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Literature summary extracted from

  • Chen, J.C.; Mustyakimov, M.; Schoenborn, B.P.; Langan, P.; Blum, M.M.
    Neutron structure and mechanistic studies of diisopropyl fluorophosphatase (DFPase) (2010), Acta Crystallogr. Sect. D, 66, 1131-1138.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.1.8.2 by vapour diffusion using a protein solution with 2 mM protein in 10 mM Tris, pH 7.5, 2 mM CaCl2, against a precipitation solution containing 11% PEG 4000 in 0.1 M MES, pH 6.5, at room temperature, X-ray diffraction structure determination and analysis at 2.2 A resolution. Comparison with structures of enzyme mutants, overview Loligo vulgaris

Protein Variants

EC Number Protein Variants Comment Organism
3.1.8.2 additional information reengineering of DFPase through rational design to bind and productively orient the more toxic SP stereoisomers of the nerve agents sarin and cyclosarin, creating a modified enzyme with enhanced overall activity and significantly increased detoxification properties Loligo vulgaris

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.1.8.2 Ca2+ dependent on Loligo vulgaris

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.1.8.2 35000
-
 x * 35000 Loligo vulgaris

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.1.8.2 diisopropyl fluorophosphate + H2O Loligo vulgaris
-
 diisopropyl phosphate + fluoride
-
 ?
3.1.8.2 additional information Loligo vulgaris diisopropyl fluorophosphatase acts on a variety of organophosphorus compounds ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.1.8.2 Loligo vulgaris
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.8.2 diisopropyl fluorophosphate + H2O
-
 Loligo vulgaris diisopropyl phosphate + fluoride
-
 ?
3.1.8.2 additional information diisopropyl fluorophosphatase acts on a variety of organophosphorus compounds Loligo vulgaris ?
-
 ?
3.1.8.2 additional information The enzyme also acts as Ca2+-dependent phosphotriesterase. The hydrolytic reaction catalyzed by DFPase leads to the formation of a phosphate or phosphonate and a fluoride ion, resulting in detoxification of the organophosphorus agent. Presence of a phosphoenzyme intermediate in the reaction mechanism, which involves direct nucleophilic attack by Asp229 on the substrate, but no metal-assisted water activation, overview Loligo vulgaris ?
-
 ?

Subunits

EC Number Subunits Comment Organism
3.1.8.2 ? x * 35000 Loligo vulgaris

Synonyms

EC Number Synonyms Comment Organism
3.1.8.2 DFPase
-
 Loligo vulgaris
3.1.8.2 diisopropyl fluorophosphatase
-
 Loligo vulgaris

General Information

EC Number General Information Comment Organism
3.1.8.2 physiological function diisopropyl fluorophosphatase is a calcium-dependent phosphotriesterase that acts on a variety of highly toxic organophosphorus compounds, that act as inhibitors of acetylcholinesterase Loligo vulgaris