Detail Information for IndEnz0005001108
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;