| IED ID | IndEnz0005000028 |
| Enzyme Type ID | lipase000028 |
| Protein Name |
Pancreatic triacylglycerol lipase PL PTL Pancreatic lipase EC 3.1.1.3 Fragment |
| Gene Name | PNLIP |
| Organism | Equus caballus (Horse) |
| 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 Perissodactyla (odd-toed ungulates) Equidae (horses) Equus Equus Equus caballus (Horse) |
| Enzyme Sequence | WTLSLLLGAVVGNEVCYERLGCFSDDSPWAGIVERPLKILPWSPEKVNTRFLLYTNENPDNFQEIVADPSTIQSSNFNTGRKTRFIIHGFIDKGEESWLSTMCQNMFKVESVNCICVDWKSGSRTAYSQASQNVRIVGAEVAYLVGVLQSSFDYSPSNVHIIGHSLGSHAAGEAGRRTNGAVGRITGLDPAEPCFQGTPELVRLDPSDAQFVDVIHTDIAPFIPNLGFGMSQTAGHLDFFPNGGKEMPGCQKNVLSQIVDIDGIWQGTRDFAACNHLRSYKYYTDSILNPDGFAGFSCASYSDFTANKCFPCSSEGCPQMGHYADRFPGRTKGVGQLFYLNTGDASNFARWRYRVDVTLSGKKVTGHVLVSLFGNKGNSRQYEIFQGTLKPDNTYSNEFDSDVEVGDLEKVKFIWYNNVINLTLPKVGASKITVERNDGSVFNFCSEETVREDVLLTLTAC |
| Enzyme Length | 461 |
| Uniprot Accession Number | P29183 |
| Absorption | |
| Active Site | ACT_SITE 165; /note=Nucleophile; ACT_SITE 189; /note=Charge relay system; ACT_SITE 276; /note=Charge relay system |
| 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:0000269|PubMed:1587279}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Beta strand (22); Chain (1); Disulfide bond (6); Domain (1); Helix (13); Metal binding (4); Mutagenesis (1); Non-terminal residue (1); Signal peptide (1); Turn (5) |
| Keywords | 3D-structure;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:0000250|UniProtKB:P16233}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL <1..12 |
| Structure 3D | X-ray crystallography (1) |
| Cross Reference PDB | 1HPL; |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 50,921 |
| Kinetics | |
| Metal Binding | METAL 200; /note=Calcium; via carbonyl oxygen; METAL 203; /note=Calcium; via carbonyl oxygen; METAL 205; /note=Calcium; METAL 208; /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 |