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Asymmetric Bioreduction of Activated Alkenes Using Cloned 12‐Oxophytodienoate Reductase Isoenzymes OPR‐1 and OPR‐3 from Lycopersicon esculentum (Tomato): A Striking Change of Stereoselectivity
Author(s) -
Hall Mélanie,
Stueckler Clemens,
Kroutil Wolfgang,
Macheroux Peter,
Faber Kurt
Publication year - 2007
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.200605168
Subject(s) - lycopersicon , chemistry , stereoselectivity , reductase , isozyme , substrate (aquarium) , stereochemistry , enantiomeric excess , enantiomer , enantioselective synthesis , enzyme , botany , catalysis , biochemistry , biology , ecology
Tomato source : 12‐Oxophytodienoate reductase isoenzymes OPR1 and OPR3 from tomato possess a broad substrate spectrum for the asymmetric bioreduction of α,β‐unsaturated enals, enones, dicarboxylic acids, and N‐substituted maleimides (see scheme). Stereocomplementary behavior of both isoenzymes was observed in the reduction of a nitroalkene that led to the formation of opposite stereoisomers in high enantiomeric excess.