EC Number | Application | Comment | Organism |
---|---|---|---|
2.5.1.18 | biotechnology | commercial fusion partner using for enhancing the solubility of recombinant proteins | Schistosoma japonicum |
3.1.1.74 | industry | Cutinase is used as a lipolytic enzyme in the composition of laundry and dishwashing detergents to more efficiently remove immobilized fats. The oleochemistry industries and pollutant degradation represent other potential uses of cutinase. | Pseudomonas putida |
EC Number | Cloned (Comment) | Organism |
---|---|---|
2.5.1.18 | Expression of recombinant proteins with glutathione S-transferase as fusion expression partner in Escherichia coli strain BL21 (DE3). | Schistosoma japonicum |
3.1.1.74 | Expression of aggregation-prone cutinase protein using RNA polymerase sigma factor (RpoS) or glutathione transferase as fusion partners in Escherichia coli strain BL21 (DE3). | Pseudomonas putida |
4.1.1.15 | Expression of aggregation-prone deletion mutant protein (amino acids 448-585) using RNA polymerase sigma factor (RpoS) or glutathione S-transferase as fusion partners in Escherichia coli strain BL21 (DE3). | Homo sapiens |
EC Number | General Stability | Organism |
---|---|---|
3.1.1.74 | Using RNA polymerase sigma factor (RpoS) or glutathione transferase as fusion expression partners, the solubility of cutinase significantly increases. | Pseudomonas putida |
4.1.1.15 | using RNA polymerase sigma factor (RpoS) or glutathione transferase as fusion expression partners, the solubility of the enzyme significantly increases. | Homo sapiens |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
3.1.1.74 | additional information | Pseudomonas putida | Cutinase is known for its hydrolytic activity for a variety of esters ranging from soluble p-nitrophenyl esters to insoluble long-chain triglycerides. The hydrolytic activity of cutinase, especially on p-nitrophenyl esters of fatty acids, is extremely sensitive to fatty acid chain length. | ? | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
2.5.1.18 | Schistosoma japonicum | - |
gene from GST descended from Schistosoma containing in vector pET42a(+) | - |
3.1.1.74 | Pseudomonas putida | - |
- |
- |
4.1.1.15 | Homo sapiens | - |
- |
- |
EC Number | Purification (Comment) | Organism |
---|---|---|
3.1.1.74 | purification of his-tagged protein using Ni2+-affinity chromatography | Pseudomonas putida |
EC Number | Source Tissue | Comment | Organism | Textmining |
---|---|---|---|---|
2.5.1.18 | cell culture | - |
Schistosoma japonicum | - |
3.1.1.74 | cell culture | - |
Pseudomonas putida | - |
4.1.1.15 | cell culture | - |
Homo sapiens | - |
EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|---|
3.1.1.74 | additional information | - |
Assay of enzymatic activity of the fusion mutant of cutinase (RpoS-CUT) shows the same selective bioactivity as native cutinase to degrade p-nitrophenyl butyrate (PNB) but not to degrade p-nitrophenyl butyrate. | Pseudomonas putida |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
2.5.1.18 | additional information | GST as fusion expression partner enhances the solubility of recombinant proteins | Schistosoma japonicum | ? | - |
? | |
3.1.1.74 | additional information | Cutinase is known for its hydrolytic activity for a variety of esters ranging from soluble p-nitrophenyl esters to insoluble long-chain triglycerides. The hydrolytic activity of cutinase, especially on p-nitrophenyl esters of fatty acids, is extremely sensitive to fatty acid chain length. | Pseudomonas putida | ? | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
2.5.1.18 | glutathione transferase | - |
Schistosoma japonicum |
2.5.1.18 | glutathione-S-transferase | - |
Schistosoma japonicum |
2.5.1.18 | GST | - |
Schistosoma japonicum |
3.1.1.74 | cutinase | - |
Pseudomonas putida |
4.1.1.15 | glutamate decarboxylase | - |
Homo sapiens |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
3.1.1.74 | 37 | - |
assay at | Pseudomonas putida |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
3.1.1.74 | 8 | - |
assay at | Pseudomonas putida |