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Cover Picture: Increased Enantioselectivity by Engineering Bottleneck Mutants in an Esterase from Pseudomonas fluorescens (ChemBioChem 18/2009)
Author(s) -
Schließmann Anna,
Hidalgo Aurelio,
Berenguer José,
Bornscheuer Uwe T.
Publication year - 2009
Publication title -
chembiochem
Language(s) - English
Resource type - Reports
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.200990082
Subject(s) - active site , pseudomonas fluorescens , mutant , chemistry , substrate (aquarium) , stereochemistry , esterase , site directed mutagenesis , wild type , biochemistry , enzyme , biology , genetics , bacteria , gene , ecology
The cover picture shows ( R )‐1‐phenyl‐2‐propyl acetate docked in the active site of a quadruple mutant (mutant Q) of the Pseudomonas fluorescens esterase I. The four point mutations involved the replacement of four Phe with Leu residues in the area lining the entrance to the active site, which was termed the bottleneck (in blue). Substitutions in this area cause changes in enantioselectivity, both due to direct interaction with the substrate and to restriction of substrate access to the active site. The detail shows the catalytic residues in green, and the bottleneck residues of the wild‐type (in dark red) and of mutant Q (in dark blue) interacting in a clearly different way with ( R )‐1‐phenyl‐2‐propyl acetate (light red and light blue for the interaction with the wild‐type enzyme and mutant Q, respectively). More information can be found on p. 2920 ff, U. Bornscheuer et al. Cover art by J. Belio.