| IED ID | IndEnz0005000606 |
| Enzyme Type ID | lipase000606 |
| Protein Name |
Pancreatic triacylglycerol lipase PL PTL Pancreatic lipase EC 3.1.1.3 |
| Gene Name | PNLIP |
| Organism | Homo sapiens (Human) |
| 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 Primates Haplorrhini Simiiformes Catarrhini Hominoidea (apes) Hominidae (great apes) Homininae Homo Homo sapiens (Human) |
| Enzyme Sequence | MLPLWTLSLLLGAVAGKEVCYERLGCFSDDSPWSGITERPLHILPWSPKDVNTRFLLYTNENPNNFQEVAADSSSISGSNFKTNRKTRFIIHGFIDKGEENWLANVCKNLFKVESVNCICVDWKGGSRTGYTQASQNIRIVGAEVAYFVEFLQSAFGYSPSNVHVIGHSLGAHAAGEAGRRTNGTIGRITGLDPAEPCFQGTPELVRLDPSDAKFVDVIHTDGAPIVPNLGFGMSQVVGHLDFFPNGGVEMPGCKKNILSQIVDIDGIWEGTRDFAACNHLRSYKYYTDSIVNPDGFAGFPCASYNVFTANKCFPCPSGGCPQMGHYADRYPGKTNDVGQKFYLDTGDASNFARWRYKVSVTLSGKKVTGHILVSLFGNKGNSKQYEIFKGTLKPDSTHSNEFDSDVDVGDLQMVKFIWYNNVINPTLPRVGASKIIVETNVGKQFNFCSPETVREEVLLTLTPC |
| Enzyme Length | 465 |
| Uniprot Accession Number | P16233 |
| Absorption | |
| Active Site | ACT_SITE 169; /note=Nucleophile; ACT_SITE 193; /note=Charge relay system; ACT_SITE 280; /note=Charge relay system |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by bile salts, is reactivated by (pro)colipase/CLPS. {ECO:0000269|PubMed:10769148}. |
| 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-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:0000269|PubMed:25862608};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40476; Evidence={ECO:0000269|PubMed:25862608}; 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:17401110};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38576; Evidence={ECO:0000305|PubMed:10769148, ECO:0000305|PubMed:17401110}; 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:0000269|PubMed:10769148};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13934; Evidence={ECO:0000305|PubMed:10769148}; 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:0000269|PubMed:17401110};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38456; Evidence={ECO:0000305|PubMed:17401110}; |
| 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:17401110}. |
| Temperature Dependency | |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7. {ECO:0000269|PubMed:17401110}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Beta strand (24); Chain (1); Disulfide bond (6); Domain (1); Glycosylation (1); Helix (12); Metal binding (4); Natural variant (1); Signal peptide (1); Turn (9) |
| Keywords | 3D-structure;Calcium;Disease variant;Disulfide bond;Glycoprotein;Hydrolase;Lipid degradation;Lipid metabolism;Metal-binding;Reference proteome;Secreted;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:25862608}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..16 |
| Structure 3D | X-ray crystallography (4) |
| Cross Reference PDB | 1GPL; 1LPA; 1LPB; 1N8S; |
| Mapped Pubmed ID | 11040182; 11393534; 12369922; 12667003; 14580194; 15316225; 16179352; 16385451; 16431912; 17269661; 18353248; 19113953; 19346257; 20136147; 20150178; 20936779; 22393262; 23918603; 24650780; 25239347; 27243230; 30789418; 31917686; 7893686; 8939760; |
| Motif | |
| Gene Encoded By | |
| Mass | 51,157 |
| Kinetics | |
| Metal Binding | METAL 204; /note=Calcium; via carbonyl oxygen; METAL 207; /note=Calcium; via carbonyl oxygen; METAL 209; /note=Calcium; METAL 212; /note=Calcium |
| 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 | 3.1.1.3; |