Literature summary for 3.5.1.99 extracted from

Patricelli M.P.; Lovato, M.A.; Cravatt, B.F.
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.

Search for more literature for 3.5.1.99

Protein Variants

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

Inhibitors	Comment	Organism	Structure
ethoxy oleoyl fluorophosphonate	irreversible inhibitor, exclusively modifies FAAH at S241	Rattus norvegicus

KM Value [mM]

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

Localization	Comment	Organism	GeneOntology No.	Textmining
membrane	bound to	Rattus norvegicus	16020	-

Natural Substrates/ Products (Substrates)

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

Organism	UniProt	Comment	Textmining
Rattus norvegicus	-	-	-

Substrates and Products (Substrate)

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

Synonyms	Comment	Organism
FAAH	-	Rattus norvegicus

Turnover Number [1/s]

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

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Release 2023.1 (January 2023)