| IED ID | IndEnz0005000264 |
| Enzyme Type ID | lipase000264 |
| Protein Name |
Extracellular lipase EC 3.1.1.3 Triacylglycerol lipase |
| Gene Name | lip |
| Organism | Aeromonas hydrophila |
| Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Gammaproteobacteria Aeromonadales Aeromonadaceae Aeromonas Aeromonas hydrophila |
| Enzyme Sequence | MKKKLIYAAVVSALLAGCGGSDDNKGDTSSYLDYLLTGSNAVGPSALAARAWDGTLKFSTETADLSNPVSAMSTLDGWSTTQAIQIVPVTSSGITVQAPTTAEFGASVAPLYLLEVTFDSTALRPSGVKKVLTYGVDFVVAASAWQAEPGSAQAVEPLPCLANDSGHRTAERQSRRCLKAGSDYGNYKNNAGSNAQEQTINGLIALQEGLFKAATGIATDHVIFSDWFGTQSGADVLVAVKGAAASVLKADPVTLDAAKLWKQDAWEHQPARHLYPGRDRPTCLPDPAGCRAVPAAEQKDAIATAFGPVLRSTRLLKRPRSIPVPSSCLTSSPHRRPQVPGARPRPSPGTVPSQPVRHRQCAEGVTRSDRRAGGGGRGSGPAGDADCRSDPPERAAGRGEQADWGDAHLRRQAAGRRAEHWSLQPAADAGRGAIRADACLRQGCPQHHHGCHHLSARRDLGQRERLRPGAGPDLEDLCRHAGGQEGGAGGDRSSAARRAWLRLSGSMDTVTTSDNPTPYLNLSYLTVARDNLKQSVAICWACVWRLAWPTPRAIGTAGSLKVHFLGHSLGASRVPTCCGRQPDHRQRASGCPVQVRYRWPGHAGSHSAAAAELADFGPTIKMGVLTSGSAELKAGFTAYAPNCTDGGAYLLRQRVPAEPGRGHSATAATRCRVQLCGPVGAGFG |
| Enzyme Length | 684 |
| Uniprot Accession Number | P40600 |
| Absorption | |
| Active Site | ACT_SITE 568; /note=Nucleophile; /evidence=ECO:0000255|PROSITE-ProRule:PRU10037 |
| 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:8368830}; |
| DNA Binding | |
| EC Number | 3.1.1.3 |
| Enzyme Function | FUNCTION: The optimum chain lengths for the acyl moiety is C6 for ester hydrolysis and C6 and C8 for triacylglycerol hydrolysis. {ECO:0000269|PubMed:8368830}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 37 degrees Celsius. Retains 90% of its activity after 30 minutes at 55 degrees Celsius. {ECO:0000269|PubMed:8368830}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.2. {ECO:0000269|PubMed:8368830}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (1); Compositional bias (2); Region (2); Signal peptide (1) |
| Keywords | Hydrolase;Lipid degradation;Lipid metabolism;Secreted;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:8368830}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..48; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 71,904 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | RHEA:12044 |
| Cross Reference Brenda |