Cloned (Comment) | Organism |
---|---|
expression in Escherichia coli of of chimeras of a carboxylesterase (EC 3.1.1.1) from Archaeoglobus fulgidus and an acylpeptide hydrolase (EC 3.4.19.1) from Aeropyrum pernix K1 | Aeropyrum pernix |
Protein Variants | Comment | Organism |
---|---|---|
additional information | construction of chimeras of a carboxylesterase (EC 3.1.1.1) from Archaeoglobus fulgidus and an acylpeptide hydrolase (EC 3.4.19.1) from Aeropyrum pernix K1. Their activities to hydrolyze 4-nitrophenyl esters (pNP) with different acyl chain lengths is explored. The chimeras inherit the thermophilic property of both parents. The substrate-binding domain is the dominant factor on enzyme substrate specificity, and the optimization of the newly formed domain interface is an important guarantee for successful domain swapping of proteins with low-sequence homology | Aeropyrum pernix |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Aeropyrum pernix | Q9YBQ2 | - |
- |
Purification (Comment) | Organism |
---|---|
- |
Aeropyrum pernix |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
80 | - |
wild-type enzyme | Aeropyrum pernix |
Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
---|---|---|---|
60 | 80 | 60°C: about 40% of maximal activity, 80°C: optimum | Aeropyrum pernix |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
8.8 | - |
wild-type enzyme | Aeropyrum pernix |
pH Minimum | pH Maximum | Comment | Organism |
---|---|---|---|
7.5 | 9.5 | pH 7.5: about 50% of maximal activity, pH 9.5: about 65% of maximal activity, wild-type enzyme | Aeropyrum pernix |