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

NMR chemical shift assignments are reported for backbone ( 15 N, 1 H) and partial side chain ( 13 Cα and β, side chain 1 H) atoms of diisopropyl fluorophosphatase (DFPase), a calcium-dependent phosphotriesterase capable of hydrolyzing phosphorus – fluorine bonds in a variety of toxic organophosphoru...

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Bibliographic Details
Published in:Biomolecular NMR assignments 2023-06, Vol.17 (1), p.55-60
Main Authors: Chen, Julian C.-H., Tonelli, Marco, Anderson, Penelope, Michalczyk, Ryszard, Blum, Marc-Michael, Williams, Robert F.
Format: Article
Language:English
Subjects:
Animals
Biochemistry
Biological and Medical Physics
Biophysics
Calcium
Loligo - metabolism
NMR
Nuclear magnetic resonance
Nuclear Magnetic Resonance, Biomolecular
Organophosphorus compounds
Organophosphorus Compounds - chemistry
Organophosphorus Compounds - metabolism
Phosphoric Triester Hydrolases - chemistry
Phosphoric Triester Hydrolases - metabolism
Phosphotriesterase
Physics
Physics and Astronomy
Polymer Sciences
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Summary:NMR chemical shift assignments are reported for backbone ( 15 N, 1 H) and partial side chain ( 13 Cα and β, side chain 1 H) 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.
ISSN:1874-2718
1874-270X
DOI:10.1007/s12104-023-10120-y