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Different Structural Origins of the Enantioselectivity of Haloalkane Dehalogenases toward Linear β‐Haloalkanes: Open–Solvated versus Occluded–Desolvated Active Sites
Author(s) -
Liskova Veronika,
Stepankova Veronika,
Bednar David,
Brezovsky Jan,
Prokop Zbynek,
Chaloupkova Radka,
Damborsky Jiri
Publication year - 2017
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.201611193
Subject(s) - chemistry , steric effects , enantioselective synthesis , stereochemistry , active site , solvent , enzyme , organic chemistry , catalysis
The enzymatic enantiodiscrimination of linear β‐haloalkanes is difficult because the simple structures of the substrates prevent directional interactions. Herein we describe two distinct molecular mechanisms for the enantiodiscrimination of the β‐haloalkane 2‐bromopentane by haloalkane dehalogenases. Highly enantioselective DbjA has an open, solvent‐accessible active site, whereas the engineered enzyme DhaA31 has an occluded and less solvated cavity but shows similar enantioselectivity. The enantioselectivity of DhaA31 arises from steric hindrance imposed by two specific substitutions rather than hydration as in DbjA.