| IED ID | IndEnz0005000759 |
| Enzyme Type ID | lipase000759 |
| Protein Name |
Lactone esterase SBLE EC 3.1.1.- Lactonase Lipase-like enzyme SBLE |
| Gene Name | sble lip1 |
| Organism | Starmerella bombicola (Yeast) (Candida bombicola) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Saccharomycotina (true yeasts) Saccharomycetes Saccharomycetales Saccharomycetales incertae sedis Starmerella Starmerella bombicola (Yeast) (Candida bombicola) |
| Enzyme Sequence | MLALFFSLAPLLSQALPLGYTAAPAESFYFWPENISSLQAGEIFRKRELLTLPDIFDFGPNLEKVVQVAYKTRLTDGNDSFSIASIFIPKNPSPELKLYSYQTFEDAVQLDCAPSYALEVGNKSSNYLPVTSNLSAISRELEKGRHCIIPDHEGYISGFFAGRQEGYAGLDGIRAARNYLNGTNETPIGIFGYSGGAQATAWIVDLHDEYAPDLNFVGTVSGGTLVDAWGTFQYIDYPKVYLKGSILIMYTGLFSGYPAQFEVIWPYIEPVIQENMLLLRLAPNDCNQSPILQGYNNSIMAGIHVDLPEFPASKYIFQHESLLANYSVVPVSTPKFPRYMYHGGSDELAKLSLVEQYVDQQWNTGANLTFVVYPGLLHDETAYRGFDAAMDWLDAQLDSGYLPPVNSTHT |
| Enzyme Length | 410 |
| Uniprot Accession Number | S5ZJC7 |
| Absorption | |
| Active Site | ACT_SITE 194; /note=Charge relay system; /evidence=ECO:0000250|UniProtKB:W3VKA4; ACT_SITE 346; /note=Charge relay system; /evidence=ECO:0000250|UniProtKB:W3VKA4; ACT_SITE 378; /note=Charge relay system; /evidence=ECO:0000250|UniProtKB:W3VKA4 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.1.1.- |
| Enzyme Function | FUNCTION: Responsible for the lactonization of acidic sophorolipids (SLs). Catalyzes the intramolecular esterification (ring closure) between the carboxyl group of the hydroxy fatty acid and the hydroxyl group of sophorose C6'' of acidic SLs. Lactonizes acetylated acidic SLs, producing di-acetylated C18:2, C18:1 and C18:0 lactonic SL, and mono-acetylated C18:1 lactonic SL. Does not catalyze the reverse reaction, the hydrolysis of lactonic SL into acidic SL, nor hydrolysis of triglycerides or paranitrophenyl esters. {ECO:0000269|PubMed:27251547}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 20-50 degrees Celsius. {ECO:0000269|PubMed:27251547}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 3.5-6. Stable from pH 3.5 to pH 8. {ECO:0000269|PubMed:27251547}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (1); Glycosylation (9); Mutagenesis (1); Signal peptide (1) |
| Keywords | Glycoprotein;Hydrolase;Lipid biosynthesis;Lipid metabolism;Secreted;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:24418522}. |
| Modified Residue | |
| Post Translational Modification | PTM: Glycosylated. {ECO:0000305|PubMed:27251547}. |
| Signal Peptide | SIGNAL 1..15; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 45,561 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=2.9 mM for acidic sophorolipids {ECO:0000269|PubMed:27251547}; |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |