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Literature summary for 3.5.1.99 extracted from

  • Min, X.; Thibault, S.T.; Porter, A.C.; Gustin, D.J.; Carlson, T.J.; Xu, H.; Lindstrom, M.; Xu, G.; Uyeda, C.; Ma, Z.; Li, Y.; Kayser, F.; Walker, N.P.; Wang, Z.
    Discovery and molecular basis of potent noncovalent inhibitors of fatty acid amide hydrolase (FAAH) (2011), Proc. Natl. Acad. Sci. USA, 108, 7379-7384.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.5.1.99

Cloned(Commentary)

Cloned (Comment) Organism
expression of His-tagged FAAH in Escherichia coli strain Rattus norvegicus
expression of His-tagged FAAH in Escherichia coli strain Homo sapiens

Crystallization (Commentary)

Crystallization (Comment) Organism
purified recombinant His-tagged apo FAAH, hanging drop vapor diffusion method, X-ray diffraction structure determination and analysis at 2.9 A resolution, molecular replacement Rattus norvegicus
purified recombinant His-tagged apo FAAH, hanging drop vapor diffusion method, X-ray diffraction structure determination and analysis at 2.9 A resolution, molecular replacement Homo sapiens

Inhibitors

Inhibitors Comment Organism Structure
1-[(3S)-1-[4-(1-benzofuran-2-yl)pyrimidin-2-yl]piperidin-3-yl]-3-ethyl-1,3-dihydro-2H-benzimidazol-2-one the compound belongs to the ketobenzimidazoles, though containing a carbonyl moiety, that do not covalently modify Ser241. These inhibitors achieve potent inhibition of FAAH activity primarily from shape complementarity to the active site and through numerous hydrophobic interactions exhibiting excellent selectivity and good pharmacokinetic properties, nonmechanism-based inhibition Homo sapiens
1-[(3S)-1-[4-(1-benzofuran-2-yl)pyrimidin-2-yl]piperidin-3-yl]-3-ethyl-1,3-dihydro-2H-benzimidazol-2-one the compound belongs to the ketobenzimidazoles, though containing a carbonyl moiety, that do not covalently modify Ser241. These inhibitors achieve potent inhibition of FAAH activity primarily from shape complementarity to the active site and through numerous hydrophobic interactions exhibiting excellent selectivity and good pharmacokinetic properties, nonmechanism-based inhibition. Pharmacokinetic parameters and selectivity 2, overview Rattus norvegicus
6-bromo-N-(2-fluorophenyl)-1'H,4H-spiro[1,3-benzodioxine-2,4'-piperidine]-1'-carboxamide an irreversible covalent inhibitor, binding structure, overview Homo sapiens
6-bromo-N-(2-fluorophenyl)-1'H,4H-spiro[1,3-benzodioxine-2,4'-piperidine]-1'-carboxamide an irreversible covalent inhibitor, binding structure, overview Rattus norvegicus
OL-135 7-phenyl-1-[5-(pyridin-2-yl)-1,3-oxazol-2-yl]heptan-1-one Homo sapiens
OL-135 7-phenyl-1-[5-(pyridin-2-yl)-1,3-oxazol-2-yl]heptan-1-one Rattus norvegicus
URB597
-
 Homo sapiens
URB597
-
 Rattus norvegicus

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane integral membrane protein Rattus norvegicus 16020
-
membrane integral membrane protein Homo sapiens 16020
-

Organism

Organism UniProt Comment Textmining
Homo sapiens O00519
-
-
Rattus norvegicus P97612
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged FAAH from Escherichia coli strain by nickel affinity chromatography Rattus norvegicus
recombinant His-tagged FAAH from Escherichia coli strain by nickel affinity chromatography Homo sapiens

Subunits

Subunits Comment Organism
More three major cavities in the active site are the membrane access channel, the acyl-chain binding pocket, and the cytosolic port, overview. The core structure of the FAAH monomer adopts an alpha/beta fold with a twisted 11-strand beta-sheet in the center and 24 alpha-helices surrounding the sheet Rattus norvegicus
More three major cavities in the active site are the membrane access channel, the acyl-chain binding pocket, and the cytosolic port, overview. The core structure of the FAAH monomer adopts an alpha/beta fold with a twisted 11-strand beta-sheet in the center and 24 alpha-helices surrounding the sheet Homo sapiens

Synonyms

Synonyms Comment Organism
FAAH
-
 Rattus norvegicus
FAAH
-
 Homo sapiens

IC50 Value

IC50 Value IC50 Value Maximum Comment Organism Inhibitor Structure
0.000003
-
 pH and temperature not specified in the publication Rattus norvegicus URB597
0.000004
-
 pH and temperature not specified in the publication Homo sapiens URB597
0.000005
-
 pH and temperature not specified in the publication Homo sapiens 6-bromo-N-(2-fluorophenyl)-1'H,4H-spiro[1,3-benzodioxine-2,4'-piperidine]-1'-carboxamide
0.000016
-
 pH and temperature not specified in the publication Homo sapiens OL-135
0.000025
-
 pH and temperature not specified in the publication Rattus norvegicus OL-135
0.000028
-
 pH and temperature not specified in the publication Homo sapiens 1-[(3S)-1-[4-(1-benzofuran-2-yl)pyrimidin-2-yl]piperidin-3-yl]-3-ethyl-1,3-dihydro-2H-benzimidazol-2-one
0.000036
-
 pH and temperature not specified in the publication Rattus norvegicus 6-bromo-N-(2-fluorophenyl)-1'H,4H-spiro[1,3-benzodioxine-2,4'-piperidine]-1'-carboxamide
0.0001
-
 pH and temperature not specified in the publication Rattus norvegicus 1-[(3S)-1-[4-(1-benzofuran-2-yl)pyrimidin-2-yl]piperidin-3-yl]-3-ethyl-1,3-dihydro-2H-benzimidazol-2-one

General Information

General Information Comment Organism
evolution fatty acid amide hydrolase is an amidase-signature family member Rattus norvegicus
evolution fatty acid amide hydrolase is an amidase-signature family member Homo sapiens
additional information catalytic triad is formed by Ser241-Ser217-Lys142 Homo sapiens
additional information the active site is located in the center cavity defined by an atypical Ser-Ser-Lys catalytic triad which comprises the catalytic nucleophile residue Ser241 along with residues Ser217 and Lys142 Rattus norvegicus