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Literature summary for 3.1.1.2 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)

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

Protein Variants

Protein Variants Comment Organism
H115W/T332/V346A site-directed mutagenesis, the mutant shows no activity with phenylacetate compared to wild-type Oryctolagus cuniculus
H115W/T332S site-directed mutagenesis, the mutant shows no activity with phenylacetate compared to wild-type Oryctolagus cuniculus
H115W/V346A site-directed mutagenesis, the mutant shows no activity with phenylacetate compared to wild-type Oryctolagus cuniculus
I74F site-directed mutagenesis, the mutant shows reduced activity with phenylacetate compared to wild-type Oryctolagus cuniculus
I74F/H115W site-directed mutagenesis, the mutant shows no activity with phenylacetate compared to wild-type Oryctolagus cuniculus
I74F/H115W/T332 site-directed mutagenesis, the mutant shows no activity with phenylacetate compared to wild-type Oryctolagus cuniculus
I74F/H115W/V346A site-directed mutagenesis, the mutant shows no activity with phenylacetate compared to wild-type Oryctolagus cuniculus
I74F/T332S site-directed mutagenesis, the mutant shows reduced activity with phenylacetate compared to wild-type Oryctolagus cuniculus
I74F/V346A site-directed mutagenesis, the mutant shows reduced activity with phenylacetate compared to wild-type Oryctolagus cuniculus
T332S site-directed mutagenesis, the mutant shows 2fold increased activity with phenylacetate compared to wild-type Oryctolagus cuniculus
T332S/V346A site-directed mutagenesis, the mutant shows reduced activity with phenylacetate compared to wild-type Oryctolagus cuniculus
V346A site-directed mutagenesis, the mutant shows reduced activity with phenylacetate compared to wild-type Oryctolagus cuniculus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
phenyl acetate + H2O Oryctolagus cuniculus
-
phenol + acetate
-
?

Organism

Organism UniProt Comment Textmining
Oryctolagus cuniculus P27170
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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 ?
-
?
phenyl acetate + H2O
-
Oryctolagus cuniculus phenol + acetate
-
?

Synonyms

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

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
assay at Oryctolagus cuniculus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
assay at Oryctolagus cuniculus