| Autor: |
Waller, J., Toogood, H. S., Karuppiah, V., Rattray, N. J. W., Mansell, D. J., Leys, D., Gardiner, J. M., Fryszkowska, A., Ahmed, S. T., Bandichhor, R., Reddy, G. P., Scrutton, N. S. |
| Jazyk: |
angličtina |
| Rok vydání: |
2017 |
| Předmět: |
|
| ISSN: |
1477-0520 |
| Popis: |
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. |
| Databáze: |
OpenAIRE |
| Externí odkaz: |
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