Detail Information for IndEnz0005000333
IED ID IndEnz0005000333
Enzyme Type ID lipase000333
Protein Name Pancreatic triacylglycerol lipase
PL
PTL
Pancreatic lipase
EC 3.1.1.3
Gene Name PNLIP
Organism Oryctolagus cuniculus (Rabbit)
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) Lagomorpha Leporidae (rabbits and hares) Oryctolagus Oryctolagus cuniculus (Rabbit)
Enzyme Sequence MLLLWALPLLLGAVAGLEVCYERLGCFGNRIPWSGGTLERPFSTLPSTPKIVNTRFLLYTNENPNNFQEISADASTIRGSNFRTDRKTRFIIHGFTDKGEENWLSNLCENLFQVETVNCICVDWKGGSRTTYPQATQNIRIVGAEVAYLVGTLQSSLGYSPSNIHVIGHSLGAHAAGEVGRRTNGTIGRITGLDPAEPYFQGTPEIVRLDPSDAQFVDVIHTDAAPMVPNLGFGMSQTVGHLDFFPNGGKEMPGCQKNVLSQIVDINGVWEGTRDFVACNHLRSYKYYADSIVNPNGFAGFSCASYTAFSANKCFPCSNGCPQMGHYADRFSRKTDGVGQTFYLNTGDSSNFARWRYQVAVTLSGRRVTGHVLVSLYGSKGNSKQYEIFTGLLKPGDTHLNEFDSDVDVGDVQKVKFVWYNNVINPTLPKVGASQITVEQNDGRVFKFCSTDTVREDILLTLTPC
Enzyme Length 465
Uniprot Accession Number Q02157
Absorption
Active Site ACT_SITE 170; /note=Nucleophile; /evidence=ECO:0000250; ACT_SITE 194; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU10037; ACT_SITE 281; /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); Metal binding (4); Signal peptide (1)
Keywords Calcium;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..16; /evidence=ECO:0000250
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 51,162
Kinetics
Metal Binding METAL 205; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000250; METAL 208; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000250; METAL 210; /note=Calcium; /evidence=ECO:0000250; METAL 213; /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