3.5.1.99	additional information	-	additional information	Michaelis-Menten kinetics, overview	718570	
3.5.1.99	0.0018	-	anandamide	liver microsomes, pH 7.3, 37°C	718570	
3.5.1.99	0.0024	-	anandamide	liver microsomes, pH 7.3, 37°C	718570	
3.5.1.99	0.0033	-	anandamide	liver mitochondria, pH 7.3, 37°C	718570	
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	690872	
3.5.1.99	0.00843	-	N-(6-methoxypyridin-3-yl)decanamide	pH 8.0, 30°C	752472	
3.5.1.99	0.009	-	oleoyl methyl amide	pH 9.0, wild-type enzyme	690871	
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	690872	
3.5.1.99	0.012	-	oleamide	pH 9.0, recombinantly expressed FAAH protein lacking the N-terminal transmembrane domain	209111	
3.5.1.99	0.012	-	oleoyl p-nitroanilide	pH 9.0, mutant enzyme K142A	690871	
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	
3.5.1.99	0.032	-	oleoyl methyl ester	pH 9.0, mutant enzyme K142E	690871	
3.5.1.99	0.037	-	oleamide	pH 9.0, wild-type enzyme	690871	
3.5.1.99	0.041	-	oleoyl methyl amide	pH 9.0, mutant enzyme K142A	690871	
3.5.1.99	0.057	-	decanoyl p-nitroanilide	pH 9.0, wild-type enzyme	690875	
3.5.1.99	0.057	-	nonanoyl p-nitroanilide	pH 9.0, mutant enzyme A487V	690875	
3.5.1.99	0.06	-	arachidonoyl p-nitroanilide	pH 9.0, wild-type enzyme	690875	
3.5.1.99	0.063	-	oleoyl methyl ester	pH 9.0, mutant enzyme K142A	690871	
3.5.1.99	0.065	-	lauroyl p-nitroanilide	pH 9.0, wild-type enzyme	690875	
3.5.1.99	0.069	-	myristoyl p-nitroanilide	pH 9.0, mutant enzyme A487V	690875	
3.5.1.99	0.072	-	myristoyl p-nitroanilide	pH 9.0, mutant enzyme I491A	690875	
3.5.1.99	0.073	-	nonanoyl p-nitroanilide	pH 9.0, mutant enzyme G489A	690875	
3.5.1.99	0.074	-	nonanoyl p-nitroanilide	pH 9.0, wild-type enzyme	690875	
3.5.1.99	0.074	-	oleoyl p-nitroanilide	pH 9.0, wild-type enzyme	690875	
3.5.1.99	0.074	-	palmitoyl p-nitroanilide	pH 9.0, wild-type enzyme	690875	
3.5.1.99	0.083	-	oleoyl p-nitroanilide	pH 9.0, mutant enzyme A487V	690875	
3.5.1.99	0.092	-	myristoyl p-nitroanilide	pH 9.0, mutant enzyme T488A	690875	
3.5.1.99	0.094	-	myristoyl p-nitroanilide	pH 9.0, mutant enzyme G489A	690875	
3.5.1.99	0.095	-	oleoyl p-nitroanilide	pH 9.0, mutant enzyme T488A	690875	
3.5.1.99	0.098	-	oleoyl p-nitroanilide	pH 9.0, mutant enzyme G489A	690875	
3.5.1.99	0.099	-	myristoyl p-nitroanilide	pH 9.0, wild-type enzyme	690875	
3.5.1.99	0.126	-	oleoyl p-nitroanilide	pH 9.0, mutant enzyme I491A	690875	
3.5.1.99	0.16	-	N-(6-methoxypyridin-3-yl)octanamide	pH 8.0, 30°C	752472	
3.5.1.99	0.179	-	nonanoyl p-nitroanilide	pH 9.0, mutant enzyme T488A	690875	
3.5.1.99	0.22	-	octanoyl p-nitroanilide	pH 9.0, wild-type enzyme	690875	
3.5.1.99	0.41	-	heptanoyl p-nitroanilide	pH 9.0, wild-type enzyme	690875	
3.5.1.99	0.57	-	nonanoyl p-nitroanilide	pH 9.0, mutant enzyme I491A	690875	
3.5.1.99	2.34	-	arachidonamide	pH 7.4, 37°C	693528	
3.5.1.99	2.78	-	anandamide	pH 7.4, 37°C	693528	
3.5.1.99	7.31	-	N-(o-hydroxyphenyl)arachidonamide	pH 7.4, 37°C	693528	
3.5.1.99	7.94	-	(S)-alpha-methanandamide	pH 7.4, 37°C	693528	
3.5.1.99	33	-	(R)-alpha-methanandamide	pH 7.4, 37°C	693528