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Literature summary extracted from

  • Hill, C.M.; Wu, F.; Cheng, T.C.; DeFrank, J.J.; Raushel, F.M.
    Substrate and stereochemical specificity of the organophosphorus acid anhydrolase from Alteromonas sp. JD6.5 toward p-nitrophenyl phosphotriesters (2000), Bioorg. Med. Chem. Lett., 10, 1285-1288.
    View publication on PubMed

Application

EC Number Application Comment Organism
3.1.8.2 degradation enzyme catalyse the hydrolysis of toxic organophosphorus cholinesterase-inhibiting compounds, including pesticides and chemical nerve agents Alteromonas sp.

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.1.8.2 additional information
-
 additional information comparison of kinetic constants of paraoxon analogs Alteromonas sp.

Organism

EC Number Organism UniProt Comment Textmining
3.1.8.2 Alteromonas sp.
-
 JD6.5, halophilic bacterium
-

Reaction

EC Number Reaction Comment Organism Reaction ID
3.1.8.2 diisopropyl fluorophosphate + H2O = diisopropyl phosphate + fluoride the enzyme exhibits stereoselectivity toward the hydrolysis of chiral substrates with a preference for the S-P enantiomers Alteromonas sp.
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.8.2 additional information p-nitrophenyltriesters Alteromonas sp. ?
-
 ?
3.1.8.2 O-cyclohexylmethylphosphonofluoridate + H2O i.e. GF Alteromonas sp. ?
-
 ?
3.1.8.2 paraoxon + H2O i.e. diethyl-4-nitrophenyl phosphate, poor substrate Alteromonas sp. diethylphosphate + 4-nitrophenol
-
 ?
3.1.8.2 paraoxon + H2O substrate are also 16 paraoxon analogs Alteromonas sp. diethylphosphate + 4-nitrophenol
-
 ?
3.1.8.2 sarin + H2O i.e. O-isopropylmethylphosphonofluoridate Alteromonas sp. ?
-
 ?
3.1.8.2 soman + H2O i.e. O-pinacoyl methyl phosphonofluoridates Alteromonas sp. ?
-
 ?