Literature summary for 3.1.8.2 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.

Search for more literature for 3.1.8.2

Cloned(Commentary)

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

Crystallization (Commentary)

Crystallization (Comment)	Organism
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

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

Metals/Ions

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

Organism

Organism	UniProt	Comment	Textmining
Loligo vulgaris	Q7SIG4	-	-

Purification (Commentary)

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

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
diisopropyl fluorophosphate + H2O	-	Loligo vulgaris	diisopropyl phosphate + fluoride	-	?

Synonyms

Synonyms	Comment	Organism
DFPase	-	Loligo vulgaris
diisopropyl fluorophosphatase	-	Loligo vulgaris

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Release 2023.1 (January 2023)