IED Industry Enzyme Database

Detail Information for IndEnz0005000024
IED ID IndEnz0005000024
Enzyme Type ID lipase000024
Protein Name Bile salt-activated lipase
BAL
EC 3.1.1.13
EC 3.1.1.3
EC 3.1.1.6
Bile salt-stimulated lipase
BSSL
Carboxyl ester lipase
Cholesterol esterase
Pancreatic lysophospholipase
Sterol esterase
Fragment
Gene Name CEL
Organism Bos taurus (Bovine)
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 Laurasiatheria Artiodactyla Ruminantia Pecora Bovidae Bovinae Bos (oxen cattle) Bos taurus (Bovine)
Enzyme Sequence LGASRLGPSPGCLAVASAAKLGSVYTEGGFVEGVNKKLSLFGDSIDIFKGIPFAAAPKALEKPERHPGWQGTLKAKSFKKRCLQATLTQDSTYGNEDCLYLNIWVPQGRKEVSHDLPVMIWIYGGAFLMGASQGANFLSNYLYDGEEIATRGNVIVVTFNYRVGPLGFLSTGDSNLPGNYGLWDQHMAIAWVKRNIEAFGGDPDNITLFGESAGGASVSLQTLSPYNKGLIKRAISQSGVGLCPWAIQQDPLFWAKRIAEKVGCPVDDTSKMAGCLKITDPRALTLAYKLPLGSTEYPKLHYLSFVPVIDGDFIPDDPVNLYANAADVDYIAGTNDMDGHLFVGMDVPAINSNKQDVTEEDFYKLVSGLTVTKGLRGANATYEVYTEPWAQDSSQETRKKTMVDLETDILFLIPTKIAVAQHKSHAKSANTYTYLFSQPSRMPIYPKWMGADHADDLQYVFGKPFATPLGYRAQDRTVSKAMIAYWTNFARTGDPNTGHSTVPANWDPYTLEDDNYLEINKQMDSNSMKLHLRTNYLQFWTQTYQALPTVTSAGASLLPPEDNSQASPVPPADNSGAPTEPSAGDSEVAQMPVVIGF
Enzyme Length 597
Uniprot Accession Number P30122
Absorption
Active Site ACT_SITE 212; /note=Acyl-ester intermediate; ACT_SITE 338; /note=Charge relay system; ACT_SITE 453; /note=Charge relay system
Activity Regulation ACTIVITY REGULATION: Activated by bile salts such as sodium taurocholate. {ECO:0000269|PubMed:10220579}.
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:0000250|UniProtKB:P19835};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12045; Evidence={ECO:0000250|UniProtKB:P19835}; 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:10220579};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38576; Evidence={ECO:0000305|PubMed:10220579}; CATALYTIC ACTIVITY: Reaction=1,2,3-trioctanoylglycerol + H2O = dioctanoylglycerol + H(+) + octanoate; Xref=Rhea:RHEA:47864, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:25646, ChEBI:CHEBI:76978, ChEBI:CHEBI:88066; Evidence={ECO:0000250|UniProtKB:P19835};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47865; Evidence={ECO:0000250|UniProtKB:P19835}; CATALYTIC ACTIVITY: Reaction=a sterol ester + H2O = a fatty acid + a sterol + H(+); Xref=Rhea:RHEA:10100, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15889, ChEBI:CHEBI:28868, ChEBI:CHEBI:35915; EC=3.1.1.13; Evidence={ECO:0000250|UniProtKB:P19835};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10101; Evidence={ECO:0000250|UniProtKB:P19835}; CATALYTIC ACTIVITY: Reaction=cholesteryl (9Z-octadecenoate) + H2O = (9Z)-octadecenoate + cholesterol + H(+); Xref=Rhea:RHEA:33875, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16113, ChEBI:CHEBI:30823, ChEBI:CHEBI:46898; Evidence={ECO:0000250|UniProtKB:P07882};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33876; Evidence={ECO:0000250|UniProtKB:P07882}; CATALYTIC ACTIVITY: Reaction=an acetyl ester + H2O = acetate + an aliphatic alcohol + H(+); Xref=Rhea:RHEA:12957, ChEBI:CHEBI:2571, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30089, ChEBI:CHEBI:47622; EC=3.1.1.6; Evidence={ECO:0000269|PubMed:10220579};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12958; Evidence={ECO:0000305|PubMed:10220579}; CATALYTIC ACTIVITY: Reaction=a butanoate ester + H2O = an aliphatic alcohol + butanoate + H(+); Xref=Rhea:RHEA:47348, ChEBI:CHEBI:2571, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17968, ChEBI:CHEBI:50477; Evidence={ECO:0000250|UniProtKB:P07882};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47349; Evidence={ECO:0000250|UniProtKB:P07882}; CATALYTIC ACTIVITY: Reaction=9-hexadecanoyloxy-octadecanoate + H2O = 9-hydroxy-octadecanoate + H(+) + hexadecanoate; Xref=Rhea:RHEA:52052, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:83670, ChEBI:CHEBI:136286; Evidence={ECO:0000250|UniProtKB:P19835};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52053; Evidence={ECO:0000250|UniProtKB:P19835}; CATALYTIC ACTIVITY: Reaction=9-(9Z-octadecenoyloxy)-octadecanoate + H2O = (9Z)-octadecenoate + 9-hydroxy-octadecanoate + H(+); Xref=Rhea:RHEA:52048, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:136282, ChEBI:CHEBI:136286; Evidence={ECO:0000250|UniProtKB:P19835};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52049; Evidence={ECO:0000250|UniProtKB:P19835}; 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:P07882};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40436; Evidence={ECO:0000250|UniProtKB:P07882}; CATALYTIC ACTIVITY: Reaction=12-hexadecanoyloxy-octadecanoate + H2O = 12-hydroxyoctadecanoate + H(+) + hexadecanoate; Xref=Rhea:RHEA:52056, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:83677, ChEBI:CHEBI:84201; Evidence={ECO:0000250|UniProtKB:Q64285};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52057; Evidence={ECO:0000250|UniProtKB:Q64285}; CATALYTIC ACTIVITY: Reaction=12-(9Z-octadecenoyloxy)-octadecanoate + H2O = (9Z)-octadecenoate + 12-hydroxyoctadecanoate + H(+); Xref=Rhea:RHEA:52060, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:84201, ChEBI:CHEBI:136302; Evidence={ECO:0000250|UniProtKB:Q64285};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52061; Evidence={ECO:0000250|UniProtKB:Q64285}; CATALYTIC ACTIVITY: Reaction=13-(9Z-octadecenoyloxy)-octadecanoate + H2O = (9Z)-octadecenoate + 13-hydroxy-octadecanoate + H(+); Xref=Rhea:RHEA:52064, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:136303, ChEBI:CHEBI:136304; Evidence={ECO:0000250|UniProtKB:Q64285};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52065; Evidence={ECO:0000250|UniProtKB:Q64285}; CATALYTIC ACTIVITY: Reaction=9-(9Z-hexadecenoyloxy)-octadecanoate + H2O = (9Z)-hexadecenoate + 9-hydroxy-octadecanoate + H(+); Xref=Rhea:RHEA:52068, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:32372, ChEBI:CHEBI:136286, ChEBI:CHEBI:136309; Evidence={ECO:0000250|UniProtKB:Q64285};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52069; Evidence={ECO:0000250|UniProtKB:Q64285}; CATALYTIC ACTIVITY: Reaction=12-(9Z-hexadecenoyloxy)-octadecanoate + H2O = (9Z)-hexadecenoate + 12-hydroxyoctadecanoate + H(+); Xref=Rhea:RHEA:52072, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:32372, ChEBI:CHEBI:84201, ChEBI:CHEBI:136312; Evidence={ECO:0000250|UniProtKB:Q64285};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52073; Evidence={ECO:0000250|UniProtKB:Q64285}; CATALYTIC ACTIVITY: Reaction=13-(9Z-hexadecenoyloxy)-octadecanoate + H2O = (9Z)-hexadecenoate + 13-hydroxy-octadecanoate + H(+); Xref=Rhea:RHEA:52076, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:32372, ChEBI:CHEBI:136304, ChEBI:CHEBI:136315; Evidence={ECO:0000250|UniProtKB:Q64285};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52077; Evidence={ECO:0000250|UniProtKB:Q64285}; CATALYTIC ACTIVITY: Reaction=12-octadecanoyloxy-octadecanoate + H2O = 12-hydroxyoctadecanoate + H(+) + octadecanoate; Xref=Rhea:RHEA:52080, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:25629, ChEBI:CHEBI:84201, ChEBI:CHEBI:136330; Evidence={ECO:0000250|UniProtKB:Q64285};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52081; Evidence={ECO:0000250|UniProtKB:Q64285}; CATALYTIC ACTIVITY: Reaction=13-octadecanoyloxy-octadecanoate + H2O = 13-hydroxy-octadecanoate + H(+) + octadecanoate; Xref=Rhea:RHEA:52084, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:25629, ChEBI:CHEBI:136304, ChEBI:CHEBI:136335; Evidence={ECO:0000250|UniProtKB:Q64285};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52085; Evidence={ECO:0000250|UniProtKB:Q64285}; CATALYTIC ACTIVITY: Reaction=5-(9Z-hexadecenoyloxy)-octadecanoate + H2O = (9Z)-hexadecenoate + 5-hydroxy-octadecanoate + H(+); Xref=Rhea:RHEA:52092, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:32372, ChEBI:CHEBI:136369, ChEBI:CHEBI:136370; Evidence={ECO:0000250|UniProtKB:Q64285};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52093; Evidence={ECO:0000250|UniProtKB:Q64285}; CATALYTIC ACTIVITY: Reaction=9-octadecanoyloxy-octadecanoate + H2O = 9-hydroxy-octadecanoate + H(+) + octadecanoate; Xref=Rhea:RHEA:52096, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:25629, ChEBI:CHEBI:136286, ChEBI:CHEBI:136373; Evidence={ECO:0000250|UniProtKB:Q64285};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52097; Evidence={ECO:0000250|UniProtKB:Q64285};
DNA Binding
EC Number 3.1.1.13; 3.1.1.3; 3.1.1.6
Enzyme Function FUNCTION: Catalyzes the hydrolysis of a wide range of substrates including cholesteryl esters, phospholipids, lysophospholipids, di- and tri-acylglycerols, and fatty acid esters of hydroxy fatty acids (FAHFA) (PubMed:10220579). Preferentially hydrolyzes FAHFAs with the ester bond further away from the carboxylate. Unsaturated FAHFAs are hydrolyzed more quickly than saturated FAHFAs (By similarity). Has an essential role in the complete digestion of dietary lipids and their intestinal absorption, along with the absorption of fat-soluble vitamins (By similarity). {ECO:0000250|UniProtKB:P19835, ECO:0000250|UniProtKB:Q64285, ECO:0000269|PubMed:10220579}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (3); Beta strand (26); Chain (1); Compositional bias (1); Disulfide bond (2); Glycosylation (2); Helix (29); Non-terminal residue (1); Region (1); Sequence conflict (2); Signal peptide (1); Turn (5)
Keywords 3D-structure;Direct protein sequencing;Disulfide bond;Glycoprotein;Hydrolase;Lipid degradation;Lipid metabolism;Reference proteome;Secreted;Serine esterase;Signal
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P19835}.
Modified Residue
Post Translational Modification
Signal Peptide SIGNAL <1..18; /evidence=ECO:0000269|PubMed:10220579
Structure 3D X-ray crystallography (3)
Cross Reference PDB 1AKN; 1AQL; 2BCE;
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 65,162
Kinetics
Metal Binding
Rhea ID RHEA:12044; RHEA:12045; RHEA:38575; RHEA:38576; RHEA:47864; RHEA:47865; RHEA:10100; RHEA:10101; RHEA:33875; RHEA:33876; RHEA:12957; RHEA:12958; RHEA:47348; RHEA:47349; RHEA:52052; RHEA:52053; RHEA:52048; RHEA:52049; RHEA:40435; RHEA:40436; RHEA:52056; RHEA:52057; RHEA:52060; RHEA:52061; RHEA:52064; RHEA:52065; RHEA:52068; RHEA:52069; RHEA:52072; RHEA:52073; RHEA:52076; RHEA:52077; RHEA:52080; RHEA:52081; RHEA:52084; RHEA:52085; RHEA:52092; RHEA:52093; RHEA:52096; RHEA:52097
Cross Reference Brenda