期刊
ORGANIC & BIOMOLECULAR CHEMISTRY
卷 15, 期 20, 页码 4440-4448出版社
ROYAL SOC CHEMISTRY
DOI: 10.1039/c7ob00163k
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资金
- UK Biotechnology and Biological Sciences Research Council [BB/I015779/1]
- Centre for Synthetic Biology of Fine and Speciality Chemicals (SynBioChem) [BBSRC: BB/M017702/1]
- Dr Reddy's Laboratories
- EPSRC [EP/J020192/1] Funding Source: UKRI
- Engineering and Physical Sciences Research Council [EP/J020192/1] Funding Source: researchfish
Reduction of double bonds of alpha, beta-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.
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