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Enantiocomplementary Enzymes: Classification, Molecular Basis for Their Enantiopreference, and Prospects for Mirror‐Image Biotransformations
Author(s) -
Mugford Paul F.,
Wagner Ulrike G.,
Jiang Yun,
Faber Kurt,
Kazlauskas Romas J.
Publication year - 2008
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.200705159
Subject(s) - enzyme , biocatalysis , enantiomer , active site , stereochemistry , mirror image , chemistry , image (mathematics) , optically active , molecule , catalysis , biochemistry , physics , computer science , reaction mechanism , organic chemistry , optics , artificial intelligence
One often‐cited weakness of biocatalysis is the lack of mirror‐image enzymes for the formation of either enantiomer of a product in asymmetric synthesis. Enantiocomplementary enzymes exist as the solution to this problem in nature. These enzyme pairs, which catalyze the same reaction but favor opposite enantiomers, are not mirror‐image molecules; however, they contain active sites that are functionally mirror images of one another. To create mirror‐image active sites, nature can change the location of the binding site and/or the location of key catalytic groups. In this Minireview, X‐ray crystal structures of enantiocomplementary enzymes are surveyed and classified into four groups according to how the mirror‐image active sites are formed.