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Author Spotlight: Developing Tools to Tune the Activity of Tyrosine Phosphatases
Published on: September 6, 2024
Improved stability and half-life of fluorinated phosphotriesterase using Rosetta
Ching-Yao Yang1, P Douglas Renfrew, Andrew J Olsen
1Department of Chemical and Biomolecular Engineering, New York University Polytechnic School of Engineering, 6 Metrotech, Brooklyn, NY 11201 (USA).
Abstract:
Recently we demonstrated that incorporating p-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.

