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Literature summary extracted from

  • Le, Q.A.; Chang, R.; Kim, Y.H.
    Rational design of paraoxonase 1 (PON1) for the efficient hydrolysis of organophosphates (2015), Chem. Commun. (Camb.), 51, 14536-14539 .
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.1.1.2 gene PON1, recombinant expression of wild-type and mutant enzymes in Escherichia coli strain Origami B (DE3) Oryctolagus cuniculus
3.1.8.1 gene PON1, recombinant expression of wild-type and mutant enzymes in Escherichia coli strain Origami B (DE3) Oryctolagus cuniculus

Protein Variants

EC Number Protein Variants Comment Organism
3.1.1.2 H115W/T332/V346A site-directed mutagenesis, the mutant shows no activity with phenylacetate compared to wild-type Oryctolagus cuniculus
3.1.1.2 H115W/T332S site-directed mutagenesis, the mutant shows no activity with phenylacetate compared to wild-type Oryctolagus cuniculus
3.1.1.2 H115W/V346A site-directed mutagenesis, the mutant shows no activity with phenylacetate compared to wild-type Oryctolagus cuniculus
3.1.1.2 I74F site-directed mutagenesis, the mutant shows reduced activity with phenylacetate compared to wild-type Oryctolagus cuniculus
3.1.1.2 I74F/H115W site-directed mutagenesis, the mutant shows no activity with phenylacetate compared to wild-type Oryctolagus cuniculus
3.1.1.2 I74F/H115W/T332 site-directed mutagenesis, the mutant shows no activity with phenylacetate compared to wild-type Oryctolagus cuniculus
3.1.1.2 I74F/H115W/V346A site-directed mutagenesis, the mutant shows no activity with phenylacetate compared to wild-type Oryctolagus cuniculus
3.1.1.2 I74F/T332S site-directed mutagenesis, the mutant shows reduced activity with phenylacetate compared to wild-type Oryctolagus cuniculus
3.1.1.2 I74F/V346A site-directed mutagenesis, the mutant shows reduced activity with phenylacetate compared to wild-type Oryctolagus cuniculus
3.1.1.2 T332S site-directed mutagenesis, the mutant shows 2fold increased activity with phenylacetate compared to wild-type Oryctolagus cuniculus
3.1.1.2 T332S/V346A site-directed mutagenesis, the mutant shows reduced activity with phenylacetate compared to wild-type Oryctolagus cuniculus
3.1.1.2 V346A site-directed mutagenesis, the mutant shows reduced activity with phenylacetate compared to wild-type Oryctolagus cuniculus
3.1.8.1 H115W/T332S site-directed mutagenesis, the mutant shows highly increased activity with diethyl-paraoxon compared to wild-type Oryctolagus cuniculus
3.1.8.1 H115W/T332S/V346A site-directed mutagenesis, the mutant shows increased activity with diethyl-paraoxon compared to wild-type Oryctolagus cuniculus
3.1.8.1 H115W/V346A site-directed mutagenesis, the mutant shows increased activity with diethyl-paraoxon compared to wild-type Oryctolagus cuniculus
3.1.8.1 I74A site-directed mutagenesis, the mutant shows highly reduced activity with diethyl-paraoxon compared to wild-type Oryctolagus cuniculus
3.1.8.1 I74F site-directed mutagenesis, the mutant shows increased activity with diethyl-paraoxon compared to wild-type Oryctolagus cuniculus
3.1.8.1 I74F/H115W site-directed mutagenesis, the mutant shows increased activity with diethyl-paraoxon compared to wild-type Oryctolagus cuniculus
3.1.8.1 I74F/H115W/T332S site-directed mutagenesis, the mutant shows very highly increased activity with diethyl-paraoxon compared to wild-type Oryctolagus cuniculus
3.1.8.1 I74F/H115W/V346A site-directed mutagenesis, the mutant shows highly increased activity with diethyl-paraoxon compared to wild-type Oryctolagus cuniculus
3.1.8.1 I74F/T332S site-directed mutagenesis, the mutant shows increased activity with diethyl-paraoxon compared to wild-type Oryctolagus cuniculus
3.1.8.1 I74F/T332S/V346A site-directed mutagenesis, the mutant shows increased activity with diethyl-paraoxon compared to wild-type Oryctolagus cuniculus
3.1.8.1 I74F/V346A site-directed mutagenesis, the mutant shows increased activity with diethyl-paraoxon compared to wild-type Oryctolagus cuniculus
3.1.8.1 I74L site-directed mutagenesis, the mutant shows unaltered activity with diethyl-paraoxon compared to wild-type Oryctolagus cuniculus
3.1.8.1 I74V site-directed mutagenesis, the mutant shows slightly reduced activity with diethyl-paraoxon compared to wild-type Oryctolagus cuniculus
3.1.8.1 I74W site-directed mutagenesis, the mutant shows unaltered activity with diethyl-paraoxon compared to wild-type Oryctolagus cuniculus
3.1.8.1 L69A site-directed mutagenesis, the mutant shows highly reduced activity with diethyl-paraoxon compared to wild-type Oryctolagus cuniculus
3.1.8.1 L69I site-directed mutagenesis, the mutant shows slightly increased activity with diethyl-paraoxon compared to wild-type Oryctolagus cuniculus
3.1.8.1 T332A site-directed mutagenesis, the mutant shows highly increased activity with diethyl-paraoxon compared to wild-type Oryctolagus cuniculus
3.1.8.1 T332S site-directed mutagenesis, the mutant shows highly increased activity with diethyl-paraoxon compared to wild-type Oryctolagus cuniculus
3.1.8.1 T332S/V346A site-directed mutagenesis, the mutant shows increased activity with diethyl-paraoxon compared to wild-type Oryctolagus cuniculus
3.1.8.1 T332V site-directed mutagenesis, almost inactive mutant Oryctolagus cuniculus
3.1.8.1 V346A site-directed mutagenesis, the mutant shows increased activity with diethyl-paraoxon compared to wild-type Oryctolagus cuniculus
3.1.8.1 V346L site-directed mutagenesis, the mutant shows highly reduced activity with diethyl-paraoxon compared to wild-type Oryctolagus cuniculus
3.1.8.1 V346L site-directed mutagenesis, the mutant shows slightly increased activity with diethyl-paraoxon compared to wild-type Oryctolagus cuniculus

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.1.8.1 diethyl-paraoxon
-
Oryctolagus cuniculus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.1.1.2 phenyl acetate + H2O Oryctolagus cuniculus
-
phenol + acetate
-
?
3.1.8.1 diethyl-paraoxon + H2O Oryctolagus cuniculus
-
diethyl phosphate + 4-nitrophenol
-
?
3.1.8.1 dimethyl-paraoxon + H2O Oryctolagus cuniculus
-
dimethyl phosphate + 4-nitrophenol
-
?

Organism

EC Number Organism UniProt Comment Textmining
3.1.1.2 Oryctolagus cuniculus P27170
-
-
3.1.8.1 Oryctolagus cuniculus P27170
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.1.2 additional information molecular docking of substrates to wild-type and mutant enzymes using the crystal structure of PON1 (PDB ID 3SRG with resolution 2.19 A), overview. The enzyme is a paraoxonase (EC 3.1.8.1) that also shows arylesterase activity (EC 3.1.1.2) with phenyl acetate as substrate Oryctolagus cuniculus ?
-
?
3.1.1.2 phenyl acetate + H2O
-
Oryctolagus cuniculus phenol + acetate
-
?
3.1.8.1 diethyl-paraoxon + H2O
-
Oryctolagus cuniculus diethyl phosphate + 4-nitrophenol
-
?
3.1.8.1 dimethyl-paraoxon + H2O
-
Oryctolagus cuniculus dimethyl phosphate + 4-nitrophenol
-
?
3.1.8.1 additional information molecular docking of substrates to wild-type and mutant enzymes using the crystal structure of PON1 (PDB ID 3SRG with resolution 2.19 A), overview. The enzyme also shows arylesterase activity (EC 3.1.1.2) with phenyl acetate as substrate Oryctolagus cuniculus ?
-
?

Synonyms

EC Number Synonyms Comment Organism
3.1.1.2 G3C9 rePON1
-
Oryctolagus cuniculus
3.1.1.2 More cf. EC 3.1.8.1 Oryctolagus cuniculus
3.1.1.2 paraoxonase 1
-
Oryctolagus cuniculus
3.1.1.2 PON1
-
Oryctolagus cuniculus
3.1.8.1 G3C9 rePON1
-
Oryctolagus cuniculus
3.1.8.1 paraoxonase 1
-
Oryctolagus cuniculus
3.1.8.1 PON1
-
Oryctolagus cuniculus

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.1.1.2 25
-
assay at Oryctolagus cuniculus
3.1.8.1 35
-
-
Oryctolagus cuniculus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.1.1.2 8
-
assay at Oryctolagus cuniculus
3.1.8.1 10.5
-
-
Oryctolagus cuniculus

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
3.1.8.1 0.192
-
diethyl-paraoxon pH 10.5, 25°C, recombinant mutant I74F/H115W/T332S Oryctolagus cuniculus
3.1.8.1 0.214
-
diethyl-paraoxon pH 10.5, 25°C, recombinant mutant H115W/T332S Oryctolagus cuniculus
3.1.8.1 0.404
-
diethyl-paraoxon pH 10.5, 25°C, recombinant mutant I74F/H115W Oryctolagus cuniculus
3.1.8.1 0.727
-
diethyl-paraoxon pH 10.5, 25°C, recombinant mutant V346A Oryctolagus cuniculus
3.1.8.1 1.54
-
diethyl-paraoxon pH 10.5, 25°C, recombinant mutant I74F/T332S Oryctolagus cuniculus
3.1.8.1 1.86
-
diethyl-paraoxon pH 10.5, 25°C, recombinant mutant I74F Oryctolagus cuniculus
3.1.8.1 2.31
-
diethyl-paraoxon pH 10.5, 25°C, recombinant mutant T332S Oryctolagus cuniculus
3.1.8.1 4.49
-
diethyl-paraoxon pH 10.5, 25°C, recombinant wild-type enzyme Oryctolagus cuniculus