title: Improved stability and half-life of fluorinated phosphotriesterase using Rosetta.
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.
authors: Department of Chemical and Biomolecular Engineering, New York University Polytechnic School of Engineering, 6 Metrotech, Brooklyn, NY 11201 (USA).
authors: Ching-Yao
authors: CY
authors: Yang
authors: P Douglas
authors: PD
authors: Renfrew
authors: Andrew J
authors: AJ
authors: Olsen
authors: Michelle
authors: M
authors: Zhang
authors: Carlo
authors: C
authors: Yuvienco
authors: Richard
authors: R
authors: Bonneau
authors: Jin Kim
authors: JK
authors: Montclare
mesh_terms: D000596:Amino Acids / Q000737:chemistry / Q000378:metabolism; D004795:Enzyme Stability; D006207:Half-Life; D054879:Halogenation; D008958:Models, Molecular; D009154:Mutation; D044345:Phosphoric Triester Hydrolases / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D013696:Temperature; D010135:p-Fluorophenylalanine / Q000737:chemistry / Q000378:metabolism*
chemical_list: D000596:Amino Acids; D010135:p-Fluorophenylalanine; D044345:Phosphoric Triester Hydrolases
keywords: amino acids; biosynthesis; computational design; half-life; noncanonical amino acids; stability