EC Number |
KM Value [mM] |
KM Value Maximum [mM] |
Substrate |
Reference |
---|
3.5.1.99 | 0.0123 |
- |
anandamide |
recombinant enzyme, pH 7.3, 37°C |
718570 |
3.5.1.99 | 0.015 |
- |
oleamide |
pH 9.0, mutant enzyme H358A, 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 | 0.015 |
- |
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 | 0.02 |
- |
oleamide |
pH 9.0, mutant enzyme K142A |
690871 |
3.5.1.99 | 0.021 |
- |
oleoyl p-nitroanilide |
pH 9.0, wild-type enzyme |
690871 |
3.5.1.99 | 0.022 |
- |
oleoyl methyl ester |
pH 9.0, wild-type enzyme |
690871 |
3.5.1.99 | 0.023 |
- |
oleamide |
pH 9.0, recombinantly expressed wild-type enzyme |
209111 |
3.5.1.99 | 0.029 |
- |
oleamide |
pH 9.0, mutant enzyme H449A, 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 | 0.03 |
- |
oleamide |
pH 9.0, mutant enzyme H184Q, 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 | 0.031 |
- |
oleamide |
pH 9.0, rat liver FAAH |
209111 |