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 (2016) Structural determinants of reductive terpene cyclization in iridoid biosynthesis. Nat Chem Biol 12(1), 6-8. PubMed

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 5β-reductase are highlighted.

HKI-Autoren
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doi: 10.1038/nchembio.1955 PMID: 26551396