title: Asymmetric bioreduction of activated carbon-carbon double bonds using Shewanella yellow enzyme (SYE-4) as novel enoate reductase.
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 = C double bonds and complements the pool of synthetic valuable enoate reductases.
authors.affiliation: Institute of Applied Synthetic Chemistry, Vienna University of Technology, Getreidemarkt 9, 163-OC, A-1060 Vienna, Austria.
authors.forename: Naseem
authors.initials: N
authors.lastname: Iqbal
authors.forename: Florian
authors.initials: F
authors.lastname: Rudroff
authors.forename: Ann
authors.initials: A
authors.lastname: Brigé
authors.forename: Jozef
authors.initials: J
authors.lastname: Van Beeumen
authors.forename: Marko D
authors.initials: MD
authors.lastname: Mihovilovic