Detail Information for IndEnz0010000985
IED ID IndEnz0010000985
Enzyme Type ID esterase000985
Protein Name Gastric triacylglycerol lipase
GL
Gastric lipase
EC 3.1.1.3
Pregastric esterase
PGE
Gene Name LIPF
Organism Bos taurus (Bovine)
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 Artiodactyla Ruminantia Pecora Bovidae Bovinae Bos (oxen cattle) Bos taurus (Bovine)
Enzyme Sequence MWWLLVTVCFIHMSGNAFCFLGKIAKNPEASMNVSQMISYWGYPSEMHKVITADGYILQVYRIPHGKNNANHLGQRPVVFLQHGLLGSATNWISNLPKNSLGFLLADAGYDVWLGNSRGNTWAQEHLYYSPDSPEFWAFSFDEMAEYDLPSTIDFILRRTGQKKLHYVGHSQGTTIGFIAFSTSPTLAEKIKVFYALAPVATVKYTKSLFNKLALIPHFLFKIIFGDKMFYPHTFLEQFLGVEMCSRETLDVLCKNALFAITGVDNKNFNMSRLDVYIAHNPAGTSVQNTLHWRQAVKSGKFQAFDWGAPYQNLMHYHQPTPPIYNLTAMNVPIAVWSADNDLLADPQDVDFLLSKLSNLIYHKEIPNYNHLDFIWAMDAPQEVYNEIVSLMAEDKK
Enzyme Length 397
Uniprot Accession Number Q29458
Absorption
Active Site ACT_SITE 171; /note=Nucleophile; /evidence=ECO:0000250|UniProtKB:P07098; ACT_SITE 342; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU10037; ACT_SITE 371; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU10037
Activity Regulation ACTIVITY REGULATION: Inhibited by diethylp-nitrophenyl phosphate but not inhibited by thiol reagents 5,5'-dithiobis(2-nitrobenzoic acid) or 4,4'-dithiopyridine. {ECO:0000269|PubMed:8615791}.
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:8615791}; CATALYTIC ACTIVITY: Reaction=1,2,3-tri-(9Z-octadecenoyl)-glycerol + H2O = (9Z)-octadecenoate + 1,2-di-(9Z-octadecenoyl)-sn-glycerol + H(+); Xref=Rhea:RHEA:39931, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:52333, ChEBI:CHEBI:53753; Evidence={ECO:0000250|UniProtKB:P07098};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39932; Evidence={ECO:0000250|UniProtKB:P07098}; CATALYTIC ACTIVITY: Reaction=1,2,3-trioctanoylglycerol + H2O = 1,2-dioctanoyl-sn-glycerol + H(+) + octanoate; Xref=Rhea:RHEA:40047, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:25646, ChEBI:CHEBI:76978, ChEBI:CHEBI:76979; Evidence={ECO:0000250|UniProtKB:P07098};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40048; Evidence={ECO:0000250|UniProtKB:P07098};
DNA Binding
EC Number 3.1.1.3
Enzyme Function FUNCTION: Catalyzes the hydrolysis of triacylglycerols to yield free fatty acids, diacylglycerol, monoacylglycerol, and glycerol (PubMed:8615791). Shows a preferential hydrolysis at the sn-3 position of triacylglycerol (By similarity). {ECO:0000250|UniProtKB:P07098, ECO:0000269|PubMed:8615791}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (3); Chain (1); Disulfide bond (1); Domain (1); Glycosylation (3); Signal peptide (1)
Keywords Direct protein sequencing;Disulfide bond;Glycoprotein;Hydrolase;Lipid degradation;Lipid metabolism;Reference proteome;Secreted;Signal
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P80035}.
Modified Residue
Post Translational Modification
Signal Peptide SIGNAL 1..19; /evidence=ECO:0000250|UniProtKB:P07098
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 45,231
Kinetics
Metal Binding
Rhea ID RHEA:12044; RHEA:39931; RHEA:39932; RHEA:40047; RHEA:40048
Cross Reference Brenda