Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Angkawidjaja, C.; Koga, Y.; Takano, K.; Kanaya, S.
    Structure and stability of a thermostable carboxylesterase from the thermoacidophilic archaeon Sulfolobus tokodaii (2012), FEBS J., 279, 3071-3084.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.1.1.1 overproduction in Escherichia coli Sulfurisphaera tokodaii

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.1.1.1 sitting-drop vapor diffusion technique, the structures of R267E, R267G and R267K are highly similar to that of Sto-Est with only slight differences in atomic coordinates Sulfurisphaera tokodaii

Protein Variants

EC Number Protein Variants Comment Organism
3.1.1.1 R267E the dimerized state of the mutant enzyme is unstable under denaturing conditions or at high temperature. The crystal structure is highly similar to that of wild-type enzyme with only slight differences in atomic coordinates. The optimum temperature of the mutant is reduced relative to that of wild-type enzyme. At pH 3 and 4 the mutant enzyme has a TM-value similar to that of wild-type enzyme. At pH 7 the mutant enzyme has a TM-value lower than that of the wild-type enzyme Sulfurisphaera tokodaii
3.1.1.1 R267G the dimerized state of the mutant enzyme is unstable under denaturing conditions or at high temperature. The crystal structure is highly similar to that of wild-type enzyme with only slight differences in atomic coordinates. The optimum temperature of the mutant is reduced relative to that of wild-type enzyme. At pH 3 and 4 the mutant enzyme has a TM-value similar to that of wild-type enzyme. At pH 7 the mutant enzyme has a TM-value lower than that of the wild-type enzyme Sulfurisphaera tokodaii
3.1.1.1 R267K the optimum temperature of the mutant enzyme is similar to that of wild-type enzyme. At pH 3 and 4 the mutant enzyme has a TM-value similart to that of wild-type enzyme. At pH 7 the mutant enzyme has a TM-value lower than that of the wild-type enzyme Sulfurisphaera tokodaii

Organism

EC Number Organism UniProt Comment Textmining
3.1.1.1 Sulfurisphaera tokodaii Q976W8
-
-
3.1.1.1 Sulfurisphaera tokodaii 7 Q976W8
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.1.1.1
-
Sulfurisphaera tokodaii

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.1.1 4-nitrophenyl acetate + H2O the acyl-length selectivity of the proteins against 4-nitrophenyl ester substrates in the order of decreasing efficiency: C8, C6, C4, C3, C2 Sulfurisphaera tokodaii 4-nitrophenol + acetate
-
?
3.1.1.1 4-nitrophenyl acetate + H2O the acyl-length selectivity of the proteins against 4-nitrophenyl ester substrates in the order of decreasing efficiency: C8, C6, C4, C3, C2 Sulfurisphaera tokodaii 7 4-nitrophenol + acetate
-
?
3.1.1.1 4-nitrophenyl butanoate + H2O the acyl-length selectivity of the proteins against 4-nitrophenyl ester substrates in the order of decreasing efficiency: C8, C6, C4, C3, C2 Sulfurisphaera tokodaii 4-nitrophenol + butanoate
-
?
3.1.1.1 4-nitrophenyl butanoate + H2O the acyl-length selectivity of the proteins against 4-nitrophenyl ester substrates in the order of decreasing efficiency: C8, C6, C4, C3, C2 Sulfurisphaera tokodaii 7 4-nitrophenol + butanoate
-
?
3.1.1.1 4-nitrophenyl hexanoate + H2O the acyl-length selectivity of the proteins against 4-nitrophenyl ester substrates in the order of decreasing efficiency: C8, C6, C4, C3, C2 Sulfurisphaera tokodaii 4-nitrophenol + hexanoate
-
?
3.1.1.1 4-nitrophenyl hexanoate + H2O the acyl-length selectivity of the proteins against 4-nitrophenyl ester substrates in the order of decreasing efficiency: C8, C6, C4, C3, C2 Sulfurisphaera tokodaii 7 4-nitrophenol + hexanoate
-
?
3.1.1.1 4-nitrophenyl octanoate + H2O the acyl-length selectivity of the proteins against 4-nitrophenyl ester substrates in the order of decreasing efficiency: C8, C6, C4, C3, C2 Sulfurisphaera tokodaii 4-nitrophenol + octanoate
-
?
3.1.1.1 4-nitrophenyl octanoate + H2O the acyl-length selectivity of the proteins against 4-nitrophenyl ester substrates in the order of decreasing efficiency: C8, C6, C4, C3, C2 Sulfurisphaera tokodaii 7 4-nitrophenol + octanoate
-
?
3.1.1.1 4-nitrophenyl propanoate + H2O the acyl-length selectivity of the proteins against 4-nitrophenyl ester substrates in the order of decreasing efficiency: C8, C6, C4, C3, C2 Sulfurisphaera tokodaii 4-nitrophenol + propanoate
-
?
3.1.1.1 4-nitrophenyl propanoate + H2O the acyl-length selectivity of the proteins against 4-nitrophenyl ester substrates in the order of decreasing efficiency: C8, C6, C4, C3, C2 Sulfurisphaera tokodaii 7 4-nitrophenol + propanoate
-
?

Subunits

EC Number Subunits Comment Organism
3.1.1.1 dimer R267 is important for the dimer integrity of Sto-Est that contributes to its overall stability Sulfurisphaera tokodaii
3.1.1.1 monomer protein exhibits activity even in the monomeric form Sulfurisphaera tokodaii

Synonyms

EC Number Synonyms Comment Organism
3.1.1.1 Sto-Est
-
Sulfurisphaera tokodaii

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.1.1.1 60
-
mutant enzyme R267E Sulfurisphaera tokodaii
3.1.1.1 80
-
wild-type enzyme Sulfurisphaera tokodaii

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
3.1.1.1 30 80 30°C: about 55% of maximal activity, 80°C: about 60% of maximal activity, mutant enzyme R267E Sulfurisphaera tokodaii
3.1.1.1 50 90 50°C: about 50% of maximal activity, 90°C: about 70% of maximal activity, wild-type enzyme Sulfurisphaera tokodaii

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.1.1.1 60
-
Tm-value at pH 3.0, wild-type enzyme Sulfurisphaera tokodaii
3.1.1.1 72
-
Tm-value at pH 4.0, wild-type enzyme Sulfurisphaera tokodaii
3.1.1.1 76
-
Tm-value at pH 6.0 and 7.0, mutant enzyme R267E Sulfurisphaera tokodaii
3.1.1.1 81
-
Tm-value at pH 6.0, wild-type enzyme Sulfurisphaera tokodaii
3.1.1.1 83
-
Tm-value at pH 5.0, wild-type enzyme Sulfurisphaera tokodaii
3.1.1.1 86
-
Tm-value at pH 9.0, wild-type enzyme Sulfurisphaera tokodaii
3.1.1.1 87
-
Tm-value at pH 7.0, wild-type enzyme Sulfurisphaera tokodaii

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.1.1.1 6
-
wild-type enzyme and R267 mutants Sulfurisphaera tokodaii