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Literature summary for 3.1.1.25 extracted from
- Characterization of human paraoxonase 1 variants suggest that His residues at 115 and 134 positions are not always needed for the lactonase/arylesterase activities of the enzyme (2013), Protein Sci., 22, 1799-1807.
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| L69G/S111T/H115W/H134R/R192K/F222S/T332S | mutant designed for expression in Escherichia coli in soluble and active form. Activity towards delta-valerolactone and homocysteinthiolactone is similar to wild-type, ativity towards N-oxododecanoyl-DL-homoserine lactone is 4fold increased | Homo sapiens |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| EDTA | complete inhibition of phenyl acetate hydrolyzing activity | Homo sapiens |  |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Homo sapiens | P27169 | - |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| delta-valerolactone + H2O | - |
Homo sapiens | 5-hydroxypentanoic acid | - |
? | |
| homocysteinthiolactone + H2O | - |
Homo sapiens | (2S)-2-aminobutanethioic S-acid | - |
? | |
| N-oxododecanoyl-DL-homoserine lactone + H2O | - |
Homo sapiens | ? | - |
? | |
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Release 2023.1 (January 2023)
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