Different Structural Origins of the Enantioselectivity of Haloalkane Dehalogenases toward Linear β-Haloalkanes: Open–Solvated versus Occluded–Desolvated Active Sites

Authors

Liskova, V., Stepankova, V., Bednar, D., Brezovsky, J., Prokop, Z., Chaloupkova, R., Damborsky, J.

Source

ANGEWANDTE CHEMIE INTERNATIONAL EDITION 56: 4719-4723 (2017)

Abstract

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.

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Citation

Liskova, V., Stepankova, V., Bednar, D., Brezovsky, J., Prokop, Z., Chaloupkova, R., Damborsky, J., 2017: Different Structural Origins of the Enantioselectivity of Haloalkane Dehalogenases toward Linear β-Haloalkanes: Open–Solvated versus Occluded–Desolvated Active Sites. Angewandte Chemie International Edition 56: 4719-4723.

Martin Toul Awarded Rector’s Award
Seminar with Prof. Ing. Stepan Podzimek from SYNPO, a.s.
Success at Vernadsky Contest for Jan Cesnek
Interview with Profs. Damborsky and Prokop
Prof. Donald Hilvert to Give Lectute at Masaryk University
New Postdoc Position for Bryja & Damborsky Labs
Prof. deMello to Give Lecture at MU