Conversion of substrate analogs suggests a Michael cyclization in iridoid biosynthesis.
| Autor: | Lindner S; Department of Biological Chemistry, The John Innes Centre, Norwich NR4 7UH, UK; Institute of Organic Chemistry, Karlsruhe Institute of Technology, Fritz-Haber-Weg 6, 76131 Karlsruhe, Germany., Geu-Flores F; Institute of Organic Chemistry, Karlsruhe Institute of Technology, Fritz-Haber-Weg 6, 76131 Karlsruhe, Germany., Bräse S; Institute of Organic Chemistry, Karlsruhe Institute of Technology, Fritz-Haber-Weg 6, 76131 Karlsruhe, Germany; Institute of Toxicology and Genetics, Hermann-von-Helmholtz-Platz 1, 76344 Eggenstein-Leopoldshafen, Germany., Sherden NH; Department of Biological Chemistry, The John Innes Centre, Norwich NR4 7UH, UK. Electronic address: nat.sherden@jic.ac.uk., O'Connor SE; Department of Biological Chemistry, The John Innes Centre, Norwich NR4 7UH, UK. Electronic address: sarah.oconnor@jic.ac.uk. |
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| Jazyk: | angličtina |
| Zdroj: | Chemistry & biology [Chem Biol] 2014 Nov 20; Vol. 21 (11), pp. 1452-6. Date of Electronic Publication: 2014 Oct 23. |
| DOI: | 10.1016/j.chembiol.2014.09.010 |
| Abstrakt: | The core structure of the iridoid monoterpenes is formed by a unique cyclization reaction. The enzyme that catalyzes this reaction, iridoid synthase, is mechanistically distinct from other terpene cyclases. Here we describe the synthesis of two substrate analogs to probe the mechanism of iridoid synthase. Enzymatic assay of these substrate analogs along with clues from the product profile of the native substrate strongly suggest that iridoid synthase utilizes a Michael reaction to achieve cyclization. This improved mechanistic understanding will facilitate the exploitation of the potential of iridoid synthase to synthesize new cyclic compounds from nonnatural substrates. (Copyright © 2014 The Authors. Published by Elsevier Ltd.. All rights reserved.) |
| Databáze: | MEDLINE |
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