Enantiocomplementary Enzymes: Classification, Molecular Basis for Their Enantiopreference, and Prospects for Mirror-Image Biotransformations
Paul F. Mugford Dr.
Department of Biochemistry, Molecular Biology & Biophysics and the Biotechnology Institute, University of Minnesota, 1479 Gortner Avenue, Saint Paul, MN 55108 (USA), Fax: (+1) 612-625-5780
Search for more papers by this authorUlrike G. Wagner Dr.
Department of Chemistry, University of Graz, Heinrichstrasse 28, 8010 Graz (Austria), Fax: (+43) 316-380-9840
Search for more papers by this authorYun Jiang
Department of Biochemistry, Molecular Biology & Biophysics and the Biotechnology Institute, University of Minnesota, 1479 Gortner Avenue, Saint Paul, MN 55108 (USA), Fax: (+1) 612-625-5780
Search for more papers by this authorKurt Faber Prof. Dr.
Department of Chemistry, University of Graz, Heinrichstrasse 28, 8010 Graz (Austria), Fax: (+43) 316-380-9840
Search for more papers by this authorRomas J. Kazlauskas Prof.
Department of Biochemistry, Molecular Biology & Biophysics and the Biotechnology Institute, University of Minnesota, 1479 Gortner Avenue, Saint Paul, MN 55108 (USA), Fax: (+1) 612-625-5780
Search for more papers by this authorPaul F. Mugford Dr.
Department of Biochemistry, Molecular Biology & Biophysics and the Biotechnology Institute, University of Minnesota, 1479 Gortner Avenue, Saint Paul, MN 55108 (USA), Fax: (+1) 612-625-5780
Search for more papers by this authorUlrike G. Wagner Dr.
Department of Chemistry, University of Graz, Heinrichstrasse 28, 8010 Graz (Austria), Fax: (+43) 316-380-9840
Search for more papers by this authorYun Jiang
Department of Biochemistry, Molecular Biology & Biophysics and the Biotechnology Institute, University of Minnesota, 1479 Gortner Avenue, Saint Paul, MN 55108 (USA), Fax: (+1) 612-625-5780
Search for more papers by this authorKurt Faber Prof. Dr.
Department of Chemistry, University of Graz, Heinrichstrasse 28, 8010 Graz (Austria), Fax: (+43) 316-380-9840
Search for more papers by this authorRomas J. Kazlauskas Prof.
Department of Biochemistry, Molecular Biology & Biophysics and the Biotechnology Institute, University of Minnesota, 1479 Gortner Avenue, Saint Paul, MN 55108 (USA), Fax: (+1) 612-625-5780
Search for more papers by this authorGraphical Abstract
Enzyme pairs that catalyze the same reaction but favor opposite enantiomers are known as enantiocomplementary enzymes (see scheme). To create mirror-image active sites, nature can switch the locations of binding sites and/or the locations of key catalytic groups. In this Minireview, X-ray crystal structures of enantiocomplementary enzymes are surveyed and classified into four groups.
Abstract
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.
Supporting Information
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