Backbone and side chain chemical shift assignment of diisopropyl fluorophosphatase (DFPase) from Loligo vulgaris, an organophosphorus-degrading enzyme

Abstract

NMR chemical shift assignments are reported for backbone (¹⁵N, ¹H) and partial side chain (¹³Cα and β, side chain ¹H) atoms of diisopropyl fluorophosphatase (DFPase), a calcium-dependent phosphotriesterase capable of hydrolyzing phosphorus - fluorine bonds in a variety of toxic organophosphorus compounds. Analysis of residues lining the active site of DFPase highlight a number of residues whose chemical shifts can be used as a diagnostic of binding and detection of organophosphorus compounds.

Keywords: Enzyme; Metalloenzyme; NMR chemical shifts; NMR resonance assignments; Organophosphorus.