| IED ID | IndEnz0005000132 |
| Enzyme Type ID | lipase000132 |
| Protein Name |
Lipase 1 EC 3.1.1.3 |
| Gene Name | LIP1 |
| Organism | Candida albicans (Yeast) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Saccharomycotina (true yeasts) Saccharomycetes Saccharomycetales Debaryomycetaceae Candida/Lodderomyces clade Candida Candida albicans (Yeast) |
| Enzyme Sequence | MRGIAVFLAFISLIFASPLTVKSPLVDDFYTAPDGYESAKLGEILKLRKTPSKLSSMFFEIDIKNSWQLLVRSEDSFGNATAIVTTVIEPYNADPSKVLSYQTFEDSANIECSPSYGMQYGAPWSTVATQIDMALMVPMLKQGYYVVSPDYEGPKSTFTVGRQSGKATLDSIRAILKSNKFTGIKSDAKVAMWGYSGGSLASGWAAALQPKYAPELKKNLIGAALGGFVTNITATAEATDGTLFAGLVPNALSGLANEYPEFKEILYQKVSKAATDNLRQGTEHCIGGAILYFAEDQYFTGDDRAFPGGYGLLKEEVVNKTISENNLMQMDKDYLPDIPIFVYHGALDSIVPISNVHVTYKNWCDWGINSFEFSEDLLNGHITETIVGAPAAITWLEARFDGEPVVKGCKKTSRITNFSYPNISDSTSSIFEGILNSVTGSELGPGVTSDNITLDGLTGFLGNFIDLK |
| Enzyme Length | 468 |
| Uniprot Accession Number | O94091 |
| Absorption | |
| Active Site | ACT_SITE 196; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 344; /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 | FUNCTION: Hydrolyzes triglycerides. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Chain (1); Glycosylation (6); Signal peptide (1) |
| Keywords | Glycoprotein;Hydrolase;Lipid degradation;Lipid metabolism;Secreted;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:11131027}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..16; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 50,811 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | RHEA:12044 |
| Cross Reference Brenda |