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Tetrahydroxynaphthalene reductase: catalytic properties of an enzyme involved in reductive asymmetric naphthol dearomatization |
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| Authors: | Schätzle Michael A Flemming Stephan Husain Syed Masood Richter Michael Günther Stefan Müller Michael |
| Affiliation: | 1. Institut für Pharmazeutische Wissenschaften, Albert‐Ludwigs‐Universit?t Freiburg, Albertstrasse 25, 79104 Freiburg (Germany);2. Laboratory for Biomaterials, Empa–Swiss Federal Laboratories for Materials Science and Technology, Lerchenfeldstrasse 5, 9014 St.?Gallen (Switzerland) |
| 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. This effect allows the identification of a homologous enzyme. |
| Keywords: | asymmetric synthesis enzyme catalysis molecular modeling structural biology substituent effects |
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