Detail Information for IndEnz0010001328
IED ID IndEnz0010001328
Enzyme Type ID esterase001328
Protein Name Carboxylesterase 3
EC 3.1.1.1
Liver carboxylesterase 31 homolog
Gene Name CES3 UNQ869/PRO1887
Organism Homo sapiens (Human)
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 Primates Haplorrhini Simiiformes Catarrhini Hominoidea (apes) Hominidae (great apes) Homininae Homo Homo sapiens (Human)
Enzyme Sequence MERAVRVESGVLVGVVCLLLACPATATGPEVAQPEVDTTLGRVRGRQVGVKGTDRLVNVFLGIPFAQPPLGPDRFSAPHPAQPWEGVRDASTAPPMCLQDVESMNSSRFVLNGKQQIFSVSEDCLVLNVYSPAEVPAGSGRPVMVWVHGGALITGAATSYDGSALAAYGDVVVVTVQYRLGVLGFFSTGDEHAPGNQGFLDVVAALRWVQENIAPFGGDLNCVTVFGGSAGGSIISGLVLSPVAAGLFHRAITQSGVITTPGIIDSHPWPLAQKIANTLACSSSSPAEMVQCLQQKEGEELVLSKKLKNTIYPLTVDGTVFPKSPKELLKEKPFHSVPFLMGVNNHEFSWLIPRGWGLLDTMEQMSREDMLAISTPVLTSLDVPPEMMPTVIDEYLGSNSDAQAKCQAFQEFMGDVFINVPTVSFSRYLRDSGSPVFFYEFQHRPSSFAKIKPAWVKADHGAEGAFVFGGPFLMDESSRLAFPEATEEEKQLSLTMMAQWTHFARTGDPNSKALPPWPQFNQAEQYLEINPVPRAGQKFREAWMQFWSETLPSKIQQWHQKQKNRKAQEDL
Enzyme Length 571
Uniprot Accession Number Q6UWW8
Absorption
Active Site ACT_SITE 229; /note=Acyl-ester intermediate; /evidence=ECO:0000255|PROSITE-ProRule:PRU10039; ACT_SITE 347; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 460; /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. Shows low catalytic efficiency for hydrolysis of CPT-11 (7-ethyl-10-[4-(1-piperidino)-1-piperidino]-carbonyloxycamptothecin), a prodrug for camptothecin used in cancer therapeutics.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (3); Alternative sequence (1); Chain (1); Disulfide bond (2); Glycosylation (1); Motif (1); Natural variant (8); Sequence conflict (2); Signal peptide (1)
Keywords Alternative splicing;Disulfide bond;Endoplasmic reticulum;Glycoprotein;Hydrolase;Reference proteome;Serine esterase;Signal
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000250}.
Modified Residue
Post Translational Modification PTM: N-glycosylated. {ECO:0000269|PubMed:15100172, ECO:0000269|PubMed:19159218}.
Signal Peptide SIGNAL 1..26; /evidence=ECO:0000255
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID 20422440; 20711500; 22700792;
Motif MOTIF 568..571; /note=Prevents secretion from ER; /evidence=ECO:0000255
Gene Encoded By
Mass 62,282
Kinetics BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=137 uM for 7-ethyl-10-[4-(1-piperidino)-1-piperidino]-carbonyloxycamptothecin {ECO:0000269|PubMed:15100172}; KM=460 uM for 7-ethyl-10-[4-(1-piperidino)-1-amino]-carbonyloxycamptothecin {ECO:0000269|PubMed:15100172};
Metal Binding
Rhea ID RHEA:21164
Cross Reference Brenda