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Literature summary for 3.1.8.1 extracted from
- Interplay between amino acid residues at positions 192 and 115 in modulating hydrolytic activities of human paraoxonase 1 (2014), Biochimie, 105, 202-210.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expression in Escherichia coli | Homo sapiens |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| H115W | significant increase in the rate of catalysis, no effect on the affinity of the substrate | Homo sapiens |
| H115W/R192K | further increases in the paraoxon hydrolyzing activity of the enzyme | Homo sapiens |
| H115W/R192Q | mutation R192Q eleiminates the effect of mutation H115W | Homo sapiens |
| additional information | the presence of a (His)6-tag at the N-terminus and at both the N- and C-termini decreases the enzymatic activity of the recombinant protein. The activity is unaffected by the presence of a (His)6-tag at its C-terminus | Homo sapiens |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.8 | - |
paraoxon | mutant H115W/R192Q, pH 8.0, 25°C | Homo sapiens |  |
| 0.9 | - |
paraoxon | mutant H115W, pH 8.0, 25°C | Homo sapiens | |
| 0.9 | - |
paraoxon | mutant H115W/R192K, pH 8.0, 25°C | Homo sapiens | |
| 1.2 | - |
paraoxon | wild-type, pH 8.0, 25°C | Homo sapiens | |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 40000 | - |
x * 40000, SDS-PAGE | Homo sapiens |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Homo sapiens | P27169 | - |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| paraoxon + H2O | - |
Homo sapiens | 4-nitrophenol + diethyl phosphate | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| ? | x * 40000, SDS-PAGE | Homo sapiens |
Turnover Number [1/s]
| Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.9 | - |
paraoxon | wild-type, pH 8.0, 25°C | Homo sapiens | |
| 3.8 | - |
paraoxon | mutant H115W/R192Q, pH 8.0, 25°C | Homo sapiens | |
| 6 | - |
paraoxon | mutant H115W, pH 8.0, 25°C | Homo sapiens | |
| 10.7 | - |
paraoxon | mutant H115W/R192K, pH 8.0, 25°C | Homo sapiens | |
General Information
| General Information | Comment | Organism |
|---|---|---|
| physiological function | the presence of a particular amino acid residue at position 192 differentially alters the effect of the H115W substitution, and the H115 residue is not always needed for the lactonase and arylesterase activities of the enzyme. The amino acid residues at position 192 and 115 act in conjunction in modulating the hydrolytic activities of the enzyme | Homo sapiens |
kcat/KM [mM/s]
| kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.7 | - |
paraoxon | wild-type, pH 8.0, 25°C | Homo sapiens | |
| 4.6 | - |
paraoxon | mutant H115W/R192Q, pH 8.0, 25°C | Homo sapiens | |
| 6.6 | - |
paraoxon | mutant H115W, pH 8.0, 25°C | Homo sapiens | |
| 10.7 | - |
paraoxon | mutant H115W/R192K, pH 8.0, 25°C | Homo sapiens | |
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