Detail Information for IndEnz0005000903
IED ID IndEnz0005000903
Enzyme Type ID lipase000903
Protein Name Pancreatic triacylglycerol lipase
PL
PTL
Pancreatic lipase
EC 3.1.1.3
Heart pancreatic lipase
PL-h
Gene Name PNLIP PTL
Organism Ictidomys tridecemlineatus (Thirteen-lined ground squirrel) (Spermophilus tridecemlineatus)
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 Sciuromorpha (squirrels) Sciuridae Xerinae Marmotini Ictidomys (lined ground squirrels) Ictidomys tridecemlineatus (Thirteen-lined ground squirrel) (Spermophilus tridecemlineatus)
Enzyme Sequence MLLVWSLALLLGAVAGKEVCYDRLGCFSDDSPWSGIVERPLKVLPWSPADVNTRFLLYTNENQDNYQQITADSSRIQSSNFKTNRKTRFIIHGFIDKGEESWLANMCKKMFQVESVNCICVDWKGGSRTGYTQASQNIRIVGAEVAYFVDFLRTQLGYSPSNVHVIGHSLGSHAAGEAGRRTNGAIGRITGLDPAEPCFEGTPELVRLDPSDAQFVDAIHTDGAPIVPNLGFGMSQTVGHLDFFPNGGIEMPGCQKNILSQIVDIDGIWEGTRDFAACNHLRSYKYYTDSIVNPTGFAAFSCASYSVFSANKCFPCPSGGCPQMGHYADRYSGKTNGVGQKFYLNTGDKSNFSRWRYKVSVTLSGQKVTGHILVSLFGNAGNSKQYEIYKGSLHPGYTHSNEFDSDVDVGDLQRVKFIWYNNVINPSLPRVGASSISVERNDGRVFKFCSAETVREDVLLTLNAC
Enzyme Length 465
Uniprot Accession Number O88354
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: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 (By similarity). Plays a role in hibernation as a key enzyme that shows high activity at low temperatures. When expressed in the hibernating heart it liberates fatty acids from triglycerides at temperatures as low as 0 degrees Celsius. {ECO:0000250|UniProtKB:P16233, ECO:0000269|PubMed:9653197}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (3); Chain (1); Disulfide bond (6); Domain (1); Metal binding (4); Sequence conflict (1); Signal peptide (1)
Keywords Calcium;Disulfide bond;Hibernation;Hydrolase;Lipid degradation;Lipid metabolism;Metal-binding;Reference proteome;Secreted;Signal
Interact With
Induction INDUCTION: Up-regulated during hibernation. {ECO:0000269|PubMed:9653197}.
Subcellular Location SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P16233}.
Modified Residue
Post Translational Modification
Signal Peptide SIGNAL 1..16; /evidence=ECO:0000250
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 51,227
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:40475; RHEA:40476; RHEA:38575; RHEA:38576; RHEA:13933; RHEA:13934; RHEA:38455; RHEA:38456
Cross Reference Brenda