Structural basis for enantiomer binding and separation of a common beta-blocker: Crystal structure of cellobiohydrolase Cel7A with bound (S)-propranolol at 1.9 angstrom resolution

Abstract

By using cellobiose as a selective competing ligand, the retention of the enantiomers of propranolol on the chiral stationary phase (CSP) based on Cel7A mutant D214N were resolved into enantioselective and non-selective binding. The enantioselective binding was weaker for both enantiomers on D214N-CSP than on wild-type-CSP. (C) 2001 Academic Press.

Keywords

cellobiohydrolase; cellulase; chiral separation; crystal structure; enantiomer

Published in

Journal of Molecular Biology
2001, volume: 305, number: 1, pages: 79-93
Publisher: ACADEMIC PRESS LTD

SLU Authors

• Ståhlberg, Jerry

  • Uppsala University

UKÄ Subject classification

Molecular Biology
Structural Biology
Biochemistry

Publication identifier

• DOI: https://doi.org/10.1006/jmbi.2000.4237

Permanent link to this page (URI)

https://res.slu.se/id/publ/53164