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Literature summary for 3.1.8.1 extracted from

  • Muthukrishnan, S.; Shete, V.S.; Sanan, T.T.; Vyas, S.; Oottikkal, S.; Porter, L.M.; Magliery, T.J.; Hadad, C.M.
    Mechanistic insights into the hydrolysis of organophosphorus compounds by paraoxonase-1: exploring the limits of substrate tolerance in a promiscuous enzyme (2012), J. Phys. Org. Chem., 25, 1247-1260.
    View publication on PubMedView publication on EuropePMC

Inhibitors

Inhibitors Comment Organism Structure
bis(cyclopropylmethyl) phosphoramidate paraoxon analogue with predominant active site binding mode synthetic construct
bis[4-(methylsulfanyl)phenyl] phosphorazidate paraoxon analogue with predominant active site binding mode synthetic construct
dibenzyl phosphoramidate paraoxon analogue with predominant active site binding mode synthetic construct

Organism

Organism UniProt Comment Textmining
synthetic construct
-
recombinant PON1 variant G2E6
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
paraoxon + H2O
-
synthetic construct 4-nitrophenol + diethyl phosphate
-
?

IC50 Value

IC50 Value IC50 Value Maximum Comment Organism Inhibitor Structure
0.03
-
pH 7.4, temperature not specified in the publication synthetic construct dibenzyl phosphoramidate
0.1 0.5 pH 7.4, temperature not specified in the publication synthetic construct bis(cyclopropylmethyl) phosphoramidate
0.3
-
pH 7.4, temperature not specified in the publication synthetic construct bis[4-(methylsulfanyl)phenyl] phosphorazidate