| IED ID | IndEnz0005000505 |
| Enzyme Type ID | lipase000505 |
| Protein Name |
Pancreatic triacylglycerol lipase PL Pancreatic lipase EC 3.1.1.3 |
| Gene Name | Pnlip |
| Organism | Rattus norvegicus (Rat) |
| 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 Myomorpha (mice and others) Muroidea Muridae Murinae Rattus Rattus norvegicus (Rat) |
| Enzyme Sequence | MLMLWTFAVLLGAVAGKEVCFDKLGCFSDDAPWSGTIDRPLKALPWSPAQINTRFLLYTNENQDNYQKITSDASSIRNSNFKTNRKTRIIIHGFIDKGEENWLSDMCKNMFKVESVNCICVDWKGGSRATYTQATQNVRVVGAEVALLVNVLKSDLGHPPDNVHLIGHSLGSHVAGEAGKRTFGAIGRITGLDAAEPYFQGTPEEVRLDPTDAQFVDAIHTDAAPIIPNLGFGMSQTVGHLDFFPNGGMEMPGCQKNILSQIVDIDGIWEGTRDFAACNHLRSYKYYTDSIVNPTGFSGFSCSSYNVFSANKCFPCGSEGCPQMGHYADKYPGKTKELYQKFYLNTGDKSNFARWRYQVTVTLSGQKVTGHILVSLFGNGGNSKQYEVFKGSLHPGDTHVKEFDSDMDVGDLQKVKFIWYNNVINPTLPKVGASRISVERNDGRVFNFCSQDTVREDVLLTLSAC |
| Enzyme Length | 465 |
| Uniprot Accession Number | P27657 |
| Absorption | |
| Active Site | ACT_SITE 169; /note=Nucleophile; /evidence=ECO:0000250; ACT_SITE 193; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU10037; ACT_SITE 280; /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:0000269|PubMed:8203536}. |
| 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:10769148};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12045; Evidence={ECO:0000305|PubMed:10769148}; 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:10769148, ECO:0000269|PubMed:8203536};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38576; Evidence={ECO:0000305|PubMed:10769148, ECO:0000305|PubMed:8203536}; 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=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:0000269|PubMed:10769148, ECO:0000269|PubMed:8203536}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (1); Disulfide bond (6); Domain (1); Metal binding (4); Signal peptide (1) |
| Keywords | Calcium;Direct protein sequencing;Disulfide bond;Hydrolase;Lipid degradation;Lipid metabolism;Metal-binding;Reference proteome;Secreted;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:8203536}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..16; /evidence=ECO:0000269|PubMed:8486693 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 15181189; 15883013; 17010228; 8656075; 8967484; |
| Motif | |
| Gene Encoded By | |
| Mass | 51,440 |
| Kinetics | |
| Metal Binding | METAL 204; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000250; METAL 207; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000250; METAL 209; /note=Calcium; /evidence=ECO:0000250; METAL 212; /note=Calcium; /evidence=ECO:0000250 |
| Rhea ID | RHEA:12044; RHEA:12045; RHEA:38575; RHEA:38576; RHEA:40475; RHEA:40476; RHEA:13933; RHEA:13934; RHEA:38455; RHEA:38456 |
| Cross Reference Brenda |