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Literature summary for 3.1.8.2 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

Application Comment Organism
degradation
-
Loligo vulgaris

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Loligo vulgaris

Molecular Weight [Da]

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

Organism

Organism UniProt Comment Textmining
Loligo vulgaris
-
-
-

Purification (Commentary)

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

Specific Activity [micromol/min/mg]

Specific Activity Minimum [Āµmol/min/mg] Specific Activity Maximum [Āµmol/min/mg] Comment Organism
213
-
-
Loligo vulgaris

Substrates and Products (Substrate)

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