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Tetrahydroxynaphthalene Reductase: Catalytic Properties of an Enzyme Involved in Reductive Asymmetric Naphthol Dearomatization

2012; Wiley; Volume: 51; Issue: 11 Linguagem: Inglês

10.1002/anie.201107695

1521-3773

Michael A. Schätzle, Stephan Flemming, Syed Masood Husain, Michael Richter, Stefan Günther, Michael Müller,

Carbohydrate Chemistry and Synthesis

Angewandte Chemie International EditionVolume 51, Issue 11 p. 2643-2646 Communication Tetrahydroxynaphthalene Reductase: Catalytic Properties of an Enzyme Involved in Reductive Asymmetric Naphthol Dearomatization† Michael A. Schätzle, Michael A. Schätzle Institut für Pharmazeutische Wissenschaften, Albert-Ludwigs-Universität Freiburg, Albertstrasse 25, 79104 Freiburg (Germany)Search for more papers by this authorStephan Flemming, Stephan Flemming Institut für Pharmazeutische Wissenschaften, Albert-Ludwigs-Universität Freiburg, Albertstrasse 25, 79104 Freiburg (Germany)Search for more papers by this authorDr. Syed Masood Husain, Dr. Syed Masood Husain Institut für Pharmazeutische Wissenschaften, Albert-Ludwigs-Universität Freiburg, Albertstrasse 25, 79104 Freiburg (Germany)Search for more papers by this authorDr. Michael Richter, Dr. Michael Richter Institut für Pharmazeutische Wissenschaften, Albert-Ludwigs-Universität Freiburg, Albertstrasse 25, 79104 Freiburg (Germany) Laboratory for Biomaterials, Empa–Swiss Federal Laboratories for Materials Science and Technology, Lerchenfeldstrasse 5, 9014 St. Gallen (Switzerland)Search for more papers by this authorDr. Stefan Günther, Dr. Stefan Günther Institut für Pharmazeutische Wissenschaften, Albert-Ludwigs-Universität Freiburg, Albertstrasse 25, 79104 Freiburg (Germany)Search for more papers by this authorProf. Dr. Michael Müller, Corresponding Author Prof. Dr. Michael Müller michael.mueller@pharmazie.uni-freiburg.de Institut für Pharmazeutische Wissenschaften, Albert-Ludwigs-Universität Freiburg, Albertstrasse 25, 79104 Freiburg (Germany)Institut für Pharmazeutische Wissenschaften, Albert-Ludwigs-Universität Freiburg, Albertstrasse 25, 79104 Freiburg (Germany)Search for more papers by this author Michael A. Schätzle, Michael A. Schätzle Institut für Pharmazeutische Wissenschaften, Albert-Ludwigs-Universität Freiburg, Albertstrasse 25, 79104 Freiburg (Germany)Search for more papers by this authorStephan Flemming, Stephan Flemming Institut für Pharmazeutische Wissenschaften, Albert-Ludwigs-Universität Freiburg, Albertstrasse 25, 79104 Freiburg (Germany)Search for more papers by this authorDr. Syed Masood Husain, Dr. Syed Masood Husain Institut für Pharmazeutische Wissenschaften, Albert-Ludwigs-Universität Freiburg, Albertstrasse 25, 79104 Freiburg (Germany)Search for more papers by this authorDr. Michael Richter, Dr. Michael Richter Institut für Pharmazeutische Wissenschaften, Albert-Ludwigs-Universität Freiburg, Albertstrasse 25, 79104 Freiburg (Germany) Laboratory for Biomaterials, Empa–Swiss Federal Laboratories for Materials Science and Technology, Lerchenfeldstrasse 5, 9014 St. Gallen (Switzerland)Search for more papers by this authorDr. Stefan Günther, Dr. Stefan Günther Institut für Pharmazeutische Wissenschaften, Albert-Ludwigs-Universität Freiburg, Albertstrasse 25, 79104 Freiburg (Germany)Search for more papers by this authorProf. Dr. Michael Müller, Corresponding Author Prof. Dr. Michael Müller michael.mueller@pharmazie.uni-freiburg.de Institut für Pharmazeutische Wissenschaften, Albert-Ludwigs-Universität Freiburg, Albertstrasse 25, 79104 Freiburg (Germany)Institut für Pharmazeutische Wissenschaften, Albert-Ludwigs-Universität Freiburg, Albertstrasse 25, 79104 Freiburg (Germany)Search for more papers by this author First published: 03 February 2012 https://doi.org/10.1002/anie.201107695Citations: 43 † Financial support of this work by the Deutsche Forschungsgemeinschaft (IRTG 1038) is gratefully acknowledged. We are grateful to E. Breitling for skillful technical support, to V. Brecht for measurement of NMR spectra, to Dr. S. Lüdeke for VCD measurement, and to Prof. Dr. U. Kück and Prof. Dr. F. J. Leeper for helpful discussions. We acknowledge the use of the computing resources provided by the Black Forest Grid initiative and T. L. Rižner for providing 17β-HSDcl. Read the full textAboutPDF ToolsRequest permissionExport citationAdd to favoritesTrack citation ShareShare Give accessShare full text accessShare full-text accessPlease review our Terms and Conditions of Use and check box below to share full-text version of article.I have read and accept the Wiley Online Library Terms and Conditions of UseShareable LinkUse the link below to share a full-text version of this article with your friends and colleagues. Learn more.Copy URL Share a linkShare onFacebookTwitterLinked InRedditWechat Abstract In reduced circumstances: Tetrahydroxynaphthalene reductase shows a broad substrate range including alternate phenolic compounds and cyclic ketones. Structural modeling reveals major enzyme–substrate interactions; C-terminal truncation of the enzyme causes an altered substrate preference, in accordance with stabilization of the substrate by the C-terminal carboxylate (see picture). This effect allows the identification of a homologous enzyme. Citing Literature Supporting Information Detailed facts of importance to specialist readers are published as "Supporting Information". Such documents are peer-reviewed, but not copy-edited or typeset. They are made available as submitted by the authors. Filename Description anie_201107695_sm_miscellaneous_information.pdf11.9 MB miscellaneous_information Please note: The publisher is not responsible for the content or functionality of any supporting information supplied by the authors. Any queries (other than missing content) should be directed to the corresponding author for the article. Volume51, Issue11March 12, 2012Pages 2643-2646 RelatedInformation