Detail Information for IndEnz0005000433
IED ID IndEnz0005000433
Enzyme Type ID lipase000433
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