| IED ID | IndEnz0010001372 |
| Enzyme Type ID | esterase001372 |
| Protein Name |
Lipase 8 EC 3.1.1.3 |
| Gene Name | LIP8 CAALFM_C703300CA CaO19.8925 |
| Organism | Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Saccharomycotina (true yeasts) Saccharomycetes Saccharomycetales Debaryomycetaceae Candida/Lodderomyces clade Candida Candida albicans (Yeast) Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast) |
| Enzyme Sequence | MLFLLFLLITPIYAGLIFLTKPSNDPFYNPPKGFEKAAVGDILQSRETPKSITGRFAPLEIQNSWQLLVRSEDSFGNPNAIVTTVIQPFNADPSKVASYQVFEDSAKGDCAPSYALQFGSDLSTLATQAETFLLAPLLEQGYYVVSPDYEGPKSTFTIGKQSGQAVLNSIRAALKSGKITNIKDDAKVVMWGYSGGSLASGWAAALQPSYAPELGGNLLGAALGGFVTNITATAQAADGTVFAGIVANALGGVANEYPEFKSILQSDTDKKSVFDEFDSHCLADGVIDYINTSFLTGDNKIFKTGWDILKSSTIAKIVKDNGLVYQKQLVPKIPIFVYHGSIDQIVPIVNVKKTYQNWCEGGISSLEFAEDGTNGHLTETVVGAPAALTWIIDRFNGKQTVSGCQHDKRLSNFQYPNISSSILKYFKVALDTMMSNGLGSDIQKDKITPDDLRKFLLGGW |
| Enzyme Length | 460 |
| Uniprot Accession Number | Q9P8V9 |
| Absorption | |
| Active Site | ACT_SITE 194; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 339; /note=Charge relay system; /evidence=ECO:0000250 |
| 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; |
| DNA Binding | |
| EC Number | 3.1.1.3 |
| Enzyme Function | |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Chain (1); Glycosylation (3); Sequence conflict (17); Signal peptide (1) |
| Keywords | Glycoprotein;Hydrolase;Lipid degradation;Lipid metabolism;Reference proteome;Secreted;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:11131027}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..14; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 49,731 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | RHEA:12044 |
| Cross Reference Brenda |