| IED ID | IndEnz0005000178 |
| Enzyme Type ID | lipase000178 |
| Protein Name |
Lipase A CalA EC 3.1.1.3 |
| Gene Name | PaG_04054 |
| Organism | Pseudozyma aphidis (strain ATCC 32657 / CBS 517.83 / DSM 70725 / JCM 10318 / NBRC 10182 / NRRL Y-7954 / St-0401) (Yeast) (Sterigmatomyces aphidis) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Basidiomycota Ustilaginomycotina Ustilaginomycetes Ustilaginales Ustilaginaceae Moesziomyces Moesziomyces aphidis Pseudozyma aphidis (strain ATCC 32657 / CBS 517.83 / DSM 70725 / JCM 10318 / NBRC 10182 / NRRL Y-7954 / St-0401) (Yeast) (Sterigmatomyces aphidis) |
| Enzyme Sequence | MRVSLRSITSLLAAATAAVLAAPATETLDRRAALPNPYDDPFYTTPSNIGTFAKGQVIQSRKVPTDIGNANNAASFQLQYRTTNTQNEAVADVATVWIPAKPASPPKIFSYQVYEDATALDCAPSYSYLTGLDQPNKVTAVLDTPIIIGWALQQGYYVVSSDHEGFKAAFIAGYEEGMAILDGIRALKNYQNLPSDSKVALEGYSGGAHATVWATSLADSYAPELNIVGASHGGTPVSAKDTFTFLNGGPFAGFALAGVSGLSLAHPDMESFIEARLNAKGQQTLKQIRGRGFCLPQVVLTYPFLNVFSLVNDTNLLNEAPIAGILKQETVVQAEASYTVSVPKFPRFIWHAIPDEIVPYQPAATYVKEQCAKGANINFSPYPIAEHLTAEIFGLVPSLWFIKQAFDGTTPKVICGTPIPAIAGITTPSADQVLGSDLANQLRSLNGKQSAFGKPFGPITPP |
| Enzyme Length | 462 |
| Uniprot Accession Number | W3VKA4 |
| Absorption | |
| Active Site | ACT_SITE 205; /note="Charge relay system"; /evidence="ECO:0000305|PubMed:17631665, ECO:0000305|PubMed:18155238"; ACT_SITE 355; /note="Charge relay system"; /evidence="ECO:0000305|PubMed:17631665, ECO:0000305|PubMed:18155238"; ACT_SITE 387; /note="Charge relay system"; /evidence="ECO:0000305|PubMed:17631665, ECO:0000305|PubMed:18155238" |
| 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:16575565, ECO:0000269|PubMed:17631665}; |
| DNA Binding | |
| EC Number | 3.1.1.3 |
| Enzyme Function | FUNCTION: Hydrolyzes triglycerides, with a preference for substrates with short-chain lengths (C4 to C8). Has the highest activity with tributyrin (C4), followed by tricaproin (C6) and tricaprylin (C8). Can also hydrolyze vinylacetate (C2) and triolein (C18), but with lower efficiency. Has no activity with tripalmitin (C16). {ECO:0000269|PubMed:16575565}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 40-70 degrees Celsius. {ECO:0000269|PubMed:16575565}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is between 7-9. {ECO:0000269|PubMed:16575565}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Beta strand (11); Chain (1); Disulfide bond (2); Erroneous initiation (1); Helix (23); Mutagenesis (7); Signal peptide (1); Turn (3) |
| Keywords | 3D-structure;Disulfide bond;Hydrolase;Lipid degradation;Lipid metabolism;Secreted;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:16575565}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..21; /evidence=ECO:0000255 |
| Structure 3D | X-ray crystallography (2) |
| Cross Reference PDB | 2VEO; 3GUU; |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 49,265 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=4483 uM for tributyrin {ECO:0000269|PubMed:16575565}; |
| Metal Binding | |
| Rhea ID | RHEA:12044 |
| Cross Reference Brenda |