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Literature summary for 3.1.1.2 extracted from

  • Hiblot, J.; Gotthard, G.; Chabriere, E.; Elias, M.
    Structural and enzymatic characterization of the lactonase SisLac from Sulfolobus islandicus (2012), PLoS One, 7, e47028.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.1.1.2

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Sulfolobus islandicus

Protein Variants

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 [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 [Da] Molecular Weight Maximum [Da] Comment Organism
80000
-
 dynamic light scattering Sulfolobus islandicus

Organism

Organism UniProt Comment Textmining
Sulfolobus islandicus C4KKZ9
-
-
Sulfolobus islandicus M.16.4 C4KKZ9
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Sulfolobus islandicus

Substrates and Products (Substrate)

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

Subunits Comment Organism
dimer at 25°C, dynamic light scattering Sulfolobus islandicus

Synonyms

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 [°C]

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 [1/s]

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 [mM/s]

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