| IED ID | IndEnz0005000605 |
| Enzyme Type ID | lipase000605 |
| Protein Name |
Triacylglycerol lipase EC 3.1.1.3 Extracellular lipase Triacylglycerol ester hydrolase |
| Gene Name | lip lipA PA2862 |
| Organism | Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) |
| Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Gammaproteobacteria Pseudomonadales Pseudomonadaceae Pseudomonas Pseudomonas aeruginosa group Pseudomonas aeruginosa Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) |
| Enzyme Sequence | MKKKSLLPLGLAIGLASLAASPLIQASTYTQTKYPIVLAHGMLGFDNILGVDYWFGIPSALRRDGAQVYVTEVSQLDTSEVRGEQLLQQVEEIVALSGQPKVNLIGHSHGGPTIRYVAAVRPDLIASATSVGAPHKGSDTADFLRQIPPGSAGEAVLSGLVNSLGALISFLSSGSTGTQNSLGSLESLNSEGAARFNAKYPQGIPTSACGEGAYKVNGVSYYSWSGSSPLTNFLDPSDAFLGASSLTFKNGTANDGLVGTCSSHLGMVIRDNYRMNHLDEVNQVFGLTSLFETSPVSVYRQHANRLKNASL |
| Enzyme Length | 311 |
| Uniprot Accession Number | P26876 |
| Absorption | |
| Active Site | ACT_SITE 108; /note="Nucleophile"; /evidence="ECO:0000305|PubMed:10893416, ECO:0000305|PubMed:1632642, ECO:0007744|PDB:1EX9"; ACT_SITE 255; /note="Charge relay system"; /evidence="ECO:0000305|PubMed:10893416, ECO:0000305|PubMed:1632642, ECO:0007744|PDB:1EX9"; ACT_SITE 277; /note="Charge relay system"; /evidence="ECO:0000305|PubMed:10893416, ECO:0000305|PubMed:1632642, ECO:0007744|PDB:1EX9" |
| Activity Regulation | ACTIVITY REGULATION: Na(+) increases lipase activity (PubMed:1748875). Inhibited by diethyl p-nitrophenyl phosphate and 3,4-dichloroisocoumarin (DCI) (PubMed:1576157, PubMed:1748875). {ECO:0000269|PubMed:1576157, ECO:0000269|PubMed:1748875}. |
| Binding Site | BINDING 42; /note="Substrate; via amide nitrogen"; /evidence="ECO:0000269|PubMed:10893416, ECO:0007744|PDB:1EX9"; BINDING 109; /note="Substrate; via amide nitrogen"; /evidence="ECO:0000269|PubMed:10893416, ECO:0007744|PDB:1EX9" |
| 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:0000305|PubMed:1748875}; |
| DNA Binding | |
| EC Number | 3.1.1.3 |
| Enzyme Function | FUNCTION: Catalyzes the hydrolysis of triacylglycerol (PubMed:1748875). It also exhibits some esterase activity with p-nitrophenyl acetate and Tween 80 as substrates, however the lipase activity is approximately eight times the esterase activity (PubMed:1748875). It shows a marked specificity for the 1,3-oleyl residues of triolein (PubMed:1748875). {ECO:0000269|PubMed:1748875, ECO:0000305|PubMed:1632642}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 50 degrees Celsius. {ECO:0000269|PubMed:1748875}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.5-9. {ECO:0000269|PubMed:1748875}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Beta strand (12); Binding site (2); Chain (1); Disulfide bond (1); Domain (1); Helix (13); Metal binding (4); Mutagenesis (2); Natural variant (4); Signal peptide (1); Turn (2) |
| 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:0000269|PubMed:1576157}. Note=During early stationary growth phase about 10% of the enzyme molecules remain cell-bound while about 90% are released into the growth medium. {ECO:0000269|PubMed:1576157}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..26; /evidence=ECO:0000269|PubMed:1576157 |
| Structure 3D | X-ray crystallography (1) |
| Cross Reference PDB | 1EX9; |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 32,723 |
| Kinetics | |
| Metal Binding | METAL 235; /note="Calcium"; /evidence="ECO:0000269|PubMed:10893416, ECO:0007744|PDB:1EX9"; METAL 279; /note="Calcium"; /evidence="ECO:0000269|PubMed:10893416, ECO:0007744|PDB:1EX9"; METAL 283; /note="Calcium; via carbonyl oxygen"; /evidence="ECO:0000269|PubMed:10893416, ECO:0007744|PDB:1EX9"; METAL 287; /note="Calcium; via carbonyl oxygen"; /evidence="ECO:0000269|PubMed:10893416, ECO:0007744|PDB:1EX9" |
| Rhea ID | RHEA:12044 |
| Cross Reference Brenda | 3.1.1.3; |