High‐Throughput Screening for Terpene‐Synthase‐Cyclization Activity and Directed Evolution of a Terpene Synthase1. Issue 21 (26th March 2013)

• Record Type: Journal Article
• Authors: Lauchli, Ryan; Rabe, Kersten S.; Kalbarczyk, Karolina Z.; Tata, Amulya; Heel, Thomas; Kitto, Rebekah Z.; Arnold, Frances H.
• Is Part Of: Angewandte Chemie international edition. Volume 52:Issue 21(2013)
• Page Start: 5571
• Page End: 5574
• Publication Date: 2013-03-26
• Subjects: Chemistry -- Periodicals; 540
• DOI: 10.1002/anie.201301362
• Languages: English
• ISSNs: 1433-7851

Abstract

<abstract abstract-type="graphical" xml:lang="en"> <title> <x xml:space="preserve">Abstract</x> </title> <p> <bold>An easy assay</bold>: A synthetic substrate enables a colorimetric screen for terpene synthase cyclization activity, thereby facilitating the engineering of these enzymes. By using directed evolution, the thermostability of a sesquiterpene synthase was increased without the loss of other properties. The technique also enabled rapid optimization of conditions for expression and stabilization in lysate of another terpene synthase. PPO=diphosphate.<boxed-text content-type="graphic" position="anchor" orientation="portrait"><graphic position="anchor" mimetype="image" xlink:href="ark:/27927/pgg1zsx7f2s" orientation="portrait" xlink:type="simple" xmlns:xlink="http://www.w3.org/1999/xlink" /></boxed-text></p> </abstract>