| IED ID | IndEnz0005000002 |
| Enzyme Type ID | lipase000002 |
| Protein Name |
Lipase EC 3.1.1.3 EC 3.1.1.32 Phospholipase A1 Triacylglycerol lipase Cleaved into: Lipase 86 kDa form; Lipase 46 kDa form |
| Gene Name | lip |
| Organism | Staphylococcus hyicus |
| Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Firmicutes Bacilli Bacillales Staphylococcaceae Staphylococcus Staphylococcus hyicus |
| Enzyme Sequence | MKETKHQHTFSIRKSAYGAASVMVASCIFVIGGGVAEANDSTTQTTTPLEVAQTSQQETHTHQTPVTSLHTATPEHVDDSKEATPLPEKAESPKTEVTVQPSSHTQEVPALHKKTQQQPAYKDKTVPESTIASKSVESNKATENEMSPVEHHASNVEKREDRLETNETTPPSVDREFSHKIINNTHVNPKTDGQTNVNVDTKTIDTVSPKDDRIDTAQPKQVDVPKENTTAQNKFTSQASDKKPTVKAAPEAVQNPENPKNKDPFVFVHGFTGFVGEVAAKGENHWGGTKANLRNHLRKAGYETYEASVSALASNHERAVELYYYLKGGRVDYGAAHSEKYGHERYGKTYEGVLKDWKPGHPVHFIGHSMGGQTIRLLEHYLRFGDKAEIAYQQQHGGIISELFKGGQDNMVTSITTIATPHNGTHASDDIGNTPTIRNILYSFAQMSSHLGTIDFGMDHWGFKRKDGESLTDYNKRIAESKIWDSEDTGLYDLTREGAEKINQKTELNPNIYYKTYTGVATHETQLGKHIADLGMEFTKILTGNYIGSVDDILWRPNDGLVSEISSQHPSDEKNISVDENSELHKGTWQVMPTMKGWDHSDFIGNDALDTKHSAIELTNFYHSISDYLMRIEKAESTKNA |
| Enzyme Length | 641 |
| Uniprot Accession Number | P04635 |
| Absorption | |
| Active Site | ACT_SITE 369; /note="Nucleophile"; /evidence="ECO:0000269|PubMed:17582438"; ACT_SITE 559; /note="Charge relay system"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10037, ECO:0000269|PubMed:17582438"; ACT_SITE 600; /note="Charge relay system"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10037, ECO:0000269|PubMed:17582438" |
| Activity Regulation | |
| 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:2611229}; CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 2-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:18689, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:57643, ChEBI:CHEBI:57875; EC=3.1.1.32; Evidence={ECO:0000269|PubMed:2611229}; |
| DNA Binding | |
| EC Number | 3.1.1.3; 3.1.1.32 |
| Enzyme Function | FUNCTION: Has a broad substrate specificity hydrolyzing a variety of triglycerides and phosphatidylcholines. {ECO:0000269|PubMed:2611229}. |
| Temperature Dependency | |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH around 9. {ECO:0000269|PubMed:2611229}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Beta strand (14); Chain (2); Compositional bias (7); Helix (21); Metal binding (5); Region (2); Signal peptide (1); Turn (2) |
| Keywords | 3D-structure;Calcium;Direct protein sequencing;Hydrolase;Lipid degradation;Lipid metabolism;Metal-binding;Secreted;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:2611229}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..38; /evidence=ECO:0000269|PubMed:2611229 |
| Structure 3D | X-ray crystallography (1) |
| Cross Reference PDB | 2HIH; |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 71,224 |
| Kinetics | |
| Metal Binding | METAL 535; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000269|PubMed:17582438; METAL 599; /note=Calcium; /evidence=ECO:0000269|PubMed:17582438; METAL 602; /note=Calcium; /evidence=ECO:0000269|PubMed:17582438; METAL 607; /note=Calcium; /evidence=ECO:0000269|PubMed:17582438; METAL 610; /note=Calcium; /evidence=ECO:0000269|PubMed:17582438 |
| Rhea ID | RHEA:12044; RHEA:18689 |
| Cross Reference Brenda |