Structural highlights
Publication Abstract from PubMed
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 5beta-reductase are highlighted.
Structural determinants of reductive terpene cyclization in iridoid biosynthesis.,Kries H, Caputi L, Stevenson CE, Kamileen MO, Sherden NH, Geu-Flores F, Lawson DM, O'Connor SE Nat Chem Biol. 2015 Nov 9. doi: 10.1038/nchembio.1955. PMID:26551396[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Kries H, Caputi L, Stevenson CE, Kamileen MO, Sherden NH, Geu-Flores F, Lawson DM, O'Connor SE. Structural determinants of reductive terpene cyclization in iridoid biosynthesis. Nat Chem Biol. 2015 Nov 9. doi: 10.1038/nchembio.1955. PMID:26551396 doi:http://dx.doi.org/10.1038/nchembio.1955
