EC Number |
Turnover Number Minimum [1/s] |
Turnover Number Maximum [1/s] |
Substrate |
Reference |
---|
3.5.1.99 | 0.0001 |
- |
oleoyl methyl amide |
pH 9.0, mutant enzyme K142A |
690871 |
3.5.1.99 | 0.0002 |
- |
oleoyl methyl ester |
pH 9.0, mutant enzyme K142E |
690871 |
3.5.1.99 | 0.00026 |
- |
oleamide |
pH 9.0, mutant enzyme K142A |
690871 |
3.5.1.99 | 0.00031 |
- |
oleoyl methyl amide |
pH 9.0, mutant enzyme K142E |
690871 |
3.5.1.99 | 0.00052 |
- |
oleoyl p-nitroanilide |
pH 9.0, mutant enzyme K142E |
690871 |
3.5.1.99 | 0.00064 |
- |
oleamide |
pH 9.0, mutant enzyme K142E |
690871 |
3.5.1.99 | 0.0022 |
- |
oleamide |
pH 9.0, mutant enzyme S217A, FAAH protein lacking its N-terminal 39 amino acids is used. This modification removes the predicted N-terminal transmembrane domain of FAAH, the deletion of which is previously found to leave catalytic properties of FAAH unaltered, while at the same time facilitating the purification |
690872 |
3.5.1.99 | 0.012 |
- |
oleoyl methyl ester |
pH 9.0, mutant enzyme K142A |
690871 |
3.5.1.99 | 0.055 |
- |
oleamide |
pH 9.0, mutant enzyme S218A, FAAH protein lacking its N-terminal 39 amino acids is used. This modification removes the predicted N-terminal transmembrane domain of FAAH, the deletion of which is previously found to leave catalytic properties of FAAH unaltered, while at the same time facilitating the purification |
690872 |
3.5.1.99 | 0.13 |
- |
myristoyl p-nitroanilide |
pH 9.0, mutant enzyme A487V |
690875 |