Jochens_2009_Angew.Chem.Int.Ed.Engl_48_3532

Reference

Title : Converting an esterase into an epoxide hydrolase - Jochens_2009_Angew.Chem.Int.Ed.Engl_48_3532
Author(s) : Jochens H , Stiba K , Savile C , Fujii R , Yu JG , Gerassenkov T , Kazlauskas RJ , Bornscheuer UT
Ref : Angew Chem Int Ed Engl , 48 :3532 , 2009
Abstract :

Entering the fold: A common structural motif in hydrolytic enzymes is the alpha,beta-hydrolase fold. The interconversion of one enzyme into another by introduction of mechanistically important residues is not enough; only substitution of a loop allows epoxide hydrolase activity in the esterase scaffold to be formed (see picture; structure comparison of epoxide hydrolases (green) with the esterase (orange)). The result is an enantioselective chimeric enzyme.

PubMedSearch : Jochens_2009_Angew.Chem.Int.Ed.Engl_48_3532
PubMedID: 19350592
Gene_locus related to this paper: psefl-este

Related information

Gene_locus psefl-este

Citations formats

Jochens H, Stiba K, Savile C, Fujii R, Yu JG, Gerassenkov T, Kazlauskas RJ, Bornscheuer UT (2009)
Converting an esterase into an epoxide hydrolase
Angew Chem Int Ed Engl 48 :3532

Jochens H, Stiba K, Savile C, Fujii R, Yu JG, Gerassenkov T, Kazlauskas RJ, Bornscheuer UT (2009)
Angew Chem Int Ed Engl 48 :3532