Detail Information for IndEnz0005000406
IED ID IndEnz0005000406
Enzyme Type ID lipase000406
Protein Name Gastric triacylglycerol lipase
GL
Gastric lipase
EC 3.1.1.3
Gene Name LIPF
Organism Canis lupus familiaris (Dog) (Canis familiaris)
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 Carnivora Caniformia Canidae (dog coyote wolf fox) Canis Canis lupus (Gray wolf) Canis lupus familiaris (Dog) (Canis familiaris)
Enzyme Sequence MWLLLTAASVISTLGTTHGLFGKLHPTNPEVTMNISQMITYWGYPAEEYEVVTEDGYILGIDRIPYGRKNSENIGRRPVAFLQHGLLASATNWISNLPNNSLAFILADAGYDVWLGNSRGNTWARRNLYYSPDSVEFWAFSFDEMAKYDLPATIDFILKKTGQDKLHYVGHSQGTTIGFIAFSTNPKLAKRIKTFYALAPVATVKYTETLLNKLMLVPSFLFKLIFGNKIFYPHHFFDQFLATEVCSRETVDLLCSNALFIICGFDTMNLNMSRLDVYLSHNPAGTSVQNVLHWSQAVKSGKFQAFDWGSPVQNMMHYHQSMPPYYNLTDMHVPIAVWNGGNDLLADPHDVDLLLSKLPNLIYHRKIPPYNHLDFIWAMDAPQAVYNEIVSMMGTDNK
Enzyme Length 398
Uniprot Accession Number P80035
Absorption
Active Site ACT_SITE 172; /note=Nucleophile; /evidence=ECO:0000269|PubMed:11689574; ACT_SITE 343; /note=Charge relay system; /evidence=ECO:0000269|PubMed:11689574; ACT_SITE 372; /note=Charge relay system; /evidence=ECO:0000269|PubMed:11689574
Activity Regulation ACTIVITY REGULATION: Inactivated by thiol reagents 5,5'- dithiobis(2-nitrobenzoic acid) and 4,4'-dithiopyridine. {ECO:0000269|PubMed:1935982}.
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:11689574, ECO:0000269|PubMed:1568562, ECO:0000269|PubMed:1935982}; CATALYTIC ACTIVITY: Reaction=1,2,3-tri-(9Z-octadecenoyl)-glycerol + H2O = (9Z)-octadecenoate + 1,2-di-(9Z-octadecenoyl)-sn-glycerol + H(+); Xref=Rhea:RHEA:39931, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:52333, ChEBI:CHEBI:53753; Evidence={ECO:0000250|UniProtKB:P07098};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39932; Evidence={ECO:0000250|UniProtKB:P07098}; CATALYTIC ACTIVITY: Reaction=1,2,3-trioctanoylglycerol + H2O = 1,2-dioctanoyl-sn-glycerol + H(+) + octanoate; Xref=Rhea:RHEA:40047, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:25646, ChEBI:CHEBI:76978, ChEBI:CHEBI:76979; Evidence={ECO:0000250|UniProtKB:P07098};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40048; Evidence={ECO:0000250|UniProtKB:P07098};
DNA Binding
EC Number 3.1.1.3
Enzyme Function FUNCTION: Catalyzes the hydrolysis of triacylglycerols to yield free fatty acids, diacylglycerol, monoacylglycerol, and glycerol (PubMed:1568562, PubMed:1935982, PubMed:11689574). Shows a preferential hydrolysis at the sn-3 position of triacylglycerol (By similarity). {ECO:0000250|UniProtKB:P07098, ECO:0000269|PubMed:11689574, ECO:0000269|PubMed:1568562, ECO:0000269|PubMed:1935982}.
Temperature Dependency
PH Dependency BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6 for short chain and medium-chain triacylglycerol and 4 for long-chain triacylglycerol (PubMed:1935982). Inactivated when pH is below 1.5 (PubMed:1568562). {ECO:0000269|PubMed:1568562, ECO:0000269|PubMed:1935982};
Pathway
nucleotide Binding
Features Active site (3); Beta strand (14); Chain (1); Disulfide bond (1); Domain (1); Glycosylation (4); Helix (22); Sequence conflict (1); Signal peptide (1); Turn (5)
Keywords 3D-structure;Direct protein sequencing;Disulfide bond;Glycoprotein;Hydrolase;Lipid degradation;Lipid metabolism;Reference proteome;Secreted;Signal
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:1568562}.
Modified Residue
Post Translational Modification
Signal Peptide SIGNAL 1..19; /evidence=ECO:0000269|PubMed:1935982
Structure 3D X-ray crystallography (1)
Cross Reference PDB 1K8Q;
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 45,131
Kinetics
Metal Binding
Rhea ID RHEA:12044; RHEA:39931; RHEA:39932; RHEA:40047; RHEA:40048
Cross Reference Brenda