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Literature summary extracted from

  • Blum, M.M.; Chen, J.C.
    Structural characterization of the catalytic calcium-binding site in diisopropyl fluorophosphatase (DFPase)-Comparison with related beta-propeller enzymes (2010), Chem. Biol. Interact., 187, 373-379.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.1.8.2 expressed in Escherichia coli BL21(DE3) cells Loligo vulgaris

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.1.8.2 mutant enzymes N120D/N175D/D229N, E21QN120D/N175D/D229N, and D121E are crystallized by hanging drop vapor diffusion method, using 0.1 M MES buffer pH 6.5, 14-20% (w/v) PEG 3350 Loligo vulgaris

Protein Variants

EC Number Protein Variants Comment Organism
3.1.8.2 D121E the mutant displays 87% activity compared to the wild type enzyme Loligo vulgaris
3.1.8.2 D229N enzymatically inactive Loligo vulgaris
3.1.8.2 E21Q/N120D/N175D/D229N the mutations lead to a loss of calcium binding and enzymatic activity Loligo vulgaris
3.1.8.2 N120D/N175D/D229N the mutations lead to a loss of calcium binding and enzymatic activity Loligo vulgaris

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.1.8.2 Ca2+ required for activity, the wild type enzyme contains two Ca2+ ions Loligo vulgaris

Organism

EC Number Organism UniProt Comment Textmining
3.1.8.2 Loligo vulgaris Q7SIG4
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-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.1.8.2 Ni-NTA column chromatography and Q-Sepharose column chromatography Loligo vulgaris

Source Tissue

EC Number Source Tissue Comment Organism Textmining

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.8.2 diisopropyl fluorophosphate + H2O
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Loligo vulgaris diisopropyl phosphate + fluoride
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Synonyms

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