Enzymes
| UniProtKB help_outline | 579 proteins |
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Reaction participants Show >> << Hide
- Name help_outline H2O Identifier CHEBI:15377 (Beilstein: 3587155; CAS: 7732-18-5) help_outline Charge 0 Formula H2O InChIKeyhelp_outline XLYOFNOQVPJJNP-UHFFFAOYSA-N SMILEShelp_outline [H]O[H] 2D coordinates Mol file for the small molecule Search links Involved in 6,204 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline N-(long-chain fatty acyl)ethanolamine Identifier CHEBI:15897 Charge 0 Formula C3H6NO2R SMILEShelp_outline OCCNC([*])=O 2D coordinates Mol file for the small molecule Search links Involved in 44 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline a long-chain fatty acid Identifier CHEBI:57560 Charge -1 Formula CO2R SMILEShelp_outline [O-]C([*])=O 2D coordinates Mol file for the small molecule Search links Involved in 727 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline ethanolamine Identifier CHEBI:57603 Charge 1 Formula C2H8NO InChIKeyhelp_outline HZAXFHJVJLSVMW-UHFFFAOYSA-O SMILEShelp_outline [NH3+]CCO 2D coordinates Mol file for the small molecule Search links Involved in 44 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:17505 | RHEA:17506 | RHEA:17507 | RHEA:17508 | |
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| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
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Publications
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Properties of rat liver N-acylethanolamine amidohydrolase.
Schmid P.C., Zuzarte-Augustin M.L., Schmid H.H.
Rat liver microsomes and mitochondria contain an amidohydrolase which catalyzes the hydrolysis of N-acylethanolamine to ethanolamine and fatty acid. The enzyme is active over a wide range of pH, does not require divalent cations, and is inhibited by sulfhydryl-reactive agents. The detergents Trito ... >> More
Rat liver microsomes and mitochondria contain an amidohydrolase which catalyzes the hydrolysis of N-acylethanolamine to ethanolamine and fatty acid. The enzyme is active over a wide range of pH, does not require divalent cations, and is inhibited by sulfhydryl-reactive agents. The detergents Triton X-100, sodium cholate, and sodium dodecyl sulfate are also inhibitory, but sodium taurodeoxycholate has little effect and was therefore used to solubilize the enzyme. The solubilized enzyme exhibits high substrate specificity for long-chain amides of ethanolamine. Amides of propanolamine or higher homologs are hydrolyzed at a drastically slower rate, and isomers prepared from long-chain amine and short-chain hydroxy acid are neither substrates nor inhibitors of the enzyme. Neither ceramide (N-acylsphingosine) nor N,O-diacylethanolamine is hydrolyzed. Both particulate and soluble enzyme preparations also catalyze the synthesis of N-acylethanolamine from ethanolamine and fatty acid, probably by the amidohydrolase acting in reverse. << Less