| 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 |
| Gene_locus | psefl-este |
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