| IED ID | IndEnz0005001132 |
| Enzyme Type ID | lipase001132 |
| Protein Name |
Pancreatic triacylglycerol lipase PL PTL Pancreatic lipase EC 3.1.1.3 Fragment |
| Gene Name | PNLIP |
| Organism | Myocastor coypus (Coypu) (Nutria) |
| 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 Glires (Rodents and rabbits) Rodentia Hystricomorpha Myocastoridae Myocastor Myocastor coypus (Coypu) (Nutria) |
| Enzyme Sequence | LLLGAVAGSEVCYDRLGCFSDDSPWAGIVERPLKVLPWSPSTINTRFLLYTNESPNNYQIVTADSSTIRSSNFRTDRKTRFIIHGYIDKGEENWLANMCEALLQVESVNCICVDWKGGSRALYTQATQNIRVVGAEVAYFVDALQSQLGYSPSNVHIIGHSLGSHVAGEAGRRTNGNIGRITGLDPAEPCFQGTPELVRLDPSDAQFVDVIHTDGAPIIPNLGFGMSQTVGHLDFFPNGGVEMPGCQKNIISQIVDINGIWEGTRDFAACNHLRSYKYYIDSILNPTGFAGFSCSSYNTFSSNNCFPCASGGCPQMGHYADRFSGKTNELFQQFYLNTGDASNFSRWRYQIAVTLSGRKVTGHVLVSLYGSGGTSKQYEIYKGSLQPGTSYVNQIDSDVDVGDIEKVKFIWYNNIINPTLPKVGASSIQVTRNDGRVFNFCSQDTVREDILLTLTPC |
| Enzyme Length | 457 |
| Uniprot Accession Number | Q64425 |
| Absorption | |
| Active Site | ACT_SITE 161; /note=Nucleophile; /evidence=ECO:0000250; ACT_SITE 185; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU10037; ACT_SITE 272; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU10037 |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by bile salts, is reactivated by (pro)colipase/CLPS. {ECO:0000250|UniProtKB:P16233}. |
| 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:P16233};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12045; Evidence={ECO:0000250|UniProtKB:P16233}; 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:0000250|UniProtKB:P16233};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40476; Evidence={ECO:0000250|UniProtKB:P16233}; 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:0000250|UniProtKB:P16233};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38576; Evidence={ECO:0000250|UniProtKB:P16233}; CATALYTIC ACTIVITY: Reaction=all-trans-retinyl hexadecanoate + H2O = all-trans-retinol + H(+) + hexadecanoate; Xref=Rhea:RHEA:13933, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17336, ChEBI:CHEBI:17616; Evidence={ECO:0000250|UniProtKB:P16233};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13934; Evidence={ECO:0000250|UniProtKB:P16233}; CATALYTIC ACTIVITY: Reaction=1,2-di-(9Z-octadecenoyl)-glycerol + H2O = (9Z)-octadecenoate + (9Z-octadecenoyl)-glycerol + H(+); Xref=Rhea:RHEA:38455, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:52323, ChEBI:CHEBI:75937; Evidence={ECO:0000250|UniProtKB:P16233};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38456; Evidence={ECO:0000250|UniProtKB:P16233}; |
| DNA Binding | |
| EC Number | 3.1.1.3 |
| Enzyme Function | FUNCTION: Plays an important role in fat metabolism. It preferentially splits the esters of long-chain fatty acids at positions 1 and 3, producing mainly 2-monoacylglycerol and free fatty acids, and shows considerably higher activity against insoluble emulsified substrates than against soluble ones. {ECO:0000250|UniProtKB:P16233}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (1); Disulfide bond (6); Domain (1); Glycosylation (1); Metal binding (4); Non-terminal residue (1); Signal peptide (1) |
| Keywords | Calcium;Disulfide bond;Glycoprotein;Hydrolase;Lipid degradation;Lipid metabolism;Metal-binding;Secreted;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P16233}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL <1..7; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 50,209 |
| Kinetics | |
| Metal Binding | METAL 196; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000250; METAL 199; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000250; METAL 201; /note=Calcium; /evidence=ECO:0000250; METAL 204; /note=Calcium; /evidence=ECO:0000250 |
| Rhea ID | RHEA:12044; RHEA:12045; RHEA:40475; RHEA:40476; RHEA:38575; RHEA:38576; RHEA:13933; RHEA:13934; RHEA:38455; RHEA:38456 |
| Cross Reference Brenda |