Structural insights into the ene-­‐reductase synthesis of Profens

John Waller, Helen Toogood, Vijaykumar Karuppiah, Nicholas Rattray, David Mansell, David Leys, John Gardiner, Anna Fryszkowska, S.T Ahmed, R Bandichhor, G.P Reddy, Nigel Scrutton

Research output: Contribution to journalArticlepeer-review


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.
Original languageEnglish
JournalOrganic and Biomolecular Chemistry
Early online date28 Apr 2017
Publication statusPublished - 2017

Research Beacons, Institutes and Platforms

  • Manchester Institute of Biotechnology


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