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I03-Macromolecular Crystallography I24-Microfocus Macromolecular Crystallography	Structural insights into the ene-reductase synthesis of profens John Waller , Helen Toogood , Vijaykumar Karuppiah , Nicholas John William Rattray , David Mansell , David Leys , John M. Gardiner , Anna Fryszkowska , Syed Ahmed , Rakeshwar Bandichhor , Prashanth Reddy Gaddameedhi , Nigel Scrutton Org. Biomol. Chem. DOI: 10.1039/C7OB00163K Diamond Proposal Number(s): [12788] Show Abstract ▼ Abstract: Reduction of double bonds of α,β-unsaturated carboxylic acids and esters by ene-reductases remains challenging and it typically requires activation by a second electron-withdrawing moiety, such as a halide or second carboxylate group. We showed that profen precursors, 2-arylpropenoic acids and their esters, were efficiently reduced by Old Yellow Enzymes (OYEs). The XenA and GYE enzymes showed activity towards acids, while a wider range of enzymes were active towards the equivalent methyl esters. Comparative co-crystal structural analysis of profen-bound OYEs highlighted key interactions important in determining substrate binding in a catalytically active conformation. The general utility of ene reductases for the synthesis of (R)-profens was established and this work will now drive future mutagenesis studies to screen for the production of pharmaceutically-active (S)-profens.	Apr 2017

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