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Literature summary for 3.1.1.1 extracted from
- Structure and stability of a thermostable carboxylesterase from the thermoacidophilic archaeon Sulfolobus tokodaii (2012), FEBS J., 279, 3071-3084.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| overproduction in Escherichia coli | Sulfurisphaera tokodaii |
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| 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
| Protein Variants | Comment | Organism |
|---|---|---|
| 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 |
| 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 |
| 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
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Sulfurisphaera tokodaii | Q976W8 | - |
- |
| Sulfurisphaera tokodaii 7 | Q976W8 | - |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
- |
Sulfurisphaera tokodaii |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 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 | - |
? |  |
| 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 | - |
? | |
| 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 | - |
? | |
| 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 | - |
? | |
| 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 | - |
? | |
| 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 | - |
? | |
| 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 | - |
? | |
| 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 | - |
? | |
| 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 | - |
? | |
| 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
| Subunits | Comment | Organism |
|---|---|---|
| dimer | R267 is important for the dimer integrity of Sto-Est that contributes to its overall stability | Sulfurisphaera tokodaii |
| monomer | protein exhibits activity even in the monomeric form | Sulfurisphaera tokodaii |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| Sto-Est | - |
Sulfurisphaera tokodaii |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 60 | - |
mutant enzyme R267E | Sulfurisphaera tokodaii |
| 80 | - |
wild-type enzyme | Sulfurisphaera tokodaii |
Temperature Range [°C]
| Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 30 | 80 | 30°C: about 55% of maximal activity, 80°C: about 60% of maximal activity, mutant enzyme R267E | Sulfurisphaera tokodaii |
| 50 | 90 | 50°C: about 50% of maximal activity, 90°C: about 70% of maximal activity, wild-type enzyme | Sulfurisphaera tokodaii |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 60 | - |
Tm-value at pH 3.0, wild-type enzyme | Sulfurisphaera tokodaii |
| 72 | - |
Tm-value at pH 4.0, wild-type enzyme | Sulfurisphaera tokodaii |
| 76 | - |
Tm-value at pH 6.0 and 7.0, mutant enzyme R267E | Sulfurisphaera tokodaii |
| 81 | - |
Tm-value at pH 6.0, wild-type enzyme | Sulfurisphaera tokodaii |
| 83 | - |
Tm-value at pH 5.0, wild-type enzyme | Sulfurisphaera tokodaii |
| 86 | - |
Tm-value at pH 9.0, wild-type enzyme | Sulfurisphaera tokodaii |
| 87 | - |
Tm-value at pH 7.0, wild-type enzyme | Sulfurisphaera tokodaii |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 6 | - |
wild-type enzyme and R267 mutants | Sulfurisphaera tokodaii |
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