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Literature summary for 3.1.8.2 extracted from

  • Belinskaya, T.; Pattabiraman, N.; diTargiani, R.; Choi, M.; Saxena, A.
    Differences in amino acid residues in the binding pockets dictate substrate specificities of mouse senescence marker protein-30, human paraoxonase1, and squid diisopropylfluorophosphatase (2012), Biochim. Biophys. Acta, 1824, 701-710.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
homology modeling and docking of substrates. The two identical hydrophobic isopropyl groups in diisopropyl fluorophosphate bind to two different sub-pockets in the binding-site. Sub-pocket 1 is formed by residues P36, E37, I72, A74 and M90 while sub-pocket 2 is formed by F173, N175, T195, and W244 Loligo vulgaris

Organism

Organism UniProt Comment Textmining
Loligo vulgaris Q7SIG4
-
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [Āµmol/min/mg] Specific Activity Maximum [Āµmol/min/mg] Comment Organism
82
-
substrate soman, pH 8.0, temperature not specified in the publication Loligo vulgaris
110
-
substrate sarin, pH 8.0, temperature not specified in the publication Loligo vulgaris
198
-
substrate cyclosarin, pH 8.0, temperature not specified in the publication Loligo vulgaris
225
-
substrate diisopropyl fluorophosphate, pH 8.0, temperature not specified in the publication Loligo vulgaris

Substrates and Products (Substrate)

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