期刊
NATURE CHEMICAL BIOLOGY
卷 12, 期 1, 页码 6-+出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/nchembio.1955
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资金
- European Research Council [ERC R20359]
- BBSRC Institute Strategic Programme grant (MET) [BB/J004561/1]
- SNF Early Postdoc Mobility Fellowship
- Biotechnology and Biological Sciences Research Council [BB/J009091/1, BBS/E/J/000CA512] Funding Source: researchfish
- BBSRC [BBS/E/J/000CA512, BB/J009091/1] Funding Source: UKRI
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 5 beta-reductase are highlighted.
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