| IED ID | IndEnz0010001466 |
| Enzyme Type ID | esterase001466 |
| Protein Name |
Lipase EC 3.1.1.3 Diheptanoyl glycerophosphocholine esterase EC 3.1.1.- Extracellular lipase GDSL-like lipase Palmitoyl-CoA hydrolase EC 3.1.2.2 SRL |
| Gene Name | |
| Organism | Streptomyces rimosus |
| Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Actinobacteria Actinomycetia (high G+C Gram-positive bacteria) Streptomycetales Streptomycetaceae Streptomyces Streptomyces rimosus |
| Enzyme Sequence | MRLSRRAATASALLLTPALALFGASAAVSAPRIQATDYVALGDSYSSGVGAGSYDSSSGSCKRSTKSYPALWAASHTGTRFNFTACSGARTGDVLAKQLTPVNSGTDLVSITIGGNDAGFADTMTTCNLQGESACLARIAKARAYIQQTLPAQLDQVYDAIDSRAPAAQVVVLGYPRFYKLGGSCAVGLSEKSRAAINAAADDINAVTAKRAADHGFAFGDVNTTFAGHELCSGAPWLHSVTLPVENSYHPTANGQSKGYLPVLNSAT |
| Enzyme Length | 268 |
| Uniprot Accession Number | Q93MW7 |
| Absorption | |
| Active Site | ACT_SITE 44; /note=Nucleophile; ACT_SITE 250; /evidence=ECO:0000305 |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by 3,4-dichloroisocoumarin and tetrahydrolipstatin in the absence of substrate, but by phenylmethylsulfonyl fluoride (PMSF) only in the presence of substrate. Several water-miscible solvents enhance the lipase hydrolytic activity in vitro. Tetrahydrofuran and N,N-dimethylformamide (both 50%) inactivate the enzyme with t1/2 of 5 minutes and t1/2 of 2 hours, respectively. {ECO:0000269|Ref.4}. |
| 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:20931591, ECO:0000269|Ref.5}; CATALYTIC ACTIVITY: Reaction=H2O + hexadecanoyl-CoA = CoA + H(+) + hexadecanoate; Xref=Rhea:RHEA:16645, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379; EC=3.1.2.2; Evidence={ECO:0000269|PubMed:20931591}; |
| DNA Binding | |
| EC Number | 3.1.1.3; 3.1.1.-; 3.1.2.2 |
| Enzyme Function | FUNCTION: Catalyzes the hydrolysis of p-nitrophenyl esters, alpha- and beta-naphthyl esters, and triacylglycerols, with a preference for medium acyl chain length (C8-C12). Shows a much higher hydrolysis rate of glycerol esters of unsaturated C16 and C18 fatty acids than that of their saturated counterparts, and a preference for cis double bond. Is also able to hydrolyze several natural oils and Tween detergents. Also displays thioesterase and phospholipase activities, towards palmitoyl-coenzyme A and diheptanoyl glycerophosphocholine, respectively. Shows transesterification activity of racemic 1-phenyl ethanol with vinyl acetate in hexane, proceeding with partial (R)-enantioselectivity. {ECO:0000269|PubMed:20931591, ECO:0000269|Ref.4, ECO:0000269|Ref.5}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 55 degrees Celsius at pH 8.0. {ECO:0000269|Ref.3}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 9.5. {ECO:0000269|Ref.3}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Beta strand (7); Chain (1); Disulfide bond (3); Helix (12); Signal peptide (1); Turn (2) |
| Keywords | 3D-structure;Direct protein sequencing;Disulfide bond;Hydrolase;Lipid degradation;Lipid metabolism;Secreted;Serine esterase;Signal |
| Interact With | |
| Induction | INDUCTION: Expressed once the cells enter stationary phase, with a maximum at the late stationary phase. {ECO:0000269|Ref.5}. |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|Ref.3}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..34; /evidence=ECO:0000269|PubMed:12115057 |
| Structure 3D | X-ray crystallography (1) |
| Cross Reference PDB | 5MAL; |
| Mapped Pubmed ID | 28558229; |
| Motif | |
| Gene Encoded By | |
| Mass | 27,607 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | RHEA:12044; RHEA:16645 |
| Cross Reference Brenda |