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Literature summary 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)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 3.1.1.2 | expression in Escherichia coli | Homo sapiens |
| 3.1.1.25 | expression in Escherichia coli | Homo sapiens |
| 3.1.8.1 | expression in Escherichia coli | Homo sapiens |
Protein Variants
| EC Number | Protein Variants | Comment | Organism |
|---|---|---|---|
| 3.1.1.2 | H115W | mutation results in decrease in the affinity and the rate of catalysis of the enzyme | Homo sapiens |
| 3.1.1.2 | H115W/R192K | partially restores the phenyl acetate-hydrolyzing activity of mutant H115W | Homo sapiens |
| 3.1.1.2 | H115W/R192Q | complete loss of phenyl acetate-hydrolyzing activity | Homo sapiens |
| 3.1.1.2 | 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 |
| 3.1.1.25 | H115W | significant decrease in the rate of catalysis, moderate increase of the affinity of the substrate | Homo sapiens |
| 3.1.1.25 | H115W/R192K | kinetic parameters comparable to mutant H115W | Homo sapiens |
| 3.1.1.25 | H115W/R192Q | complete loss of activity | Homo sapiens |
| 3.1.1.25 | 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 |
| 3.1.8.1 | H115W | significant increase in the rate of catalysis, no effect on the affinity of the substrate | Homo sapiens |
| 3.1.8.1 | H115W/R192K | further increases in the paraoxon hydrolyzing activity of the enzyme | Homo sapiens |
| 3.1.8.1 | H115W/R192Q | mutation R192Q eleiminates the effect of mutation H115W | Homo sapiens |
| 3.1.8.1 | 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]
| EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 3.1.1.2 | 2.1 | - |
phenyl acetate | wild-type, pH 8.0, 25°C | Homo sapiens |  |
| 3.1.1.2 | 4.1 | - |
phenyl acetate | mutant H115W/R192K, pH 8.0, 25°C | Homo sapiens | |
| 3.1.1.2 | 10.8 | - |
phenyl acetate | mutant H115W, pH 8.0, 25°C | Homo sapiens | |
| 3.1.1.25 | 0.4 | - |
delta-valerolactone | mutant H115W, pH 8.3, 25°C | Homo sapiens | |
| 3.1.1.25 | 0.5 | - |
delta-valerolactone | mutant H115W/R192K, pH 8.3, 25°C | Homo sapiens | |
| 3.1.1.25 | 1.5 | - |
delta-valerolactone | wild-type, pH 8.3, 25°C | Homo sapiens | |
| 3.1.8.1 | 0.8 | - |
paraoxon | mutant H115W/R192Q, pH 8.0, 25°C | Homo sapiens | |
| 3.1.8.1 | 0.9 | - |
paraoxon | mutant H115W, pH 8.0, 25°C | Homo sapiens | |
| 3.1.8.1 | 0.9 | - |
paraoxon | mutant H115W/R192K, pH 8.0, 25°C | Homo sapiens | |
| 3.1.8.1 | 1.2 | - |
paraoxon | wild-type, pH 8.0, 25°C | Homo sapiens | |
Molecular Weight [Da]
| EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|---|
| 3.1.1.2 | 40000 | - |
x * 40000, SDS-PAGE | Homo sapiens |
| 3.1.1.25 | 40000 | - |
x * 40000, SDS-PAGE | Homo sapiens |
| 3.1.8.1 | 40000 | - |
x * 40000, SDS-PAGE | Homo sapiens |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 3.1.1.2 | Homo sapiens | P27169 | - |
- |
| 3.1.1.25 | Homo sapiens | P27169 | - |
- |
| 3.1.8.1 | Homo sapiens | P27169 | - |
- |
Source Tissue
| EC Number | Source Tissue | Comment | Organism | Textmining |
|---|
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.1.1.2 | phenyl acetate + H2O | - |
Homo sapiens | phenol + acetate | - |
? | |
| 3.1.1.25 | delta-valerolactone + H2O | - |
Homo sapiens | 5-hydroxypentanoic acid | - |
? | |
| 3.1.8.1 | paraoxon + H2O | - |
Homo sapiens | 4-nitrophenol + diethyl phosphate | - |
? | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 3.1.1.2 | ? | x * 40000, SDS-PAGE | Homo sapiens |
| 3.1.1.25 | ? | x * 40000, SDS-PAGE | Homo sapiens |
| 3.1.8.1 | ? | x * 40000, SDS-PAGE | Homo sapiens |
Turnover Number [1/s]
| EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 3.1.1.2 | 525.8 | - |
phenyl acetate | mutant H115W, pH 8.0, 25°C | Homo sapiens | |
| 3.1.1.2 | 759 | - |
phenyl acetate | mutant H115W/R192K, pH 8.0, 25°C | Homo sapiens | |
| 3.1.1.2 | 843.6 | - |
phenyl acetate | wild-type, pH 8.0, 25°C | Homo sapiens | |
| 3.1.1.25 | 0.5 | - |
delta-valerolactone | mutant H115W, pH 8.3, 25°C | Homo sapiens | |
| 3.1.1.25 | 0.9 | - |
delta-valerolactone | mutant H115W/R192K, pH 8.3, 25°C | Homo sapiens | |
| 3.1.1.25 | 29.8 | - |
delta-valerolactone | wild-type, pH 8.3, 25°C | Homo sapiens | |
| 3.1.8.1 | 0.9 | - |
paraoxon | wild-type, pH 8.0, 25°C | Homo sapiens | |
| 3.1.8.1 | 3.8 | - |
paraoxon | mutant H115W/R192Q, pH 8.0, 25°C | Homo sapiens | |
| 3.1.8.1 | 6 | - |
paraoxon | mutant H115W, pH 8.0, 25°C | Homo sapiens | |
| 3.1.8.1 | 10.7 | - |
paraoxon | mutant H115W/R192K, pH 8.0, 25°C | Homo sapiens | |
General Information
| EC Number | General Information | Comment | Organism |
|---|---|---|---|
| 3.1.1.2 | 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 |
| 3.1.1.25 | 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 |
| 3.1.8.1 | 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]
| EC Number | kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 3.1.1.2 | 48.6 | - |
phenyl acetate | mutant H115W, pH 8.0, 25°C | Homo sapiens | |
| 3.1.1.2 | 185.6 | - |
phenyl acetate | mutant H115W/R192K, pH 8.0, 25°C | Homo sapiens | |
| 3.1.1.2 | 401.7 | - |
phenyl acetate | wild-type, pH 8.0, 25°C | Homo sapiens | |
| 3.1.1.25 | 1.3 | - |
delta-valerolactone | mutant H115W, pH 8.3, 25°C | Homo sapiens | |
| 3.1.1.25 | 1.9 | - |
delta-valerolactone | mutant H115W/R192K, pH 8.3, 25°C | Homo sapiens | |
| 3.1.1.25 | 19.8 | - |
delta-valerolactone | wild-type, pH 8.3, 25°C | Homo sapiens | |
| 3.1.8.1 | 0.7 | - |
paraoxon | wild-type, pH 8.0, 25°C | Homo sapiens | |
| 3.1.8.1 | 4.6 | - |
paraoxon | mutant H115W/R192Q, pH 8.0, 25°C | Homo sapiens | |
| 3.1.8.1 | 6.6 | - |
paraoxon | mutant H115W, pH 8.0, 25°C | Homo sapiens | |
| 3.1.8.1 | 10.7 | - |
paraoxon | mutant H115W/R192K, pH 8.0, 25°C | Homo sapiens | |
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