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

摘要

Cellobiohydrolase Cel7A (previously called CBH 1), the major cellulase produced by the mould fungus Trichoderma reesei, has been successfully exploited as a chiral selector for separation of stereo-isomers of some important pharmaceutical compounds, e.g. adrenergic beta -blockers. Previous investigations, including experiments with catalytically deficient mutants of Cel7A, point unanimously to the active site as being responsible for discrimination of enantiomers.