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3.5.1.99: fatty acid amide hydrolase

This is an abbreviated version!
For detailed information about fatty acid amide hydrolase, go to the full flat file.

Word Map on EC 3.5.1.99

Reaction

anandamide
+
H2O
=
arachidonic acid
 +
ethanolamine

Synonyms

AAH, anandamide amidohydrolase, AtFAAH, endocannabinoid-degrading enzyme, FA amide hydrolase, FAAH, FAAH-1, FAAH-2, fatty acid amide hydrolase, fatty-acid amide hydrolase, hFAAH, oleamide hydrolase

ECTree

     3 Hydrolases
         3.5 Acting on carbon-nitrogen bonds, other than peptide bonds
             3.5.1 In linear amides
                3.5.1.99 fatty acid amide hydrolase

Crystallization

Crystallization on EC 3.5.1.99 - fatty acid amide hydrolase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
2.8 A crystal structure
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
recombinant fatty acid amide hydrolase mutant L192F/F194Y/A377T/S435N/I491V/V495M bound to carbamate inhibitor URB597 or inhibitor PF-3845, 25-30 mg/ml protein in 10 mM HEPES, pH 7.0, 500 mM NaCl, 2 mM dithiothreitol, and 0.08% n-undecyl-beta-D-maltoside or 0.1% n-decyl-beta-D-maltoside for inhibitor URB597-enzyme or PF-3845-enzyme conjugate, respectively, supplementation of the FAAH–URB597 proteinsample with 1.6% benzyldimethyl(2-dodecyloxyethyl)-ammonium chloride and mixed at a 1:1 proportion with a crystallization buffer containing 30% PEG 400, 100 mM TrisHCl pH 7.5, and 100 mM MgCl2, supplementation of the FAAH–PF-3845 protein sample with 1.6% benzyl-dimethyl-dodecyl ammonium bromide and mixed at a 1:1 ratio with a crystallization buffer containing 30% PEG 400, 100 mM 2-(N-morpholino)ethanesulfonate/NaOH, pH 5.5, and 400 mM LiCl, sitting drop vapor diffusion at 14°C, X-ray diffraction structure determination and analysis at 2.3 A resolution