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Literature summary extracted from
- Identification of amino acids related to catalytic function of Sulfolobus solfataricus P1 carboxylesterase by site-directed mutagenesis and molecular modeling (2016), BMB Rep., 49, 349-354 .
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 3.1.1.79 | sequence comparisons, recombinant expression of wild-type and mutant enzymes in Escherichia coli strain BL21 (DE3), subcloning in Escherichia coli strain DH5alpha | Saccharolobus solfataricus |
Protein Variants
| EC Number | Protein Variants | Comment | Organism |
|---|---|---|---|
| 3.1.1.79 | A152F | site-directed mutagenesis, the mutant shows 12.83% activity compared to wild-type | Saccharolobus solfataricus |
| 3.1.1.79 | C101S | site-directed mutagenesis, the mutant shows 31.55% activity compared to wild-type | Saccharolobus solfataricus |
| 3.1.1.79 | C103S | site-directed mutagenesis, the mutant shows 17.95% activity compared to wild-type | Saccharolobus solfataricus |
| 3.1.1.79 | C184S | site-directed mutagenesis, the mutant shows 16.93% activity compared to wild-type | Saccharolobus solfataricus |
| 3.1.1.79 | C94S | site-directed mutagenesis, the mutant shows 11.90% activity compared to wild-type | Saccharolobus solfataricus |
| 3.1.1.79 | D244N | site-directed mutagenesis, the mutant shows 1.55% activity compared to wild-type | Saccharolobus solfataricus |
| 3.1.1.79 | G80E | site-directed mutagenesis, the mutant shows 14.09% activity compared to wild-type | Saccharolobus solfataricus |
| 3.1.1.79 | G81E | site-directed mutagenesis, the mutant shows 16.94% activity compared to wild-type | Saccharolobus solfataricus |
| 3.1.1.79 | H274N | site-directed mutagenesis, almost inactive mutant | Saccharolobus solfataricus |
| 3.1.1.79 | additional information | the cysteine residues are located near the active site or at the positions inducing any conformational changes of the enzyme by their replacement with serine residues | Saccharolobus solfataricus |
| 3.1.1.79 | S151A | site-directed mutagenesis, inactive mutant | Saccharolobus solfataricus |
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.1.1.79 | 4-chloromercuribenzoate | - |
Saccharolobus solfataricus |  |
| 3.1.1.79 | diethyl dicarbonate | - |
Saccharolobus solfataricus | |
| 3.1.1.79 | diisopropylfluorophosphate | - |
Saccharolobus solfataricus | |
| 3.1.1.79 | HgCl2 | - |
Saccharolobus solfataricus | |
| 3.1.1.79 | PMSF | - |
Saccharolobus solfataricus | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 3.1.1.79 | Saccharolobus solfataricus | A0A0E3GVY6 | - |
- |
| 3.1.1.79 | Saccharolobus solfataricus DSM1616 | A0A0E3GVY6 | - |
- |
| 3.1.1.79 | Saccharolobus solfataricus P1 | A0A0E3GVY6 | - |
- |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 3.1.1.79 | recombinant wild-type 19.35fold to homogeneity and of mutant enzymes, from Escherichia coli strain BL21 (DE3), by heat treatment and hydrophobic interaction chromatography | Saccharolobus solfataricus |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.1.1.79 | 4-nitrophenol caprylate + H2O | - |
Saccharolobus solfataricus | 4-nitrophenol + caprylate | - |
? | |
| 3.1.1.79 | 4-nitrophenol caprylate + H2O | - |
Saccharolobus solfataricus P1 | 4-nitrophenol + caprylate | - |
? | |
| 3.1.1.79 | 4-nitrophenol caprylate + H2O | - |
Saccharolobus solfataricus DSM1616 | 4-nitrophenol + caprylate | - |
? | |
| 3.1.1.79 | tributyrin + H2O | - |
Saccharolobus solfataricus | dibutyrin + butyrate | - |
? | |
| 3.1.1.79 | tributyrin + H2O | - |
Saccharolobus solfataricus P1 | dibutyrin + butyrate | - |
? | |
| 3.1.1.79 | tributyrin + H2O | - |
Saccharolobus solfataricus DSM1616 | dibutyrin + butyrate | - |
? | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 3.1.1.79 | ? | x * 33500, about, sequence calculation, x * 34000, recombinant wild-type and mutant enzymes, SDS-PAGE | Saccharolobus solfataricus |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 3.1.1.79 | alpha/beta hydrolase | UniProt | Saccharolobus solfataricus |
| 3.1.1.79 | HSL-like carboxylesterase | - |
Saccharolobus solfataricus |
| 3.1.1.79 | SsoP1Est | - |
Saccharolobus solfataricus |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 3.1.1.79 | 60 | - |
assay at | Saccharolobus solfataricus |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 3.1.1.79 | 7 | - |
assay at | Saccharolobus solfataricus |
General Information
| EC Number | General Information | Comment | Organism |
|---|---|---|---|
| 3.1.1.79 | evolution | archaeon Sulfolobus solfataricus P1 carboxylesterase is a thermostable enzyme belonging to the mammalian hormone-sensitive lipase (HSL) family. Enzyme SsoP1Est belongs to the HSL family exhibiting a classic alpha/beta hydrolase fold by sequence alignment with homologous esterases, which were well characterized in the structure. Thus, it contains a typical catalytic triad of esterases, which is expected to be composed of Ser151, Asp244, and His274, and another typical oxyanion hole, which is presumed to be composed of Gly80, Gly81, and Ala152 | Saccharolobus solfataricus |
| 3.1.1.79 | additional information | residues Ser151, Asp244, and His274 form the catalytic triad of the native SsoP1Est, residues Gly80, Gly81, and Ala152 form the oxyanion hole. Enzyme structure homology modeling, overview | Saccharolobus solfataricus |
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