| IED ID | IndEnz0005001135 |
| Enzyme Type ID | lipase001135 |
| Protein Name |
Lipase B EC 3.1.1.3 CALB |
| Gene Name | |
| Organism | Pseudozyma antarctica (Yeast) (Candida antarctica) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Basidiomycota Ustilaginomycotina Ustilaginomycetes Ustilaginales Ustilaginaceae Moesziomyces Pseudozyma antarctica (Yeast) (Candida antarctica) |
| Enzyme Sequence | MKLLSLTGVAGVLATCVAATPLVKRLPSGSDPAFSQPKSVLDAGLTCQGASPSSVSKPILLVPGTGTTGPQSFDSNWIPLSTQLGYTPCWISPPPFMLNDTQVNTEYMVNAITALYAGSGNNKLPVLTWSQGGLVAQWGLTFFPSIRSKVDRLMAFAPDYKGTVLAGPLDALAVSAPSVWQQTTGSALTTALRNAGGLTQIVPTTNLYSATDEIVQPQVSNSPLDSSYLFNGKNVQAQAVCGPLFVIDHAGSLTSQFSYVVGRSALRSTTGQARSADYGITDCNPLPANDLTPEQKVAAAALLAPAAAAIVAGPKQNCEPDLMPYARPFAVGKRTCSGIVTP |
| Enzyme Length | 342 |
| Uniprot Accession Number | P41365 |
| Absorption | |
| Active Site | ACT_SITE 130; /evidence=ECO:0000269|PubMed:8527460; ACT_SITE 212; /evidence=ECO:0000269|PubMed:8527460; ACT_SITE 249 |
| 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: Hydrolysis of triglycerides. Is very stereospecific both in hydrolysis and in organic synthesis and has a potentially important application in glucolipid synthesis. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Beta strand (12); Chain (1); Disulfide bond (3); Glycosylation (1); Helix (19); Propeptide (1); Signal peptide (1); Turn (5) |
| Keywords | 3D-structure;Cleavage on pair of basic residues;Disulfide bond;Glycoprotein;Hydrolase;Lipid degradation;Lipid metabolism;Signal;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..18; /evidence=ECO:0000255 |
| Structure 3D | X-ray crystallography (25) |
| Cross Reference PDB | 1LBS; 1LBT; 1TCA; 1TCB; 1TCC; 3ICV; 3ICW; 3W9B; 4K5Q; 4K6G; 4K6H; 4K6K; 4ZV7; 5A6V; 5A71; 5GV5; 6ISP; 6ISQ; 6ISR; 6J1P; 6J1Q; 6J1R; 6J1S; 6J1T; 6TP8; |
| Mapped Pubmed ID | 19683009; 24448805; 26447231; 26716135; 31023008; 31324776; 32380114; |
| Motif | |
| Gene Encoded By | |
| Mass | 35,518 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | RHEA:12044 |
| Cross Reference Brenda |