3-D structure of enzyme critical to creation of anticancer compounds in plants identified

November 9, 2015, John Innes Centre
The biosynthesis of iridoids, a class of bicyclic monoterpenes, features an atypical cyclization reaction catalyzed by iridoid synthase (ISY). Crystallographic and biochemical characterization of ISY from Catharanthus roseus provides insights into the ISY enzymatic mechanism and highlights similarities with the homologous progesterone 5β-reductase. Credit: The John Innes Centre

Scientists identify 3D structure of enzyme critical to the creation of anticancer and antimalarial compounds in plants

In a paper published today in Nature Chemical Biology, Professor Sarah O'Connor and Dr Dave Lawson have identified, for the first time, the 3D structure of the enzyme iridoid synthase responsible for a very specific form of cyclisation of monoterpenes which creates anticancer and .

The enzyme iridoid synthase plays a crucial role in the biosynthesis of a large class of plant natural products, the iridoids. Iridoids are the starting precursors for a large group of products such as the anticancer agent vinblastine, the antimalarial quinine and the of catnip. Iridoid synthase generates the core of iridoid natural products by cyclizing a monoterpene precursor in a mode that is fundamentally different from other enzymes acting on monoterpenes.

The first gene of an iridoid synthase has only recently been discovered. In their paper they report the three-D structure of this which provides more detailed information on the mechanism of iridoid synthase.

Explore further: Gateway enzyme for chemicals from catnip to cancer drug

More information: Structural determinants of reductive terpene cyclization in iridoid biosynthesis, Nature Chemical Biology, DOI: 10.1038/nchembio.1955

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