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Structural Basis and Enzymatic Mechanism of the Biosynthesis of C9‐ from C10‐Monoterpenoid Indole Alkaloids |
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| Authors: | Liuqing Yang Marco Hill Dr. Meitian Wang Dr. Santosh Panjikar Dr. Joachim Stöckigt Prof. Dr. |
| Affiliation: | 1. Institute of Materia Medica, College of Pharmaceutical Sciences, Zhejiang University, 383 Yu Hang Tang Road, Hangzhou 310058 (China);2. Lehrstuhl für Pharmazeutische Biologie, Institut für Pharmazie, Johannes‐Gutenberg Universit?t, Staudinger Weg 5, 55128 Mainz (Germany), Fax: (+49)?6131‐392‐3752;3. Swiss Light Source PX III, Paul Scherrer Institute, 5232 Villigen (Switzerland);4. European Molecular Biology Laboratory Hamburg, Outstation Deutsches Elektronen‐Synchrotron, Notkestrasse 85, 22603 Hamburg (Germany) |
| Abstract: | Cutting carbons : The three‐dimensional structure of polyneuridine aldehyde esterase (PNAE) gives insight into the enzymatic mechanism of the biosynthesis of C9‐ from C10‐monoterpenoid indole alkaloids (see scheme). PNAE is a very substrate‐specific serine esterase. It harbors the catalytic triad S87‐D216‐H244, and is a new member of the α/β‐fold hydrolase superfamily. Its novel function leads to the diversification of alkaloid structures.  |
| Keywords: | alkaloids biosynthesis enzyme catalysis esterases protein structures |