Protein Variants | Comment | Organism |
---|---|---|
H184Q | activity with oleamide is similar to wild-type enzyme | Rattus norvegicus |
H358A | activity with oleamide is similar to wild-type enzyme | Rattus norvegicus |
H449A | activity with oleamide is similar to wild-type enzyme | Rattus norvegicus |
S217A | mutant shows 2300fold reductions in kcat for oleamide | Rattus norvegicus |
S217A/S218A | mutant displays a 230000fold decrease in kcat for oleamide | Rattus norvegicus |
S218A | mutant shows 95fold reductions in kcat for oleamide | Rattus norvegicus |
S241A | mutant exhibits no detectable catalytic activity for oleamide | Rattus norvegicus |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
ethoxy oleoyl fluorophosphonate | irreversible inhibitor, exclusively modifies FAAH at S241 | Rattus norvegicus |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.007 | - |
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 | Rattus norvegicus | |
0.011 | - |
oleamide | pH 9.0, wild-type enzyme, 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 | Rattus norvegicus | |
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 | Rattus norvegicus | |
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 | Rattus norvegicus | |
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 | Rattus norvegicus | |
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 | Rattus norvegicus |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
membrane | bound to | Rattus norvegicus | 16020 | - |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
anandamide + H2O | Rattus norvegicus | enzyme is responsible for the catabolism of neuromodulatory fatty acid amides, including anandamide and oleamide | ethanolamine + arachidonic acid | - |
? | |
oleamide + H2O | Rattus norvegicus | enzyme is responsible for the catabolism of neuromodulatory fatty acid amides, including anandamide and oleamide | oleic acid + NH3 | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Rattus norvegicus | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
anandamide + H2O | enzyme is responsible for the catabolism of neuromodulatory fatty acid amides, including anandamide and oleamide | Rattus norvegicus | ethanolamine + arachidonic acid | - |
? | |
oleamide + H2O | enzyme is responsible for the catabolism of neuromodulatory fatty acid amides, including anandamide and oleamide | Rattus norvegicus | oleic acid + NH3 | - |
? | |
oleamide + H2O | serine residue 241 acts as the catalytic nucleophile of the enzyme. FAAH does not utilize a histidine base for the activation of its serine nucleophile | Rattus norvegicus | oleic acid + NH3 | - |
? |
Synonyms | Comment | Organism |
---|---|---|
FAAH | - |
Rattus norvegicus |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
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 | Rattus norvegicus | |
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 | Rattus norvegicus | |
4.4 | - |
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 | Rattus norvegicus | |
5.2 | - |
oleamide | pH 9.0, wild-type enzyme, 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 | Rattus norvegicus | |
7.7 | - |
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 | Rattus norvegicus | |
20 | - |
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 | Rattus norvegicus |