Research article2001Peer reviewed
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
Ståhlberg, Jerry; Henriksson, Hongbin; Divne, Christina; Isaksson, Roland; Pettersson, Göran; Johansson, Gunnar; Jones, T. Alwyn
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
UKÄ Subject classification
Structural Biology
Biochemistry and Molecular Biology
Publication identifier
DOI: https://doi.org/10.1006/jmbi.2000.4237
Permanent link to this page (URI)
https://res.slu.se/id/publ/53164