Enantiocomplementary enzymes: classification, molecular basis for their enantiopreference, and prospects for mirror-image biotransformations.
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.
Department of Biochemistry, Molecular Biology & Biophysics and the Biotechnology Institute, University of Minnesota, 1479 Gortner Avenue, Saint Paul, MN 55108, USA.
Paul F
PF
Mugford
Ulrike G
UG
Wagner
Yun
Y
Jiang
Kurt
K
Faber
Romas J
RJ
Kazlauskas
D001665:Binding Sites; D020134:Catalytic Domain; D004798:Enzymes / Q000737:chemistry / Q000145:classification / Q000378:metabolism*; D017510:Protein Folding; D013237:Stereoisomerism; D013379:Substrate Specificity
D004798:Enzymes