Structural determinants of reductive terpene cyclization in iridoid biosynthesis

Kries, Hajo; Caputi, Lorenzo; Stevenson, Clare E. M.; Kamileen, Mohammed O.; Sherden, Nathaniel H.; Geu-Flores, Fernando; Lawson, David M.; O'Connor, Sarah E.

doi:10.1038/nchembio.1955

Item

ITEM ACTIONSEXPORT

Add to Basket

Local TagsRelease HistoryDetailsSummary

Released

Journal Article

Structural determinants of reductive terpene cyclization in iridoid biosynthesis

MPS-Authors

There are no MPG-Authors in the publication available

External Resource

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4685742/
(Publisher version)

Fulltext (restricted access)

There are currently no full texts shared for your IP range.

Fulltext (public)

There are no public fulltexts stored in PuRe

Supplementary Material (public)

There is no public supplementary material available

Citation

Kries, H., Caputi, L., Stevenson, C. E. M., Kamileen, M. O., Sherden, N. H., Geu-Flores, F., et al. (2016). Structural determinants of reductive terpene cyclization in iridoid biosynthesis. Nature Chemical Biology, 12(1), 6-8. doi:10.1038/nchembio.1955.

Cite as: https://hdl.handle.net/21.11116/0000-0002-B896-5

Abstract

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.