| 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 |