Structural determinants of reductive terpene cyclization in iridoid biosynthesis
Research output: Contribution to journal › Journal article › Research › peer-review
The carbon skeleton of ecologically and pharmacologically important iridoid monoterpenes is formed in a reductive cyclization reaction unrelated to canonical terpene cyclization. Here we report the crystal structure of the recently discovered iridoid cyclase (from Catharanthus roseus) bound to a mechanism-inspired inhibitor that illuminates substrate binding and catalytic function of the enzyme. Key features that distinguish iridoid synthase from its close homolog progesterone 5β-reductase are highlighted.
Original language | English |
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Journal | Nature Chemical Biology |
Volume | 12 |
Issue number | 1 |
Pages (from-to) | 6-8 |
Number of pages | 3 |
ISSN | 1552-4450 |
DOIs | |
Publication status | Published - 2016 |
- Catharanthus, Crystallography, X-Ray, Cyclization, Iridoids, Models, Molecular, Oxidoreductases, Plant Proteins, Protein Conformation, Terpenes, Journal Article, Research Support, Non-U.S. Gov't
Research areas
ID: 164345624