IED Industry Enzyme Database

Detail Information for IndEnz0005001134
IED ID IndEnz0005001134
Enzyme Type ID lipase001134
Protein Name Endothelial lipase
EC 3.1.1.3
Endothelial cell-derived lipase
EDL
EL
Phospholipase A1
EC 3.1.1.32
Gene Name LIPG UNQ387/PRO719
Organism Homo sapiens (Human)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Primates Haplorrhini Simiiformes Catarrhini Hominoidea (apes) Hominidae (great apes) Homininae Homo Homo sapiens (Human)
Enzyme Sequence MSNSVPLLCFWSLCYCFAAGSPVPFGPEGRLEDKLHKPKATQTEVKPSVRFNLRTSKDPEHEGCYLSVGHSQPLEDCSFNMTAKTFFIIHGWTMSGIFENWLHKLVSALHTREKDANVVVVDWLPLAHQLYTDAVNNTRVVGHSIARMLDWLQEKDDFSLGNVHLIGYSLGAHVAGYAGNFVKGTVGRITGLDPAGPMFEGADIHKRLSPDDADFVDVLHTYTRSFGLSIGIQMPVGHIDIYPNGGDFQPGCGLNDVLGSIAYGTITEVVKCEHERAVHLFVDSLVNQDKPSFAFQCTDSNRFKKGICLSCRKNRCNSIGYNAKKMRNKRNSKMYLKTRAGMPFRVYHYQMKIHVFSYKNMGEIEPTFYVTLYGTNADSQTLPLEIVERIEQNATNTFLVYTEEDLGDLLKIQLTWEGASQSWYNLWKEFRSYLSQPRNPGRELNIRRIRVKSGETQRKLTFCTEDPENTSISPGRELWFRKCRDGWRMKNETSPTVELP
Enzyme Length 500
Uniprot Accession Number Q9Y5X9
Absorption
Active Site ACT_SITE 169; /note=Nucleophile; /evidence=ECO:0000250; ACT_SITE 193; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU10037; ACT_SITE 274; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU10037
Activity Regulation ACTIVITY REGULATION: Inhibited by serum and NaCl. {ECO:0000269|PubMed:12032167}.
Binding Site
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=a triacylglycerol + H2O = a diacylglycerol + a fatty acid + H(+); Xref=Rhea:RHEA:12044, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17855, ChEBI:CHEBI:18035, ChEBI:CHEBI:28868; EC=3.1.1.3; Evidence={ECO:0000269|PubMed:10192396, ECO:0000269|PubMed:10318835, ECO:0000269|PubMed:12032167}; CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 2-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:18689, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:57643, ChEBI:CHEBI:57875; EC=3.1.1.32; Evidence={ECO:0000269|PubMed:12032167}; CATALYTIC ACTIVITY: Reaction=1,2,3-tri-(9Z-octadecenoyl)-glycerol + H2O = (9Z)-octadecenoate + di-(9Z)-octadecenoylglycerol + H(+); Xref=Rhea:RHEA:38575, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:53753, ChEBI:CHEBI:75945; Evidence={ECO:0000269|PubMed:12032167};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38576; Evidence={ECO:0000305|PubMed:12032167}; CATALYTIC ACTIVITY: Reaction=1,2,3-tributanoylglycerol + H2O = butanoate + dibutanoylglycerol + H(+); Xref=Rhea:RHEA:40475, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17968, ChEBI:CHEBI:35020, ChEBI:CHEBI:76478; Evidence={ECO:0000269|PubMed:12032167};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40476; Evidence={ECO:0000305|PubMed:12032167}; CATALYTIC ACTIVITY: Reaction=1,2-dihexadecanoyl-sn-glycero-3-phosphocholine + H2O = H(+) + hexadecanoate + hexadecanoyl-sn-glycero-3-phosphocholine; Xref=Rhea:RHEA:41384, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:64563, ChEBI:CHEBI:72999; Evidence={ECO:0000269|PubMed:12032167};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41385; Evidence={ECO:0000305|PubMed:12032167};
DNA Binding
EC Number 3.1.1.3; 3.1.1.32
Enzyme Function FUNCTION: Exerts both phospholipase and triglyceride lipase activities (PubMed:12032167, PubMed:10318835, PubMed:10192396). More active as a phospholipase than a triglyceride lipase (PubMed:12032167). Hydrolyzes triglycerides, both with short-chain fatty acyl groups (tributyrin) and long-chain fatty acyl groups (triolein) with similar levels of activity toward both types of substrates (PubMed:12032167). Hydrolyzes high density lipoproteins (HDL) more efficiently than other lipoproteins (PubMed:12032167, PubMed:10192396). {ECO:0000269|PubMed:10192396, ECO:0000269|PubMed:10318835, ECO:0000269|PubMed:12032167}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (3); Alternative sequence (2); Chain (1); Disulfide bond (5); Domain (1); Glycosylation (5); Natural variant (4); Region (1); Sequence conflict (1); Signal peptide (1)
Keywords Alternative splicing;Disulfide bond;Glycoprotein;Heparin-binding;Hydrolase;Lipid degradation;Lipid metabolism;Reference proteome;Secreted;Signal
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10318835}.
Modified Residue
Post Translational Modification
Signal Peptide SIGNAL 1..20; /evidence=ECO:0000255
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID 12164779; 12569156; 12601178; 12867537; 12884003; 14517167; 15117821; 15231747; 15342690; 15485805; 15576837; 15961789; 16023652; 16039280; 16877778; 16940551; 16980590; 17016617; 17093291; 17322565; 17356047; 17495604; 17526978; 17545692; 17570372; 17651673; 17700364; 17822686; 17986713; 18039650; 18193043; 18193044; 18683147; 18988890; 18996102; 19060906; 19060911; 19136670; 19148283; 19287092; 19380136; 19411665; 19411705; 19578796; 19780863; 19878569; 19913121; 19948975; 20031538; 20045866; 20167577; 20370913; 20394740; 20466371; 20571754; 20602615; 20621031; 20628086; 20679960; 20688330; 20691829; 20711500; 20855565; 20923576; 20972250; 21122200; 21130993; 21145773; 21816559; 21852675; 21957202; 22174694; 22464213; 22723003; 22740344; 22952570; 22972429; 23075452; 23109900; 23243195; 23510199; 23673478; 23991054; 24115033; 24458708; 24634127; 24852509; 24886585; 25250890; 25291260; 26124511; 26447519; 27045898; 27430252; 27431295; 27590083; 27600285; 27612170; 28546217; 29350614; 30150432; 30621702; 30651409; 30653260; 30657227; 31020688; 31216999; 31220617; 31473149; 31923467; 32572177; 32667032; 32893849; 33882321; 34001944;
Motif
Gene Encoded By
Mass 56,795
Kinetics
Metal Binding
Rhea ID RHEA:12044; RHEA:18689; RHEA:38575; RHEA:38576; RHEA:40475; RHEA:40476; RHEA:41384; RHEA:41385
Cross Reference Brenda