Engineering enzyme stability and resistance to an organic cosolvent by modification of residues in the access tunnel Article

Koudelakova, T, Chaloupkova, R, Brezovsky, J et al. (2013). Engineering enzyme stability and resistance to an organic cosolvent by modification of residues in the access tunnel . ANGEWANDTE CHEMIE-INTERNATIONAL EDITION, 52(7), 1959-1963. 10.1002/anie.201206708

cited authors

  • 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

authors

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 19 °C. 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). Copyright © 2013 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.

publication date

  • February 11, 2013

published in

Digital Object Identifier (DOI)

start page

  • 1959

end page

  • 1963

volume

  • 52

issue

  • 7