EC Number | Cloned (Comment) | Organism |
---|---|---|
3.4.22.B78 | expression in Escherichia coli | Pyrococcus horikoshii |
EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
3.4.11.B7 | E12T | protease activity of E12T is 3.8 fold higher than that of wild-type enzyme. The mutant is more stable than wild-type at 85°C | Pyrococcus horikoshii |
3.4.22.B78 | E12T | the mutant enzyme is more stable than the wild-type enzyme | Pyrococcus horikoshii |
EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
---|
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
3.4.11.B7 | Pyrococcus horikoshii | O59413 | - |
- |
3.4.11.B7 | Pyrococcus horikoshii DSM 12428 | O59413 | - |
- |
3.4.22.B78 | Pyrococcus horikoshii | O59413 | - |
- |
3.4.22.B78 | Pyrococcus horikoshii DSM 12428 | O59413 | - |
- |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
3.4.11.B7 | Ala-Ala-Phe-Arg-7-amido-4-methylcoumarin + H2O | Glu12 is responsible for substrate binding | Pyrococcus horikoshii | Ala-Ala-Phe-Arg + 7-amino-4-methylcoumarin | - |
? | |
3.4.11.B7 | Ala-Ala-Phe-Arg-7-amido-4-methylcoumarin + H2O | Glu12 is responsible for substrate binding | Pyrococcus horikoshii DSM 12428 | Ala-Ala-Phe-Arg + 7-amino-4-methylcoumarin | - |
? | |
3.4.22.B78 | Ala-Ala-Phe-Arg-7-amido-4-methylcoumarin + H2O | Glu12 plays an important role in substrate binding | Pyrococcus horikoshii | Ala-Ala-Phe-Arg + 7-amino-4-methylcoumarin | - |
? | |
3.4.22.B78 | Ala-Ala-Phe-Arg-7-amido-4-methylcoumarin + H2O | Glu12 plays an important role in substrate binding | Pyrococcus horikoshii DSM 12428 | Ala-Ala-Phe-Arg + 7-amino-4-methylcoumarin | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
3.4.22.B78 | PhpI | ambiguous | Pyrococcus horikoshii |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
3.4.11.B7 | 85 | - |
assay at | Pyrococcus horikoshii |
3.4.22.B78 | 85 | - |
assay at | Pyrococcus horikoshii |
EC Number | Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|---|
3.4.11.B7 | 85 | - |
mutant enzyme E12T is more stable than wild-type at 85°C | Pyrococcus horikoshii |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
3.4.11.B7 | 7.5 | - |
assay at | Pyrococcus horikoshii |
3.4.22.B78 | 7.5 | - |
assay at | Pyrococcus horikoshii |