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Biotechnol Bioeng. 2013 Dec;110(12):3085-92. doi: 10.1002/bit.24981. Epub 2013 Jul 10.

Overcoming co-product inhibition in the nicotinamide independent asymmetric bioreduction of activated C=C-bonds using flavin-dependent ene-reductases.

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  • 1Department of Chemistry, Organic and Bioorganic Chemistry, University of Graz, Heinrichstrasse 28, A-8010, Graz, Austria.

Abstract

Eleven flavoproteins from the old yellow enzyme family were found to catalyze the disproportionation ("dismutation") of conjugated enones. Incomplete conversions, which were attributed to enzyme inhibition by the co-product phenol could be circumvented via in situ co-product removal by scavenging the phenol using the polymeric adsorbent MP-carbonate. The optimized system allowed to reduce an alkene activated by ester groups in a "coupled-substrate" approach via nicotinamide-free hydrogen transfer with >90% conversion and complete stereoselectivity.

© 2013 The Authors. Biotechnology and Bioengineering Published by Wiley Periodicals, Inc.

KEYWORDS:

disproportionation; ene-reductase; in situ co-product removal; old yellow enzyme

PMID:
23794404
[PubMed - indexed for MEDLINE]
PMCID:
PMC4034509
Free PMC Article

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