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
6200 registered users
111673x CAVER downloaded

news

September 19, 2022

CAVER tool was recently cited in the publication O2-tolerant CO dehydrogenase via tunnel redesign...

Read more

CAVER was cited by the paper The involvement of CYP1A2 in biodegradation of dioxins in pigs,...

Read more

CAVER was recently cited by the article The coupling mechanism of mammalian mitochondrial complex I,...

Read more


other tools

acknowledgement