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Asymmetric Bioreduction of Activated C=C Bonds Using Zymomonas mobilis NCR Enoate Reductase and Old Yellow Enzymes OYE 1–3 from Yeasts
Author(s) -
Hall Mélanie,
Stueckler Clemens,
Hauer Bernhard,
Stuermer Rainer,
Friedrich Thomas,
Breuer Michael,
Kroutil Wolfgang,
Faber Kurt
Publication year - 2008
Publication title -
european journal of organic chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.825
H-Index - 155
eISSN - 1099-0690
pISSN - 1434-193X
DOI - 10.1002/ejoc.200701208
Subject(s) - zymomonas mobilis , chemistry , stereochemistry , substrate (aquarium) , stereoselectivity , alkene , moiety , aldehyde , enantiomeric excess , biocatalysis , ketone , double bond , reductase , enzyme , enantioselective synthesis , organic chemistry , catalysis , ethanol , reaction mechanism , oceanography , ethanol fuel , geology
The asymmetric bioreduction of C=C‐bonds bearing an electron‐withdrawing group, such as an aldehyde, ketone, imide, nitro, carboxylic acid, or ester moiety by a novel enoate reductase from Zymomonas mobilis and Old Yellow Enzymes OYE 1–3 from yeasts furnished the corresponding saturated products in up to >99 % ee . Depending on the substrate type, stereocontrol was achieved by variation of the substrate structure, by switching the ( E / Z ) geometry of the alkene or by choice of the appropriate enzyme. This substrate‐ orenzyme‐based stereocontrol allowed access to the opposite enantiomeric products.(© Wiley‐VCH Verlag GmbH & Co. KGaA, 69451 Weinheim, Germany, 2008)