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Structural determinants of reductive terpene cyclization in iridoid biosynthesis

DOI: 10.1038/nchembio.1955 DOI Help
PMID: 26551396 PMID Help

Authors: Hajo Kries (John Innes Centre) , Lorenzo Caputi (John Innes Centre) , Clare E M Stevenson (John Innes Centre) , Mohammed O Kamileen (John Innes Centre) , Nathaniel H Sherden (John Innes Centre) , Fernando Geu-Flores (University of Copenhagen) , David Lawson (John Innes Centre) , Sarah E O'Connor (John Innes Centre)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Nature Chemical Biology

State: Published (Approved)
Published: November 2015

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.

Journal Keywords: Enzyme Mechanisms; Metabolic Pathways; Plant Sciences

Diamond Keywords: Enzymes

Subject Areas: Biology and Bio-materials, Chemistry


Instruments: I03-Macromolecular Crystallography , I04-1-Macromolecular Crystallography (fixed wavelength) , I04-Macromolecular Crystallography

Added On: 18/11/2015 14:08

Discipline Tags:

Biochemistry Chemistry Structural biology Life Sciences & Biotech

Technical Tags:

Diffraction Macromolecular Crystallography (MX)