Cloned (Comment) | Organism |
---|---|
expression in Escherichia coli | Sulfolobus islandicus |
Protein Variants | Comment | Organism |
---|---|---|
E14K | Tm-value for the mutant enzyme is 6°C lower than wild-type Tm-value. The efficiency of methyl-paraoxon hydrolysis is similar for wild-type and the mutants, whereas the mutants exhibit higher catalytic efficiency against ethyl-paraoxon than the wild-type. The mutants exhibit a heavily reduced N-acyl-homoserine lactonase-, delta-lactonase- and gamma-lactonase activity | Sulfolobus islandicus |
E14K/Y34Q | Tm-value for the mutant enzyme is 4°C lower than wild-type Tm-value. The efficiency of methyl-paraoxon hydrolysis is similar for wild-type and the mutants, whereas the mutants exhibit higher catalytic efficiency against ethyl-paraoxon than the wild-type. The mutants exhibit a heavily reduced N-acyl-homoserine lactonase-, delta-lactonase- and gamma-lactonase activity | Sulfolobus islandicus |
Y34Q | Tm-value for the mutant enzyme is 8°C lower than wild-type Tm-value. The efficiency of methyl-paraoxon hydrolysis is similar for wild-type and the mutants, whereas the mutants exhibit higher catalytic efficiency against ethyl-paraoxon than the wild-type. The mutants exhibit a heavily reduced N-acyl-homoserine lactonase-, delta-lactonase- and gamma-lactonase activity | Sulfolobus islandicus |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.124 | - |
4-nitrophenyl acetate | pH 8.0, 25°C | Sulfolobus islandicus |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
80000 | - |
dynamic light scattering | Sulfolobus islandicus |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Sulfolobus islandicus | C4KKZ9 | - |
- |
Sulfolobus islandicus M.16.4 | C4KKZ9 | - |
- |
Purification (Comment) | Organism |
---|---|
- |
Sulfolobus islandicus |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
4-nitrophenyl acetate + H2O | - |
Sulfolobus islandicus | 4-nitrophenol + acetate | - |
? | |
4-nitrophenyl acetate + H2O | - |
Sulfolobus islandicus M.16.4 | 4-nitrophenol + acetate | - |
? | |
additional information | no activity with phenyl acetate, 4-nitrophenyl-decanoate or 3-phenyl acetate | Sulfolobus islandicus | ? | - |
? | |
additional information | no activity with phenyl acetate, 4-nitrophenyl-decanoate or 3-phenyl acetate | Sulfolobus islandicus M.16.4 | ? | - |
? |
Subunits | Comment | Organism |
---|---|---|
dimer | at 25°C, dynamic light scattering | Sulfolobus islandicus |
Synonyms | Comment | Organism |
---|---|---|
SisLac | the enzyme also shows activity of aryldialkylphosphatase (EC 3.1.8.1) and 1,4-lactonase aryldialkylphosphatase(EC 3.1.1.25) | Sulfolobus islandicus |
Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|
80 | - |
half-life: 84 min | Sulfolobus islandicus |
90 | - |
half-life: 8.5 min | Sulfolobus islandicus |
94 | - |
Tm-value, mutant enzyme Y34Q | Sulfolobus islandicus |
95 | - |
half-life: 3.6 min | Sulfolobus islandicus |
96 | - |
Tm-value, mutant enzyme E14K | Sulfolobus islandicus |
98 | - |
Tm-value, mutant enzyme E14K/Y34Q | Sulfolobus islandicus |
102 | - |
Tm-value, wild-type enzyme | Sulfolobus islandicus |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.2 | - |
4-nitrophenyl acetate | pH 8.0, 25°C | Sulfolobus islandicus |
kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
1.6 | - |
4-nitrophenyl acetate | pH 8.0, 25°C | Sulfolobus islandicus |