Improved Stability and Half‐Life of Fluorinated Phosphotriesterase Using Rosetta. Issue 12 (25th July 2014)

• Record Type: Journal Article
• Authors: Yang, Ching‐Yao; Renfrew, P. Douglas; Olsen, Andrew J.; Zhang, Michelle; Yuvienco, Carlo; Bonneau, Richard; Montclare, Jin Kim
• Is Part Of: Chembiochem. Volume 15:Issue 12(2014)
• Page Start: 1761
• Page End: 1764
• Publication Date: 2014-07-25
• Subjects: Biochemistry -- Periodicals; Molecular biology -- Periodicals; Pharmaceutical chemistry -- Periodicals; 572
• DOI: 10.1002/cbic.201402062
• Languages: English
• ISSNs: 1439-4227

Abstract

<abstract abstract-type="main" xml:lang="en"> <title>Abstract</title> <p>Recently we demonstrated that incorporating <italic>p</italic>‐fluorophenylalanine (pFF) into phosphotriesterase dramatically improved folding, thereby leading to enhanced stability and function at elevated temperatures. To further improve the stability of the fluorinated enzyme, Rosetta was used to identify multiple potential stabilizing mutations. One such variant, pFF‐F104A, exhibited enhanced activity at elevated temperature and maintained activity over many days in solution at room temperature.</p> </abstract>