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Tetrahedron. 2012 Sep 16;68(37):7619-7623.

Asymmetric bioreduction of activated carbon-carbon double bonds using Shewanella yellow enzyme (SYE-4) as novel enoate reductase.

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  • 1Institute of Applied Synthetic Chemistry, Vienna University of Technology, Getreidemarkt 9, 163-OC, A-1060 Vienna, Austria.

Abstract

Shewanella yellow enzyme (SYE-4), a novel recombinant enoate reductase, was screened against a variety of different substrates bearing an activated double bond, such as unsaturated cyclic ketones, diesters, and substituted imides. Dimethyl- and ethyl esters of 2-methylmaleic acid were selectively reduced to (R)-configured succinic acid derivatives and various N-substituted maleimides furnished the desired (R)-products in up to >99% enantiomeric excess. Naturally occurring (+)-carvone was selectively reduced to (-)-cis-dihydrocarvone and (-)-carvone was converted to the diastereomeric product, respectively. Overall SYE-4 proved to be a useful biocatalyst for the selective reduction of activated C 000000000000 000000000000 000000000000 111111111111 000000000000 111111111111 000000000000 000000000000 000000000000 C double bonds and complements the pool of synthetic valuable enoate reductases.

PMID:
22991485
PMCID:
PMC3415682
DOI:
10.1016/j.tet.2012.05.092
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