| IED ID | IndEnz0005000147 |
| Enzyme Type ID | lipase000147 |
| Protein Name |
Lipase 1 EC 3.1.1.3 Arylesterase EC 3.1.1.- |
| Gene Name | SCO1725 SCI11.14c |
| Organism | Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145) |
| Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Actinobacteria Actinomycetia (high G+C Gram-positive bacteria) Streptomycetales Streptomycetaceae Streptomyces Streptomyces albidoflavus group Streptomyces coelicolor Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145) |
| Enzyme Sequence | MRRFRLVGFLSSLVLAAGAALTGAATAQAAQPAAADGYVALGDSYSSGVGAGSYISSSGDCKRSTKAHPYLWAAAHSPSTFDFTACSGARTGDVLSGQLGPLSSGTGLVSISIGGNDAGFADTMTTCVLQSESSCLSRIATAEAYVDSTLPGKLDGVYSAISDKAPNAHVVVIGYPRFYKLGTTCIGLSETKRTAINKASDHLNTVLAQRAAAHGFTFGDVRTTFTGHELCSGSPWLHSVNWLNIGESYHPTAAGQSGGYLPVLNGAA |
| Enzyme Length | 268 |
| Uniprot Accession Number | Q9S2A5 |
| Absorption | |
| Active Site | ACT_SITE 44; /note=Nucleophile; /evidence=ECO:0000250; ACT_SITE 250; /evidence=ECO:0000250 |
| Activity Regulation | ACTIVITY REGULATION: Strongly inhibited by Ag(+). The cations Ca(2+), Mg(2+), Co(2+) and Cu(2+) do not significantly reduce the lipolytic activity of SCO1725. Is also inhibited by DTT in vitro, but not by EDTA or by the reagent masking SH-groups, p-hydroxymercuribenzoate (pHMB). Is resistant to PMSF inhibition, except in the presence of Ca(2+). Is also strongly inhibited by 3,4-dichloroisocoumarin (DCI), another inhibitor of serine hydrolases. Addition of tetrahydrofuran and 1,4-dioxane significantly increases (2- and 4- fold, respectively) hydrolytic activity of lipase towards p-nitrophenyl caprylate. {ECO:0000269|PubMed:19041687, ECO:0000269|Ref.2}. |
| 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:19041687}; |
| DNA Binding | |
| EC Number | 3.1.1.3; 3.1.1.- |
| Enzyme Function | FUNCTION: Catalyzes the hydrolysis of fatty acid esters with a preference for mid-length acyl chain (C10-C16). Is able to hydrolyze the triacylglycerol triolein and mixed triacylglycerols from a wide range of natural oils; better activity is obtained with corn-, wheat germ- and olive oil that have higher content of linoleic and/or oleic acid (C18:2; C18:1, cis). Tween detergents are also substrates for this enzyme. Displays arylesterase activity towards p-nitrophenyl alkanoate esters and alpha- and beta-naphthyl esters. {ECO:0000269|PubMed:19041687, ECO:0000269|Ref.2}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 20-30 degrees Celsius (DOI=10.1016/j.enzmictec.2008.01.009). The His-tagged protein shows a higher optimum temperature of 55 degrees Celsius, and a thermal denaturation midpoint (Tm) of 66.63 degrees Celsius (PubMed:19041687). Is stable when incubated for 30 minutes at temperatures in the range of 30-70 degrees Celsius at pH 7 (DOI=10.1016/j.enzmictec.2008.01.009). {ECO:0000269|PubMed:19041687, ECO:0000269|Ref.2}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.5. Shows high stability over a broad range of pH 4-9.5 (80-100% of enzyme activity). Becomes unstable at pH over 10, where the activity drops to 34% at pH 10.5 and to 8% at pH 11. {ECO:0000269|PubMed:19041687, ECO:0000269|Ref.2}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Chain (1); Disulfide bond (3); Signal peptide (1) |
| Keywords | Disulfide bond;Hydrolase;Lipid degradation;Lipid metabolism;Reference proteome;Secreted;Serine esterase;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:19041687, ECO:0000269|Ref.2}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..29; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 27,394 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | RHEA:12044 |
| Cross Reference Brenda | 3.1.1.3; |