IED ID | IndEnz0010000995 |
Enzyme Type ID | esterase000995 |
Protein Name |
Monoglyceride lipase faah-4 EC 3.1.1.23 Fatty acid amide hydrolase 4 EC 3.5.1.99 |
Gene Name | faah-4 Y56A3A.12 |
Organism | Caenorhabditis elegans |
Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Protostomia Ecdysozoa Nematoda (roundworms) Chromadorea Rhabditida Rhabditina Rhabditomorpha Rhabditoidea Rhabditidae Peloderinae Caenorhabditis Caenorhabditis elegans |
Enzyme Sequence | MGNNFWSTWSPSQRIFSLIWPATILYLIMKLLIEKMWGKNRGAVERFQTRREALFDDFKSRSAPASLVNNPRIVKGNETAEQIETTFNEILKLDLIALKSALQTDKYNAYTVLCAFVWRAIDVNSEINCITEVIREAFNTAEALDDNYAQTGEKGQLFGLPFSVKSNFYMENYDVTVGLAKLLEQPKTTTCPMVQFLSDQGAVPFCLTNVPQGLLSYVSSNPIYGTTKNPWDFSRTPGGSSGGEAALLAAGGAAFGIGSDLAGSLRIPAAFCGLVTLKPTQDRLCVTDTHGGLPGRGRLGLSFGFYTRSVKEQEFLLGLIVGRSEYLELCPMSSPAKLEKHIEKDQKLVIGWFVDDGFNPVVPSNRRAVEETVKSLQAKGHQVVELKLADVSEEFPPFAVADMLFRNVMPDNGAYMSEMYAGEQYDEHMKLFIRLVCLKQNFLVSFLLRYGVMPFAKLALSKRLACIGSAYNSDLAACRQNQENTDSYKLQWIRYWKSKKIDALICPSFITPAQPFEYPAQLSNGAFITGLFNMLDVPAGVVPVSPVNQKDVDQLIDGFSTEGDLLLKKQREAARGTTGLPNAVQVVTLPNCEEMCLRVMRLVEESAEGVQRLQWRVGASAAPIDVENTPAGVVSSLEHFERVNLLH |
Enzyme Length | 647 |
Uniprot Accession Number | Q9U217 |
Absorption | |
Active Site | ACT_SITE 165; /note=Charge relay system; /evidence=ECO:0000250|UniProtKB:P97612; ACT_SITE 240; /note=Charge relay system; /evidence=ECO:0000250|UniProtKB:P97612; ACT_SITE 264; /note=Acyl-ester intermediate; /evidence=ECO:0000250|UniProtKB:P97612 |
Activity Regulation | ACTIVITY REGULATION: Inhibited by the benzodioxole 4-[bis(1,3-benzodioxol-5-yl)-hydroxymethyl]-1-piperidinecarboxylic acid (4-nitrophenyl) ester (JZL184). {ECO:0000269|PubMed:30911178}. |
Binding Site | |
Calcium Binding | |
catalytic Activity | CATALYTIC ACTIVITY: Reaction=Hydrolyzes glycerol monoesters of long-chain fatty acids.; EC=3.1.1.23; Evidence={ECO:0000269|PubMed:30911178}; CATALYTIC ACTIVITY: Reaction=H2O + N-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-ethanolamine = (5Z,8Z,11Z,14Z)-eicosatetraenoate + ethanolamine; Xref=Rhea:RHEA:26136, ChEBI:CHEBI:2700, ChEBI:CHEBI:15377, ChEBI:CHEBI:32395, ChEBI:CHEBI:57603; EC=3.5.1.99; Evidence={ECO:0000269|PubMed:30911178}; CATALYTIC ACTIVITY: Reaction=2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-glycerol + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + glycerol + H(+); Xref=Rhea:RHEA:26132, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17754, ChEBI:CHEBI:32395, ChEBI:CHEBI:52392; Evidence={ECO:0000269|PubMed:30911178}; |
DNA Binding | |
EC Number | 3.1.1.23; 3.5.1.99 |
Enzyme Function | FUNCTION: Converts monoacylglycerides to free fatty acids and glycerol (PubMed:30911178). Hydrolyzes the endocannabinoid 2-arachidonoylglycerol (2-AG), and thereby regulates the degradation of endocannabinoid-related monoacylglycerides (PubMed:30911178). Also hydrolyzes arachidonoyl ethanolamide (anandamide, or AEA), but with low efficiency (PubMed:30911178). Plays a role in the regulation of longevity and resistance to oxidative stress (PubMed:30911178). {ECO:0000269|PubMed:30911178}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Active site (3); Alternative sequence (1); Chain (1) |
Keywords | Alternative splicing;Hydrolase;Lipid degradation;Lipid metabolism;Reference proteome;Serine esterase |
Interact With | |
Induction | |
Subcellular Location | |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | 10778742; 11381264; 20439776; 21085631; 21110867; 21177967; 21367940; 22267497; 22560298; 23800452; 24884423; 25378320; 25487147; 30140741; 6593563; |
Motif | |
Gene Encoded By | |
Mass | 71,729 |
Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: Vmax=19.4 pmol/min/mg enzyme towards arachidonoyl ethanolamide (at 37 degrees Celsius) {ECO:0000269|PubMed:30911178}; Vmax=1200.8 pmol/min/mg enzyme towards endocannabinoid 2-arachidonoylglycerol (at 37 degrees Celsius) {ECO:0000269|PubMed:30911178}; |
Metal Binding | |
Rhea ID | RHEA:26136; RHEA:26132 |
Cross Reference Brenda |