Evidence map›Paper›PMID 26842837›Full record

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

Identification of amino acid networks governing catalysis in the closed complex of class I terpene synthases.

Patrick Schrepfer, Alexander Buettner, Christian Goerner, Michael Hertel, Jeaphianne van Rijn, Frank Wallrapp, Wolfgang Eisenreich, Volker Sieber, Robert Kourist, Thomas Brück

Abstract 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 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing 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

35 citing papers in PubMed.

  1. Article
  2. Article
  3. Review
  4. Article
  5. On the Role of Hydrogen Migrations in the Taxadiene System.Angewandte Chemie (International ed. in English) · 2025
    Article
  6. Review
  7. Article
  8. Article
  9. Review
  10. A diterpene synthase from the sandflyProceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. Molecular Determinants of Carbocation Cyclisation in Bacterial Monoterpene Synthases.Chembiochem : a European journal of chemical biology · 2022
    Article
  16. Article
  17. Article
  18. Article
  19. Review
  20. Review
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.

Patrick SchrepferDivision for Industrial Biocatalysis, Technische Universität München, 85748 Garching, Germany;ORCID http://orcid.org/0000-0003-1708-9630
Alexander BuettnerDivision for Industrial Biocatalysis, Technische Universität München, 85748 Garching, Germany;
Christian GoernerDivision for Industrial Biocatalysis, Technische Universität München, 85748 Garching, Germany;
Michael HertelDivision for Industrial Biocatalysis, Technische Universität München, 85748 Garching, Germany;
Jeaphianne van RijnDepartment of Theoretical Chemistry, Max-Planck-Institut für Kohlenforschung, 45470 Mülheim an der Ruhr, Germany;
Frank WallrappChair of Bioinformatics and Computational Biology, Technische Universität München, 85748 Garching, Germany;
Wolfgang EisenreichChair of Biochemistry, Technische Universität München, 85748 Garching, Germany;
Volker SieberChair of Chemistry of Biogenic Resources, Technische Universität München, 94315 Straubing, Germany;
Robert KouristJunior Research Group for Microbial Biotechnology, Ruhr-Universität Bochum, 44780 Bochum, Germany.
Thomas BrückDivision for Industrial Biocatalysis, Technische Universität München, 85748 Garching, Germany; brueck@tum.de.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Class I terpene synthases generate the structural core of bioactive terpenoids. Deciphering structure-function relationships in the reactive closed complex and targeted engineering is hampered by highly dynamic carbocation rearrangements during catalysis. Available crystal structures, however, represent the open, catalytically inactive form or harbor nonproductive substrate analogs. Here, we present a catalytically relevant, closed conformation of taxadiene synthase (TXS), the model class I terpene synthase, which simulates the initial catalytic time point. In silico modeling of subsequent catalytic steps allowed unprecedented insights into the dynamic reaction cascades and promiscuity mechanisms of class I terpene synthases. This generally applicable methodology enables the active-site localization of carbocations and demonstrates the presence of an active-site base motif and its dominating role during catalysis. It additionally allowed in silico-designed targeted protein engineering that unlocked the path to alternate monocyclic and bicyclic synthons representing the basis of a myriad of bioactive terpenoids.

Indexed as

Models, MolecularAlkyl and Aryl TransferasesAmino Acid MotifsCatalysisCatalytic DomainSequence Analysis, ProteinAlkyl and Aryl Transferasesterpene synthaseclosed complex modelingcomputational biologyprotein engineeringterpene synthase catalysisterpene synthases

Identifiers

PMID26842837
PMCPMC4776449

What OpenQuestion holds

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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.