| IED ID | IndEnz0005000464 |
| Enzyme Type ID | lipase000464 |
| Protein Name |
Carboxylesterase 1D Carboxyesterase ES-10 Carboxylesterase 3 EC 3.1.1.1 EC 3.1.1.67 ES-HVEL Fatty acid ethyl ester synthase FAEE synthase Liver carboxylesterase 10 pI 6.1 esterase |
| Gene Name | Ces1d Ces3 |
| Organism | Rattus norvegicus (Rat) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Glires (Rodents and rabbits) Rodentia Myomorpha (mice and others) Muroidea Muridae Murinae Rattus Rattus norvegicus (Rat) |
| Enzyme Sequence | MRLYPLVWLFLAACTAWGYPSSPPVVNTVKGKVLGKYVNLEGFAQPVAVFLGIPFAKPPLGSLRFAPPQPAEPWNFVKNTTSYPPMCSQDAVGGQVLSELFTNRKENIPLQFSEDCLYLNVYTPADLTKNSRLPVMVWIHGGGLVVGGASTYDGQVLSAHENVVVVTIQYRLGIWGFFSTGDEHSQGNWGHLDQVAALHWVQDNIANFGGNPGSVTIFGESAGGFSVSALVLSPLAKNLFHRAISESGVVLTSALITTDSKPIANLIATLSGCKTTTSAVMVHCLRQKTEDELLETSLKLNLFKLDLLGNPKESYPFLPTVIDGVVLPKTPEEILAEKSFNTVPYIVGINKQEFGWIIPTLMGYPLSEGKLDQKTAKSLLWKSYPTLKISEKMIPVVAEKYFGGTDDPAKRKDLFQDLVADVMFGVPSVMVSRSHRDAGAPTFMYEFEYRPSFVSAMRPKTVIGDHGDELFSVFGSPFLKDGASEEETNLSKMVMKYWANFARNGNPNGGGLPHWPEYDQKEGYLKIGASTQAAQRLKDKEVAFWSELRAKEAAEEPSHWKHVEL |
| Enzyme Length | 565 |
| Uniprot Accession Number | P16303 |
| Absorption | |
| Active Site | ACT_SITE 221; /note=Acyl-ester intermediate; /evidence=ECO:0000255|PROSITE-ProRule:PRU10039; ACT_SITE 353; /note=Charge relay system; /evidence=ECO:0000250|UniProtKB:P23141; ACT_SITE 466; /note=Charge relay system; /evidence=ECO:0000250|UniProtKB:P23141 |
| Activity Regulation | ACTIVITY REGULATION: FAEE-synthesizing and PNPB-hydrolyzing activities are both inhibited by DFP. {ECO:0000269|PubMed:1429692}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=all-trans-retinyl hexadecanoate + H2O = all-trans-retinol + H(+) + hexadecanoate; Xref=Rhea:RHEA:13933, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17336, ChEBI:CHEBI:17616; Evidence={ECO:0000269|PubMed:12230550};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13934; Evidence={ECO:0000305|PubMed:12230550}; CATALYTIC ACTIVITY: Reaction=a carboxylic ester + H2O = a carboxylate + an alcohol + H(+); Xref=Rhea:RHEA:21164, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29067, ChEBI:CHEBI:30879, ChEBI:CHEBI:33308; EC=3.1.1.1; Evidence={ECO:0000255|PROSITE-ProRule:PRU10039, ECO:0000269|PubMed:1429692}; CATALYTIC ACTIVITY: Reaction=a long-chain fatty acyl ethyl ester + H2O = a long-chain fatty acid + ethanol + H(+); Xref=Rhea:RHEA:16641, ChEBI:CHEBI:13209, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16236, ChEBI:CHEBI:57560; EC=3.1.1.67; Evidence={ECO:0000269|PubMed:1429692}; |
| DNA Binding | |
| EC Number | 3.1.1.1; 3.1.1.67 |
| Enzyme Function | FUNCTION: Major lipase in white adipose tissue (By similarity). Involved in the metabolism of xenobiotics and of natural substrates. Hydrolyzes triacylglycerols and monoacylglycerols, with a preference for monoacylglycerols. The susceptibility of the substrate increases with decreasing acyl chain length of the fatty acid moiety. Catalyzes the synthesis of fatty acid ethyl esters (PubMed:1429692). Hydrolyzes retinyl esters (PubMed:12230550). {ECO:0000250|UniProtKB:Q8VCT4, ECO:0000269|PubMed:12230550, ECO:0000269|PubMed:1429692}. |
| Temperature Dependency | |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH for FAEE synthesis is 7.0. Optimum pH for PNPB-hydrolyzing activity is 6-8. {ECO:0000269|PubMed:1429692}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (1); Disulfide bond (2); Glycosylation (2); Modified residue (1); Motif (1); Mutagenesis (5); Sequence conflict (13); Signal peptide (1) |
| Keywords | Cytoplasm;Direct protein sequencing;Disulfide bond;Endoplasmic reticulum;Glycoprotein;Hydrolase;Lipid degradation;Lipid droplet;Lipid metabolism;Microsome;Reference proteome;Serine esterase;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000250|UniProtKB:Q8VCT4}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q8VCT4}. Lipid droplet {ECO:0000250|UniProtKB:Q8VCT4}. Microsome {ECO:0000269|PubMed:12230550}. |
| Modified Residue | MOD_RES 382; /note=N6-succinyllysine; /evidence=ECO:0000250|UniProtKB:Q8VCT4 |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..18; /evidence="ECO:0000269|PubMed:1429692, ECO:0000269|PubMed:8597091" |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | MOTIF 562..565; /note=Prevents secretion from ER; /evidence=ECO:0000255 |
| Gene Encoded By | |
| Mass | 62,147 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.71 M for oleic acid {ECO:0000269|PubMed:1429692}; KM=1.16 uM for retinyl palmitate {ECO:0000269|PubMed:12230550}; Vmax=1482 nmol/h/mg enzyme toward oleic acid {ECO:0000269|PubMed:1429692}; Note=kcat is 0.22 min(-1) with retinyl palmitate as substrate. {ECO:0000269|PubMed:12230550}; |
| Metal Binding | |
| Rhea ID | RHEA:13933; RHEA:13934; RHEA:21164; RHEA:16641 |
| Cross Reference Brenda | 3.1.1.1; |