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 | Zendy

Hall Mélanie | Zendy; Stueckler Clemens | Zendy; Kroutil Wolfgang | Zendy; Macheroux Peter | Zendy; Faber Kurt | Zendy

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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.

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