Directed evolution and axial chirality: optimization of the enantioselectivity of Pseudomonas aeruginosa lipase towards the kinetic resolution of a racemic allene.
Directed evolution of Pseudomonas aeruginosa lipase by the use of combinatorial active site saturation test (CAST) criteria provided a highly enantioselective mutant (Leu162Phe) for kinetic resolution of an axially chiral allene, p-nitrophenyl 4-cyclohexyl-2-methylbuta-2,3-dienoate (E=111); the high enantioselectivity of the Leu162Phe mutant was rationalized by pi-pi stacking.
Carballeira
José Daniel
JD
Max-Planck-Institut für Kohlenforschung, Kaiser- Wilhelm-Platz 1, D-45470, MülheimlRuhr, Germany.
Krumlinde
Patrik
P
Bocola
Marco
M
Vogel
Andreas
A
Reetz
Manfred T
MT
Bäckvall
Jan E
JE
D000466:Alkadienes / Q000737:chemistry*; D019020:Directed Molecular Evolution; D007700:Kinetics; D008049:Lipase / Q000737:chemistry*; D008954:Models, Biological; D008968:Molecular Conformation; D015394:Molecular Structure; D009154:Mutation; D011550:Pseudomonas aeruginosa / Q000201:enzymology* / Q000235:genetics; D013237:Stereoisomerism
D000466:Alkadienes; C025947:propadiene; D008049:Lipase