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

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.

Source

Liskova, V., Stepankova, V., Bednar, D., Brezovsky, J., Prokop, Z., Chaloupkova, R., Damborsky, J.: 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, 2017.


sign in

E-mail:
Password:   

Create new user account

Forgot your password? Please contact us at caver@caver.cz.

HANDS-ON COMPUTATIONAL ENZYME DESIGN COURSE

user statistics

1219 citations
6405 registered users
112037x CAVER downloaded

news

CAVER was cited in NATURE Communications paper entitled Molecular mechanism underlying regulation of...

Read more

June 22, 2023

CAVER was recently cited by the NATURE publication entitled Structural basis of the binding of DNP...

Read more

May 14, 2023

CAVER was recently cited in Nature in paper In situ architecture of the ER–mitochondria encounter...

Read more


other tools

acknowledgement