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Literature summary extracted from
- Chemical and mutagenic investigations of fatty acid amide hydrolase: evidence for a family of serine hydrolases with distinct catalytic properties (1999), Biochemistry, 38, 9804-9812.
Protein Variants
| EC Number | Protein Variants | Comment | Organism |
|---|---|---|---|
| 3.5.1.99 | H184Q | activity with oleamide is similar to wild-type enzyme | Rattus norvegicus |
| 3.5.1.99 | H358A | activity with oleamide is similar to wild-type enzyme | Rattus norvegicus |
| 3.5.1.99 | H449A | activity with oleamide is similar to wild-type enzyme | Rattus norvegicus |
| 3.5.1.99 | S217A | mutant shows 2300fold reductions in kcat for oleamide | Rattus norvegicus |
| 3.5.1.99 | S217A/S218A | mutant displays a 230000fold decrease in kcat for oleamide | Rattus norvegicus |
| 3.5.1.99 | S218A | mutant shows 95fold reductions in kcat for oleamide | Rattus norvegicus |
| 3.5.1.99 | S241A | mutant exhibits no detectable catalytic activity for oleamide | Rattus norvegicus |
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.5.1.99 | ethoxy oleoyl fluorophosphonate | irreversible inhibitor, exclusively modifies FAAH at S241 | Rattus norvegicus |  |
KM Value [mM]
| EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 3.5.1.99 | 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 | |
| 3.5.1.99 | 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 | |
| 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 | Rattus norvegicus | |
| 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 | Rattus norvegicus | |
| 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 | Rattus norvegicus | |
| 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 | Rattus norvegicus | |
Localization
| EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|---|
| 3.5.1.99 | membrane | bound to | Rattus norvegicus | 16020 | - |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.5.1.99 | anandamide + H2O | Rattus norvegicus | enzyme is responsible for the catabolism of neuromodulatory fatty acid amides, including anandamide and oleamide | ethanolamine + arachidonic acid | - |
? | |
| 3.5.1.99 | oleamide + H2O | Rattus norvegicus | enzyme is responsible for the catabolism of neuromodulatory fatty acid amides, including anandamide and oleamide | oleic acid + NH3 | - |
? | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 3.5.1.99 | Rattus norvegicus | - |
- |
- |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.5.1.99 | anandamide + H2O | enzyme is responsible for the catabolism of neuromodulatory fatty acid amides, including anandamide and oleamide | Rattus norvegicus | ethanolamine + arachidonic acid | - |
? | |
| 3.5.1.99 | oleamide + H2O | enzyme is responsible for the catabolism of neuromodulatory fatty acid amides, including anandamide and oleamide | Rattus norvegicus | oleic acid + NH3 | - |
? | |
| 3.5.1.99 | 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
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 3.5.1.99 | FAAH | - |
Rattus norvegicus |
Turnover Number [1/s]
| EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 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 | Rattus norvegicus | |
| 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 | Rattus norvegicus | |
| 3.5.1.99 | 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 | |
| 3.5.1.99 | 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 | |
| 3.5.1.99 | 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 | |
| 3.5.1.99 | 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 | |
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