Koudelakova_2013_Angew.Chem.Int.Ed.Engl_52_1959

Reference

Title : Engineering enzyme stability and resistance to an organic cosolvent by modification of residues in the access tunnel - Koudelakova_2013_Angew.Chem.Int.Ed.Engl_52_1959
Author(s) : Koudelakova T , Chaloupkova R , Brezovsky J , Prokop Z , Sebestova E , Hesseler M , Khabiri M , Plevaka M , Kulik D , Kuta Smatanova I , Rezacova P , Ettrich R , Bornscheuer UT , Damborsky J
Ref : Angew Chem Int Ed Engl , 52 :1959 , 2013
Abstract :

Mutations targeting as few as four residues lining the access tunnel extended the half-life of an enzyme in 40% dimethyl sulfoxide from minutes to weeks and increased its melting temperature by 190C. Protein crystallography and molecular dynamics revealed that the tunnel residue packing is a key determinant of protein stability and the active-site accessibility for cosolvent molecules (red dots).

PubMedSearch : Koudelakova_2013_Angew.Chem.Int.Ed.Engl_52_1959
PubMedID: 23303607
Gene_locus related to this paper: rhoso-halo1

Related information

Inhibitor Benzoic-acid
Gene_locus rhoso-halo1
Family Haloalkane_dehalogenase-HLD2
Structure 4F5Z    4F60

Citations formats

Koudelakova T, Chaloupkova R, Brezovsky J, Prokop Z, Sebestova E, Hesseler M, Khabiri M, Plevaka M, Kulik D, Kuta Smatanova I, Rezacova P, Ettrich R, Bornscheuer UT, Damborsky J (2013)
Engineering enzyme stability and resistance to an organic cosolvent by modification of residues in the access tunnel
Angew Chem Int Ed Engl 52 :1959

Koudelakova T, Chaloupkova R, Brezovsky J, Prokop Z, Sebestova E, Hesseler M, Khabiri M, Plevaka M, Kulik D, Kuta Smatanova I, Rezacova P, Ettrich R, Bornscheuer UT, Damborsky J (2013)
Angew Chem Int Ed Engl 52 :1959