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Literature summary extracted from

  • Hartleib, J.; Ruterjans, H.
    High-yield expression, purification, and characterization of the recombinant diisopropylfluorophosphatase from Loligo vulgaris (2001), Protein Expr. Purif., 21, 210-219.
    View publication on PubMed

Application

EC Number Application Comment Organism
3.1.8.2 degradation
-
 Loligo vulgaris

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.1.8.2 expression in Escherichia coli Loligo vulgaris

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.1.8.2 35220
-
 calculated from amino acid frequence Loligo vulgaris

Organism

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

Purification (Commentary)

EC Number Purification (Comment) Organism
3.1.8.2 recombinant enzyme, production of large amounts Loligo vulgaris

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
3.1.8.2 213
-
-
 Loligo vulgaris

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.8.2 cyclohexylsarin + H2O
-
 Loligo vulgaris ?
-
 ?
3.1.8.2 diisopropyl fluorophosphate + H2O
-
 Loligo vulgaris diisopropyl phosphate + fluoride
-
 ?
3.1.8.2 sarin + H2O
-
 Loligo vulgaris ?
-
 ?
3.1.8.2 soman + H2O
-
 Loligo vulgaris ?
-
 ?
3.1.8.2 tabun + H2O
-
 Loligo vulgaris ?
-
 ?