Engineering Enzyme Stability and Resistance to an Organic Cosolvent by Modification of Residues in the Access Tunnel1. Issue 7 (9th January 2013)

• Record Type: Journal Article
• Authors: Koudelakova, Tana; Chaloupkova, Radka; Brezovsky, Jan; Prokop, Zbynek; Sebestova, Eva; Hesseler, Martin; Khabiri, Morteza; Plevaka, Maryia; Kulik, Daryna; Kuta Smatanova, Ivana; Rezacova, Pavlina; Ettrich, Rudiger; Bornscheuer, Uwe T.; Damborsky, Jiri
• Is Part Of: Angewandte Chemie international edition. Volume 52:Issue 7(2013)
• Page Start: 1959
• Page End: 1963
• Publication Date: 2013-01-09
• Subjects: Chemistry -- Periodicals; 540
• DOI: 10.1002/anie.201206708
• Languages: English
• ISSNs: 1433-7851

Abstract

<abstract abstract-type="graphical" xml:lang="en"> <title> <x xml:space="preserve">Abstract</x> </title> <p> <bold>Mutations</bold> 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).<boxed-text content-type="graphic" position="anchor" orientation="portrait"><graphic position="anchor" mimetype="image" xlink:href="ark:/27927/pgg1v4b10v7" orientation="portrait" xlink:type="simple" xmlns:xlink="http://www.w3.org/1999/xlink" /></boxed-text></p> </abstract>