IED ID | IndEnz0010000014 |
Enzyme Type ID | esterase000014 |
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 |