Cloned (Comment) | Organism |
---|---|
gene PON1, recombinant expression of wild-type and mutant enzymes in Escherichia coli strain Origami B (DE3) | Oryctolagus cuniculus |
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 | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
phenyl acetate + H2O | Oryctolagus cuniculus | - |
phenol + acetate | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Oryctolagus cuniculus | P27170 | - |
- |
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 | 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 Maximum [°C] | Comment | Organism |
---|---|---|---|
25 | - |
assay at | Oryctolagus cuniculus |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
8 | - |
assay at | Oryctolagus cuniculus |