnatural productsplant defenseterpenes

Identifiers

PMID27412861
PMCPMC4968742
OpenAlexW2463962543

What OpenQuestion holds

Textmetadata
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.