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Enhancing Activity and Controlling Stereoselectivity in a Designed PLP‐Dependent Aldolase
Author(s) -
Toscano Miguel D.,
Müller Manuel M.,
Hilvert Donald
Publication year - 2007
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.200700710
Subject(s) - aldolase a , stereoselectivity , selectivity , chemistry , stereochemistry , active site , pyridoxal phosphate , biochemistry , directed evolution , mutagenesis , enzyme , gene , cleavage (geology) , computational biology , combinatorial chemistry , biology , mutation , mutant , cofactor , paleontology , fracture (geology) , catalysis
Chop and change : Site‐directed mutagenesis has been employed to optimize the activity of an engineered pyridoxal phosphate‐dependent aldolase and to invert its inherent threo selectivity in the cleavage of D ‐β‐phenylserines. The modification of the active‐site residues generates significant retroaldol activity that compares favorably with that of natural enzymes in terms of efficiency and selectivity.