Enzymes
| UniProtKB help_outline | 4 proteins |
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- Name help_outline 1-O-methyl-(5Z,8Z,11Z,14Z)-eicosatetraenoate Identifier CHEBI:78033 (CAS: 2566-89-4) help_outline Charge 0 Formula C21H34O2 InChIKeyhelp_outline OFIDNKMQBYGNIW-ZKWNWVNESA-N SMILEShelp_outline CCCCC\C=C/C\C=C/C\C=C/C\C=C/CCCC(=O)OC 2D coordinates Mol file for the small molecule Search links Involved in 5 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- 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 (5Z,8Z,11Z,14Z)-eicosatetraenoate Identifier CHEBI:32395 (Beilstein: 5439048) help_outline Charge -1 Formula C20H31O2 InChIKeyhelp_outline YZXBAPSDXZZRGB-DOFZRALJSA-M SMILEShelp_outline CCCCC\C=C/C\C=C/C\C=C/C\C=C/CCCC([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 83 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline H+ Identifier CHEBI:15378 Charge 1 Formula H InChIKeyhelp_outline GPRLSGONYQIRFK-UHFFFAOYSA-N SMILEShelp_outline [H+] 2D coordinates Mol file for the small molecule Search links Involved in 9,431 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline methanol Identifier CHEBI:17790 (Beilstein: 1098229; CAS: 67-56-1) help_outline Charge 0 Formula CH4O InChIKeyhelp_outline OKKJLVBELUTLKV-UHFFFAOYSA-N SMILEShelp_outline CO 2D coordinates Mol file for the small molecule Search links Involved in 45 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:63052 | RHEA:63053 | RHEA:63054 | RHEA:63055 | |
|---|---|---|---|---|
| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
| UniProtKB help_outline |
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Related reactions help_outline
More general form(s) of this reaction
Publications
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Catalytic properties of purified recombinant anandamide amidohydrolase.
Ueda N., Katayama K., Goparaju S.K., Kurahashi Y., Yamanaka K., Suzuki H., Yamamoto S.
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Reversible hydrolysis and synthesis of anandamide demonstrated by recombinant rat fatty-acid amide hydrolase.
Kurahashi Y., Ueda N., Suzuki H., Suzuki M., Yamamoto S.
Previously we suggested that one porcine brain enzyme (anandamide amidohydrolase) catalyzed both the hydrolysis of anandamide and its synthesis from arachidonic acid and ethanolamine (Ueda et al., J. Biol. Chem. 270, 23823-23827, 1995). In the present study we investigated the reversibility of the ... >> More
Previously we suggested that one porcine brain enzyme (anandamide amidohydrolase) catalyzed both the hydrolysis of anandamide and its synthesis from arachidonic acid and ethanolamine (Ueda et al., J. Biol. Chem. 270, 23823-23827, 1995). In the present study we investigated the reversibility of the enzyme reactions by the use of recombinant fatty-acid amide hydrolase of rat liver, which appears to be catalytically identical to porcine anandamide amidohydrolase. The particulate fraction of the COS-7 cells, in which the rat enzyme was overexpressed, hydrolyzed anandamide with a specific activity of 132 nmol/min/mg protein at 37 degrees C, and the Km value for anandamide was 18 microM. The enzyme also synthesized anandamide at a rate of 177 nmol/min/mg protein, and the Km values for arachidonic acid and ethanolamine as substrates were as high as 190 microM and 36 mM, respectively. The control cells transfected with the insert-free vector showed neither the hydrolase activity nor the synthase activity. Thus, the hydrolase and synthase are attributed to the same enzyme protein coded by one gene. However, the enzyme may act as a hydrolase rather than a synthase under physiological conditions judging from its high Km values for substrates in the synthase reactions. In addition, primary amides of fatty acids such as arachidonamide and oleamide and fatty acid ester like methyl arachidonate were hydrolyzed at considerable rates, and their reverse reactions occurred even if at lower rates. << Less
Biochem. Biophys. Res. Commun. 237:512-515(1997) [PubMed] [EuropePMC]
This publication is cited by 3 other entries.
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Anandamide amidohydrolase of porcine brain: cDNA cloning, functional expression and site-directed mutagenesis.
Goparaju S.K., Kurahashi Y., Suzuki H., Ueda N., Yamamoto S.
Anandamide (arachidonoylethanolamide) is an endogenous ligand for cannabinoid receptors, and its cannabimimetic activities are lost when the compound is hydrolyzed to arachidonic acid and ethanolamine by an enzyme referred to as anandamide amidohydrolase. We cloned a cDNA for the enzyme of porcine ... >> More
Anandamide (arachidonoylethanolamide) is an endogenous ligand for cannabinoid receptors, and its cannabimimetic activities are lost when the compound is hydrolyzed to arachidonic acid and ethanolamine by an enzyme referred to as anandamide amidohydrolase. We cloned a cDNA for the enzyme of porcine brain, and the cDNA encoded a protein of 579 amino acids with a molecular mass of 62.9 kDa. The amino acid sequence was 81, 80 and 85% identical with the enzymes previously cloned from the liver of rat, mouse, and human, respectively. When the enzyme protein was overexpressed in COS-7 cells, the particulate fraction of the cells showed an anandamide hydrolyzing activity and also catalyzed the reverse reaction synthesizing anandamide from arachidonic acid and ethanolamine both with a specific activity of 0. 2-0.3 micromol/min/mg protein at 37 degrees C. The brain enzyme exhibited a wide substrate specificity hydrolyzing oleamide, 2-arachidonoylglycerol, and methyl arachidonate. The point mutation of Ser-217, Asp-237, Ser-241, or Cys-249 completely abolished the hydrolyses of all the above-mentioned substrates as well as the synthesis of anandamide in the reverse reaction. << Less
Biochim. Biophys. Acta 1441:77-84(1999) [PubMed] [EuropePMC]