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

Sammanfattning

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.

Nyckelord

cellobiohydrolase; cellulase; chiral separation; crystal structure; enantiomer

Publicerad i

Journal of Molecular Biology
2001, volym: 305, nummer: 1, sidor: 79-93
Utgivare: ACADEMIC PRESS LTD

SLU författare

• Ståhlberg, Jerry

  • Uppsala universitet

UKÄ forskningsämne

Molekylärbiologi
Strukturbiologi
Biokemi

Publikationens identifierare

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

Permanent länk till denna sida (URI)

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