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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Hertel, Michael Buettner, Alexander Eisenreich, Wolfgang Schrepfer, Patrick Brück, Thomas Goerner, Christian Wallrapp, Frank Van Rijn, Jeaphianne Sieber, Volker Kourist, Robert |
| Description | Author Affiliation: Schrepfer P ( Division for Industrial Biocatalysis, Technische Universität München, 85748 Garching, Germany); Buettner A ( Division for Industrial Biocatalysis, Technische Universität München, 85748 Garching, Germany); Goerner C ( Division for Industrial Biocatalysis, Technische Universität München, 85748 Garching, Germany); Hertel M ( Division for Industrial Biocatalysis, Technische Universität München, 85748 Garching, Germany); van Rijn J ( Department of Theoretical Chemistry, Max-Planck-Institut für Kohlenforschung, 45470 Mülheim an der Ruhr, Germany); Wallrapp F ( Chair of Bioinformatics and Computational Biology, Technische Universität München, 85748 Garching, Germany); Eisenreich W ( Chair of Biochemistry, Technische Universität München, 85748 Garching, Germany); Sieber V ( Chair of Chemistry of Biogenic Resources, Technische Universität München, 94315 Straubing, Germany); Kourist R ( Junior Research Group for Microbial Biotechnology, Ruhr-Universität Bochum, 44780 Bochum, Germany.); Brück T ( Division for Industrial Biocatalysis, Technische Universität München, 85748 Garching, Germany); |
| 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. |
| ISSN | 00278424 |
| e-ISSN | 10916490 |
| Journal | Proceedings of the National Academy of Sciences of the United States of America |
| Issue Number | 8 |
| Volume Number | 113 |
| Language | English |
| Publisher | National Academy of Sciences |
| Publisher Date | 2016-02-01 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | Alkyl And Aryl Transferases Chemistry Models, Molecular Sequence Analysis, Protein Amino Acid Motifs Catalysis Catalytic Domain Research Support, Non-U.S. Gov't Multidisciplinary |
| Content Type | Text |
| Resource Type | Article |
| Subject | Multidisciplinary |
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