IED ID | IndEnz0005001108 |
Enzyme Type ID | lipase001108 |
Protein Name |
Liver carboxylesterase 1 EC 3.1.1.1 Acyl-coenzyme A:cholesterol acyltransferase |
Gene Name | |
Organism | Oryctolagus cuniculus (Rabbit) |
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) Lagomorpha Leporidae (rabbits and hares) Oryctolagus Oryctolagus cuniculus (Rabbit) |
Enzyme Sequence | MWLCALALASLAACTAWGHPSAPPVVDTVHGKVLGKFVSLEGFAQPVAVFLGVPFAKPPLGSLRFAPPQPAESWSHVKNTTSYPPMCSQDAVSGHMLSELFTNRKENIPLKFSEDCLYLNIYTPADLTKRGRLPVMVWIHGGGLMVGGASTYDGLALSAHENVVVVTIQYRLGIWGFFSTGDEHSRGNWGHLDQVAALRWVQDNIANFGGDPGSVTIFGESAGGQSVSILLLSPLTKNLFHRAISESGVALLSSLFRKNTKSLAEKIAIEAGCKTTTSAVMVHCLRQKTEEELMEVTLKMKFMALDLVGDPKENTAFLTTVIDGVLLPKAPAEILAEKKYNMLPYMVGINQQEFGWIIPMQMLGYPLSEGKLDQKTATELLWKSYPIVNVSKELTPVATEKYLGGTDDPVKKKDLFLDMLADLLFGVPSVNVARHHRDAGAPTYMYEYRYRPSFSSDMRPKTVIGDHGDEIFSVLGAPFLKEGATEEEIKLSKMVMKYWANFARNGNPNGEGLPQWPAYDYKEGYLQIGATTQAAQKLKDKEVAFWTELWAKEAARPRETEHIEL |
Enzyme Length | 565 |
Uniprot Accession Number | P12337 |
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; ACT_SITE 467; /note=Charge relay system; /evidence=ECO:0000250 |
Activity Regulation | |
Binding Site | |
Calcium Binding | |
catalytic Activity | 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}; |
DNA Binding | |
EC Number | 3.1.1.1 |
Enzyme Function | FUNCTION: Involved in the detoxification of xenobiotics and in the activation of ester and amide prodrugs. {ECO:0000269|PubMed:9635592}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Active site (3); Beta strand (17); Chain (1); Disulfide bond (2); Glycosylation (2); Helix (20); Motif (1); Sequence conflict (4); Signal peptide (1); Turn (5) |
Keywords | 3D-structure;Direct protein sequencing;Disulfide bond;Endoplasmic reticulum;Glycoprotein;Hydrolase;Reference proteome;Serine esterase;Signal |
Interact With | |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Endoplasmic reticulum lumen. Note=Microsomal membrane, lumen of endoplasmic reticulum. |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | SIGNAL 1..18; /evidence="ECO:0000269|PubMed:3343253, ECO:0000269|PubMed:3667634, ECO:0000269|PubMed:9635592" |
Structure 3D | X-ray crystallography (1) |
Cross Reference PDB | 1K4Y; |
Mapped Pubmed ID | - |
Motif | MOTIF 565; /note=Prevents secretion from ER; /evidence=ECO:0000255 |
Gene Encoded By | |
Mass | 62,292 |
Kinetics | |
Metal Binding | |
Rhea ID | RHEA:21164 |
Cross Reference Brenda | 3.1.1.1; |