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Cover Picture: Control of Lipase Enantioselectivity by Engineering the Substrate Binding Site and Access Channel (ChemBioChem 17/2009)
Author(s) -
Lafaquière Vincent,
Barbe Sophie,
PuechGuenot Sophie,
Guieysse David,
Cortés Juan,
Monsan Pierre,
Siméon Thierry,
André Isabelle,
RemaudSiméon Magali
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.200990076
Subject(s) - cover (algebra) , substrate (aquarium) , lipase , protein engineering , chemistry , biocatalysis , binding site , combinatorial chemistry , enzyme , biochemistry , engineering , catalysis , biology , reaction mechanism , mechanical engineering , ecology
The cover picture highlights the concept of adapting path‐planning algorithms, originating from robotics, to investigating various molecular‐motion problems, such as the access of R and S enantiomers to the active site of an enzyme. With this technique, both the enzyme and the substrates are modelled as polyarticulated mechanisms. On p. 2760 ff. of this issue, M. Remaud‐Siméon et al. show how the combined use of computational approaches and molecular‐engineering techniques allowed the fast isolation of several mutants of the lipase from Burkholderia cepacia with remarkably enhanced (up to tenfold) or reversed enantioselectivity compared to the wild‐type enzyme. By re‐engineering the deeply buried substrate binding site and access channel of the B. cepacia lipase, highly enantioselective biocatalysts with a 15‐fold enhanced specific activity compared to the parental enzyme were developed for the kinetic resolution of 2‐substituted racemic acids. Model of the Justin Robot from the German Aerospace Center (DLR), Institute of Robotics and Mechatronics.