IED Industry Enzyme Database

Detail Information for IndEnz0005000005
IED ID IndEnz0005000005
Enzyme Type ID lipase000005
Protein Name Hepatic triacylglycerol lipase
HL
Hepatic lipase
EC 3.1.1.3
Lipase member C
Lysophospholipase
EC 3.1.1.5
Phospholipase A1
EC 3.1.1.32
Gene Name LIPC HTGL
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 MDTSPLCFSILLVLCIFIQSSALGQSLKPEPFGRRAQAVETNKTLHEMKTRFLLFGETNQGCQIRINHPDTLQECGFNSSLPLVMIIHGWSVDGVLENWIWQMVAALKSQPAQPVNVGLVDWITLAHDHYTIAVRNTRLVGKEVAALLRWLEESVQLSRSHVHLIGYSLGAHVSGFAGSSIGGTHKIGRITGLDAAGPLFEGSAPSNRLSPDDANFVDAIHTFTREHMGLSVGIKQPIGHYDFYPNGGSFQPGCHFLELYRHIAQHGFNAITQTIKCSHERSVHLFIDSLLHAGTQSMAYPCGDMNSFSQGLCLSCKKGRCNTLGYHVRQEPRSKSKRLFLVTRAQSPFKVYHYQFKIQFINQTETPIQTTFTMSLLGTKEKMQKIPITLGKGIASNKTYSFLITLDVDIGELIMIKFKWENSAVWANVWDTVQTIIPWSTGPRHSGLVLKTIRVKAGETQQRMTFCSENTDDLLLRPTQEKIFVKCEIKSKTSKRKIR
Enzyme Length 499
Uniprot Accession Number P11150
Absorption
Active Site ACT_SITE 168; /note=Nucleophile; /evidence=ECO:0000250; ACT_SITE 194; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU10037; ACT_SITE 279; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU10037
Activity Regulation ACTIVITY REGULATION: Phospholipase A1 and triacylglycerol lipase are inhibited by sphingomyelin. {ECO:0000269|PubMed:26193433}.
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:12032167, ECO:0000269|PubMed:26193433, ECO:0000269|PubMed:7592706, ECO:0000269|PubMed:8798474}; CATALYTIC ACTIVITY: Reaction=a 1-acyl-sn-glycero-3-phosphocholine + H2O = a fatty acid + H(+) + sn-glycerol 3-phosphocholine; Xref=Rhea:RHEA:15177, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16870, ChEBI:CHEBI:28868, ChEBI:CHEBI:58168; EC=3.1.1.5; Evidence={ECO:0000250|UniProtKB:P07867}; 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, ECO:0000269|PubMed:26193433, ECO:0000269|PubMed:7592706}; 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, ECO:0000269|PubMed:7592706, ECO:0000269|PubMed:8798474};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38576; Evidence={ECO:0000305|PubMed:7592706}; CATALYTIC ACTIVITY: Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + H2O = (9Z)-octadecenoate + (9Z-octadecenoyl)-sn-glycero-3-phosphocholine + H(+); Xref=Rhea:RHEA:38699, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:74669, ChEBI:CHEBI:76083; Evidence={ECO:0000269|PubMed:7592706};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38700; Evidence={ECO:0000305|PubMed:7592706}; 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:7592706};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40476; Evidence={ECO:0000305|PubMed:7592706}; 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}; CATALYTIC ACTIVITY: Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycerol + H2O = (9Z)-octadecenoate + 2-(9Z-octadecenoyl)-glycerol + H(+); Xref=Rhea:RHEA:38511, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:52333, ChEBI:CHEBI:73990; Evidence={ECO:0000250|UniProtKB:P07867};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38512; Evidence={ECO:0000250|UniProtKB:P07867}; CATALYTIC ACTIVITY: Reaction=1,2,3-tri-(9Z-octadecenoyl)-glycerol + H2O = (9Z)-octadecenoate + 2,3-di-(9Z)-octadecenoyl-sn-glycerol + H(+); Xref=Rhea:RHEA:38391, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:53753, ChEBI:CHEBI:75824; Evidence={ECO:0000250|UniProtKB:P07867};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38392; Evidence={ECO:0000250|UniProtKB:P07867}; CATALYTIC ACTIVITY: Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phospho-L-serine + H2O = (9Z)-octadecenoate + H(+) + sn-glycero-3-phospho-L-serine; Xref=Rhea:RHEA:40499, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:64765, ChEBI:CHEBI:74617; Evidence={ECO:0000250|UniProtKB:P07867};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40500; Evidence={ECO:0000250|UniProtKB:P07867}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-sn-glycero-3-phosphocholine + H2O = H(+) + hexadecanoate + sn-glycerol 3-phosphocholine; Xref=Rhea:RHEA:40435, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16870, ChEBI:CHEBI:72998; Evidence={ECO:0000250|UniProtKB:P07867};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40436; Evidence={ECO:0000250|UniProtKB:P07867}; CATALYTIC ACTIVITY: Reaction=1,3-di-(9Z-octadecenoyl)-glycerol + H2O = (9Z)-octadecenoate + 3-(9Z-octadecenoyl)-sn-glycerol + H(+); Xref=Rhea:RHEA:38651, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:75735, ChEBI:CHEBI:75938; Evidence={ECO:0000250|UniProtKB:P07867};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38652; Evidence={ECO:0000250|UniProtKB:P07867};
DNA Binding
EC Number 3.1.1.3; 3.1.1.5; 3.1.1.32
Enzyme Function FUNCTION: Catalyzes the hydrolysis of triglycerides and phospholipids present in circulating plasma lipoproteins, including chylomicrons, intermediate density lipoproteins (IDL), low density lipoproteins (LDL) of large size and high density lipoproteins (HDL), releasing free fatty acids (FFA) and smaller lipoprotein particles (PubMed:7592706, PubMed:8798474, PubMed:12032167, PubMed:26193433). Also exhibits lysophospholipase activity (By similarity). Can hydrolyze both neutral lipid and phospholipid substrates but shows a greater binding affinity for neutral lipid substrates than phospholipid substrates (By similarity). In native LDL, preferentially hydrolyzes the phosphatidylcholine species containing polyunsaturated fatty acids at sn-2 position (PubMed:26193433). {ECO:0000250|UniProtKB:P07867, ECO:0000269|PubMed:12032167, ECO:0000269|PubMed:26193433, ECO:0000269|PubMed:7592706, ECO:0000269|PubMed:8798474}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (3); Chain (1); Domain (1); Glycosylation (4); Mutagenesis (2); Natural variant (9); Region (1); Sequence conflict (1); Signal peptide (1)
Keywords Direct protein sequencing;Disease variant;Glycoprotein;HDL;Heparin-binding;Hydrolase;Lipid degradation;Lipid metabolism;Reference proteome;Secreted;Signal
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:2828141}.
Modified Residue
Post Translational Modification
Signal Peptide SIGNAL 1..22; /evidence=ECO:0000269|PubMed:2839510
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID 10487498; 10712408; 10894818; 10936588; 11171287; 11181756; 11322655; 11427182; 11427226; 11454011; 11512679; 11533368; 11916946; 11947893; 11968086; 11971936; 12006918; 12082592; 12116231; 12235167; 12354428; 12364471; 12364543; 12403660; 12417924; 12514935; 12544508; 12547874; 12642787; 12689525; 12691171; 12700335; 12777470; 12798568; 12818414; 12860265; 12883629; 12964943; 14531818; 14557872; 14564687; 14585761; 14608050; 14615390; 14650352; 14657196; 14679168; 14709367; 14967812; 14985399; 15099346; 15135251; 15135253; 15156410; 15205216; 15284087; 15292235; 15292318; 15304509; 15379569; 15608561; 15656877; 15657615; 15721010; 15755868; 15817871; 15821100; 15855254; 15941898; 15949705; 15961789; 15979432; 15983229; 15983323; 16005462; 16030523; 16038892; 16039291; 16077949; 16115483; 16141008; 16153627; 16164573; 16205020; 16316842; 16324926; 16330034; 16338252; 16343038; 16419358; 16427731; 16449872; 16542392; 16554020; 16570154; 16603721; 1671786; 16770077; 16793047; 16822236; 16879193; 16928730; 17080261; 17137217; 17157861; 17175070; 17234195; 17318300; 17327141; 17342071; 17390085; 17399967; 17406067; 17428321; 17440012; 17537154; 17568951; 17700364; 17855807; 17919884; 17994020; 18001531; 18059528; 18084291; 18160998; 18164013; 18193043; 18193044; 18249219; 18275964; 18354102; 18413186; 18468200; 18510853; 18513389; 18592285; 18599739; 18622260; 18636124; 18641720; 18660489; 18675312; 18676680; 18724972; 18758746; 18927546; 18978678; 18996102; 19034316; 19043545; 19052449; 19056482; 19060906; 19060910; 19060911; 19088157; 19101670; 19131662; 19136429; 19148283; 19155102; 19155782; 19170196; 19263529; 19285487; 19336370; 19350521; 19367320; 19420105; 19428034; 19429860; 19479237; 19489872; 19528346; 19534808; 19558527; 19578796; 19625176; 19656773; 19689828; 19691831; 19692168; 19695855; 19734193; 19773416; 19783858; 19810818; 19876004; 19878569; 19913121; 19936222; 20031551; 20125193; 20160193; 20167577; 20186155; 20222961; 20373033; 20384434; 20385819; 20385826; 20400780; 20403997; 20430392; 20444273; 20452482; 20492333; 20536507; 20565774; 20595410; 20602615; 20628086; 20634891; 20673868; 20679960; 20682687; 20822508; 20851298; 20855565; 20888482; 21139980; 21189265; 21252145; 21261091; 21352420; 21371711; 21447484; 21447678; 21548985; 21750705; 21960661; 21986251; 21988832; 22047520; 22073289; 22262398; 22294764; 22385360; 22449147; 22464213; 22935046; 23109900; 23343765; 23348725; 23351562; 23457133; 23874450; 23991054; 24124978; 24223199; 24458708; 24909692; 25010633; 25117371; 25239670; 25550127; 25926410; 26101956; 26282880; 26503844; 26839156; 27573733; 27846285; 29244870; 29883758; 30015857; 30322388; 30399423; 30600300; 30685440; 31077211; 31358896; 31640222; 31947886; 32196671; 32603185; 32617858; 33004870; 33499410; 33673789; 8300609; 8485124; 9114024; 9379936; 9409263; 9486964; 9741704; 9812910;
Motif
Gene Encoded By
Mass 55,914
Kinetics BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=16 mM for 1,2,3-tri-(9Z-octadecenoyl)-glycerol {ECO:0000269|PubMed:8798474}; Vmax=1.4 umol/min/ug enzyme with 1,2,3-tri-(9Z-octadecenoyl)-glycerol as substrate {ECO:0000269|PubMed:8798474};
Metal Binding
Rhea ID RHEA:12044; RHEA:15177; RHEA:18689; RHEA:38575; RHEA:38576; RHEA:38699; RHEA:38700; RHEA:40475; RHEA:40476; RHEA:41384; RHEA:41385; RHEA:38511; RHEA:38512; RHEA:38391; RHEA:38392; RHEA:40499; RHEA:40500; RHEA:40435; RHEA:40436; RHEA:38651; RHEA:38652
Cross Reference Brenda