IED Industry Enzyme Database

Detail Information for IndEnz0005000500
IED ID IndEnz0005000500
Enzyme Type ID lipase000500
Protein Name Liver carboxylesterase
EC 3.1.1.1
Proline-beta-naphthylamidase
Retinyl ester hydrolase
REH
Gene Name
Organism Sus scrofa (Pig)
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 Laurasiatheria Artiodactyla Suina Suidae (pigs) Sus Sus scrofa (Pig)
Enzyme Sequence MWLLPLVLTSLASSATWAGQPASPPVVDTAQGRVLGKYVSLEGLAQPVAVFLGVPFAKPPLGSLRFAPPQPAEPWSFVKNTTSYPPMCCQDPVVEQMTSDLFTNGKERLTLEFSEDCLYLNIYTPADLTKRGRLPVMVWIHGGGLVLGGAPMYDGVVLAAHENVVVVAIQYRLGIWGFFSTGDEHSRGNWGHLDQVAALHWVQENIANFGGDPGSVTIFGESAGGESVSVLVLSPLAKNLFHRAISESGVALTVALVRKDMKAAAKQIAVLAGCKTTTSAVFVHCLRQKSEDELLDLTLKMKFLTLDFHGDQRESHPFLPTVVDGVLLPKMPEEILAEKDFNTVPYIVGINKQEFGWLLPTMMGFPLSEGKLDQKTATSLLWKSYPIANIPEELTPVATDKYLGGTDDPVKKKDLFLDLMGDVVFGVPSVTVARQHRDAGAPTYMYEFQYRPSFSSDKKPKTVIGDHGDEIFSVFGFPLLKGDAPEEEVSLSKTVMKFWANFARSGNPNGEGLPHWPMYDQEEGYLQIGVNTQAAKRLKGEEVAFWNDLLSKEAAKKPPKIKHAEL
Enzyme Length 566
Uniprot Accession Number Q29550
Absorption
Active Site ACT_SITE 222; /note=Acyl-ester intermediate; /evidence=ECO:0000255|PROSITE-ProRule:PRU10039; ACT_SITE 354; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 467; /note=Charge relay system; /evidence=ECO:0000250
Activity Regulation ACTIVITY REGULATION: Activated by CHAPS at concentrations of up to 130 mM, higher concentrations reduce activity. In the presence of CHAPS, activity is stimulated by non-ionic detergents. Inhibited by the esterase inhibitors diisopropylfluorophosphate and phenylmethylsulfonyl fluoride. {ECO:0000269|PubMed:9490062, ECO:0000269|PubMed:9799112}.
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, ECO:0000269|PubMed:16223870, ECO:0000269|PubMed:9490062, ECO:0000269|PubMed:9799112};
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. Active towards triacylglycerides containing short-chain fatty acids from C2 to C6, and 1(3)-monoacylglycerols containing fatty acids from C2 to C12. Inactive on long-chain triacylglycerols and diacylglycerol. Hydrolyzes aromatic and alkyl esters and vitamin A acetate. The hydrolysis rate depends upon the amino acid promoiety and the esterification site of the prodrug. Aromatic promoieties are favored, highest rates are observed with phenylalanyl progdrugs, hydrolysis of valyl and isoleucyl prodrugs is less efficient. With floxuridine prodrugs, activity is higher on 5' monoesters than on 3' monoesters. With gemcitabine prodrugs, activity is higher on 3' monoesters than on 5' monoesters. {ECO:0000269|PubMed:16223870, ECO:0000269|PubMed:9490062, ECO:0000269|PubMed:9799112}.
Temperature Dependency
PH Dependency BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.0 with tributylglycerol as substrate, and 8.2 with retinyl palmitate as substrate. Active from pH 4.5-9.5 with retinyl palmitate as substrate. {ECO:0000269|PubMed:16223870, ECO:0000269|PubMed:9490062, ECO:0000269|PubMed:9799112};
Pathway
nucleotide Binding
Features Active site (3); Beta strand (19); Chain (1); Disulfide bond (2); Glycosylation (1); Helix (26); Modified residue (1); Motif (1); Sequence conflict (18); Signal peptide (1); Turn (2)
Keywords 3D-structure;Direct protein sequencing;Disulfide bond;Endoplasmic reticulum;Glycoprotein;Hydrolase;Phosphoprotein;Reference proteome;Serine esterase;Signal
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Endoplasmic reticulum lumen.
Modified Residue MOD_RES 379; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P23141
Post Translational Modification
Signal Peptide SIGNAL 1..18; /evidence=ECO:0000250
Structure 3D X-ray crystallography (1)
Cross Reference PDB 5FV4;
Mapped Pubmed ID 31664043;
Motif MOTIF 563..566; /note=Prevents secretion from ER; /evidence=ECO:0000255
Gene Encoded By
Mass 62,016
Kinetics BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=27.5 uM for retinyl palmitate {ECO:0000269|PubMed:16223870, ECO:0000269|PubMed:9490062, ECO:0000269|PubMed:9799112}; KM=0.46 mM for 5'-L-phenylalanyl-floxuridine {ECO:0000269|PubMed:16223870, ECO:0000269|PubMed:9490062, ECO:0000269|PubMed:9799112}; KM=0.44 mM for 5'-D-phenylalanyl-floxuridine {ECO:0000269|PubMed:16223870, ECO:0000269|PubMed:9490062, ECO:0000269|PubMed:9799112}; KM=1.40 mM for 3'-D-phenylalanyl-floxuridine {ECO:0000269|PubMed:16223870, ECO:0000269|PubMed:9490062, ECO:0000269|PubMed:9799112}; KM=0.74 mM for 3'-L-phenylalanyl-floxuridine {ECO:0000269|PubMed:16223870, ECO:0000269|PubMed:9490062, ECO:0000269|PubMed:9799112}; KM=1.87 mM for 5'-L-prolyl-floxuridine {ECO:0000269|PubMed:16223870, ECO:0000269|PubMed:9490062, ECO:0000269|PubMed:9799112}; KM=0.97 mM for 5'-L-leucyl-floxuridine {ECO:0000269|PubMed:16223870, ECO:0000269|PubMed:9490062, ECO:0000269|PubMed:9799112}; KM=4.85 mM for 3'-L-prolyl-floxuridine {ECO:0000269|PubMed:16223870, ECO:0000269|PubMed:9490062, ECO:0000269|PubMed:9799112}; KM=1.46 mM for 3'-L-leucyl-floxuridine {ECO:0000269|PubMed:16223870, ECO:0000269|PubMed:9490062, ECO:0000269|PubMed:9799112}; KM=3.08 mM for 3'-L-lysyl-floxuridine {ECO:0000269|PubMed:16223870, ECO:0000269|PubMed:9490062, ECO:0000269|PubMed:9799112}; KM=6.25 mM for 5'-L-lysyl-floxuridine {ECO:0000269|PubMed:16223870, ECO:0000269|PubMed:9490062, ECO:0000269|PubMed:9799112}; KM=1.11 mM for 3'-L-isoleucyl-floxuridine {ECO:0000269|PubMed:16223870, ECO:0000269|PubMed:9490062, ECO:0000269|PubMed:9799112}; KM=3.00 mM for 5'-L-aspartyl-floxuridine {ECO:0000269|PubMed:16223870, ECO:0000269|PubMed:9490062, ECO:0000269|PubMed:9799112}; KM=0.93 mM for 3'-L-aspartyl-floxuridine {ECO:0000269|PubMed:16223870, ECO:0000269|PubMed:9490062, ECO:0000269|PubMed:9799112}; KM=4.12 mM for 5'-D-valyl-floxuridine {ECO:0000269|PubMed:16223870, ECO:0000269|PubMed:9490062, ECO:0000269|PubMed:9799112}; KM=2.87 mM for 3'-L-valyl-floxuridine {ECO:0000269|PubMed:16223870, ECO:0000269|PubMed:9490062, ECO:0000269|PubMed:9799112}; KM=3.58 mM for 5'-L-valyl-floxuridine {ECO:0000269|PubMed:16223870, ECO:0000269|PubMed:9490062, ECO:0000269|PubMed:9799112}; KM=2.94 mM for 5'-L-isoleucyl-floxuridine {ECO:0000269|PubMed:16223870, ECO:0000269|PubMed:9490062, ECO:0000269|PubMed:9799112}; KM=11.23 mM for 3'-D-valyl-floxuridine {ECO:0000269|PubMed:16223870, ECO:0000269|PubMed:9490062, ECO:0000269|PubMed:9799112}; KM=0.51 mM for 3'-L-phenylalanyl-gemcitabine {ECO:0000269|PubMed:16223870, ECO:0000269|PubMed:9490062, ECO:0000269|PubMed:9799112}; KM=0.97 mM for 3'-D-phenylalanyl-gemcitabine {ECO:0000269|PubMed:16223870, ECO:0000269|PubMed:9490062, ECO:0000269|PubMed:9799112}; KM=0.17 mM for 5'-L-phenylalanyl-gemcitabine {ECO:0000269|PubMed:16223870, ECO:0000269|PubMed:9490062, ECO:0000269|PubMed:9799112}; KM=0.22 mM for 5'-D-phenylalanyl-gemcitabine {ECO:0000269|PubMed:16223870, ECO:0000269|PubMed:9490062, ECO:0000269|PubMed:9799112}; KM=0.90 mM for 3'-L-valyl-gemcitabine {ECO:0000269|PubMed:16223870, ECO:0000269|PubMed:9490062, ECO:0000269|PubMed:9799112}; KM=0.94 mM for 3'-L-isoleucyl-gemcitabine {ECO:0000269|PubMed:16223870, ECO:0000269|PubMed:9490062, ECO:0000269|PubMed:9799112}; KM=1.43 mM for 3'-D-valyl-gemcitabine {ECO:0000269|PubMed:16223870, ECO:0000269|PubMed:9490062, ECO:0000269|PubMed:9799112}; KM=0.85 mM for 5'-L-isoleucyl-gemcitabine {ECO:0000269|PubMed:16223870, ECO:0000269|PubMed:9490062, ECO:0000269|PubMed:9799112}; KM=1.16 mM for 5'-D-valyl-gemcitabine {ECO:0000269|PubMed:16223870, ECO:0000269|PubMed:9490062, ECO:0000269|PubMed:9799112}; KM=0.96 mM for 5'-L-valyl-gemcitabine {ECO:0000269|PubMed:16223870, ECO:0000269|PubMed:9490062, ECO:0000269|PubMed:9799112}; KM=0.91 mM for 5'-L-phenylalanyl-BDCRB {ECO:0000269|PubMed:16223870, ECO:0000269|PubMed:9490062, ECO:0000269|PubMed:9799112}; KM=0.90 mM for 5'-D-phenylalanyl-BDCRB {ECO:0000269|PubMed:16223870, ECO:0000269|PubMed:9490062, ECO:0000269|PubMed:9799112}; KM=0.14 mM for pNPB {ECO:0000269|PubMed:16223870, ECO:0000269|PubMed:9490062, ECO:0000269|PubMed:9799112}; KM=0.52 mM for pNPA {ECO:0000269|PubMed:16223870, ECO:0000269|PubMed:9490062, ECO:0000269|PubMed:9799112}; KM=1.18 mM for PHEE {ECO:0000269|PubMed:16223870, ECO:0000269|PubMed:9490062, ECO:0000269|PubMed:9799112}; KM=0.08 mM for PHBE {ECO:0000269|PubMed:16223870, ECO:0000269|PubMed:9490062, ECO:0000269|PubMed:9799112}; KM=0.40 mM for AcPHEE {ECO:0000269|PubMed:16223870, ECO:0000269|PubMed:9490062, ECO:0000269|PubMed:9799112}; KM=0.63 mM for 5' cinn-floxuridine {ECO:0000269|PubMed:16223870, ECO:0000269|PubMed:9490062, ECO:0000269|PubMed:9799112}; KM=4.21 mM for CPT-11 {ECO:0000269|PubMed:16223870, ECO:0000269|PubMed:9490062, ECO:0000269|PubMed:9799112}; KM=8.81 mM for VACV {ECO:0000269|PubMed:16223870, ECO:0000269|PubMed:9490062, ECO:0000269|PubMed:9799112}; Vmax=530 nmol/h/mg enzyme with retinyl palmitate as substrate {ECO:0000269|PubMed:16223870, ECO:0000269|PubMed:9490062, ECO:0000269|PubMed:9799112}; Vmax=1.82 nmol/min/ug enzyme with 5'-L-phenylalanyl-floxuridine as substrate {ECO:0000269|PubMed:16223870, ECO:0000269|PubMed:9490062, ECO:0000269|PubMed:9799112}; Vmax=1.63 nmol/min/ug enzyme with 5'-D-phenylalanyl-floxuridine as substrate {ECO:0000269|PubMed:16223870, ECO:0000269|PubMed:9490062, ECO:0000269|PubMed:9799112}; Vmax=4.05 nmol/min/ug enzyme with 3'-D-phenylalanyl-floxuridine as substrate {ECO:0000269|PubMed:16223870, ECO:0000269|PubMed:9490062, ECO:0000269|PubMed:9799112}; Vmax=1.55 nmol/min/ug enzyme with 3'-L-phenylalanyl-floxuridine as substrate {ECO:0000269|PubMed:16223870, ECO:0000269|PubMed:9490062, ECO:0000269|PubMed:9799112}; Vmax=1.97 nmol/min/ug enzyme with 5'-L-prolyl-floxuridine as substrate {ECO:0000269|PubMed:16223870, ECO:0000269|PubMed:9490062, ECO:0000269|PubMed:9799112}; Vmax=0.92 nmol/min/ug enzyme with 5'-L-leucyl-floxuridine as substrate {ECO:0000269|PubMed:16223870, ECO:0000269|PubMed:9490062, ECO:0000269|PubMed:9799112}; Vmax=4.53 nmol/min/ug enzyme with 3'-L-prolyl-floxuridine as substrate {ECO:0000269|PubMed:16223870, ECO:0000269|PubMed:9490062, ECO:0000269|PubMed:9799112}; Vmax=0.70 nmol/min/ug enzyme with 3'-L-leucyl-floxuridine as substrate {ECO:0000269|PubMed:16223870, ECO:0000269|PubMed:9490062, ECO:0000269|PubMed:9799112}; Vmax=0.59 nmol/min/ug enzyme with 3'-L-lysyl-floxuridine as substrate {ECO:0000269|PubMed:16223870, ECO:0000269|PubMed:9490062, ECO:0000269|PubMed:9799112}; Vmax=1.11 nmol/min/ug enzyme with 5'-L-lysyl-floxuridine as substrate {ECO:0000269|PubMed:16223870, ECO:0000269|PubMed:9490062, ECO:0000269|PubMed:9799112}; Vmax=0.16 nmol/min/ug enzyme with 3'-L-isoleucyl-floxuridine as substrate {ECO:0000269|PubMed:16223870, ECO:0000269|PubMed:9490062, ECO:0000269|PubMed:9799112}; Vmax=0.33 nmol/min/ug enzyme with 5'-L-aspartyl-floxuridine as substrate {ECO:0000269|PubMed:16223870, ECO:0000269|PubMed:9490062, ECO:0000269|PubMed:9799112}; Vmax=0.10 nmol/min/ug enzyme with 3'-L-aspartyl-floxuridine as substrate {ECO:0000269|PubMed:16223870, ECO:0000269|PubMed:9490062, ECO:0000269|PubMed:9799112}; Vmax=0.30 nmol/min/ug enzyme with 5'-D-valyl-floxuridine as substrate {ECO:0000269|PubMed:16223870, ECO:0000269|PubMed:9490062, ECO:0000269|PubMed:9799112}; Vmax=0.19 nmol/min/ug enzyme with 3'-L-valyl-floxuridine as substrate {ECO:0000269|PubMed:16223870, ECO:0000269|PubMed:9490062, ECO:0000269|PubMed:9799112}; Vmax=0.21 nmol/min/ug enzyme with 5'-L-valyl-floxuridine as substrate {ECO:0000269|PubMed:16223870, ECO:0000269|PubMed:9490062, ECO:0000269|PubMed:9799112}; Vmax=0.15 nmol/min/ug enzyme with 5'-L-isoleucyl-floxuridine as substrate {ECO:0000269|PubMed:16223870, ECO:0000269|PubMed:9490062, ECO:0000269|PubMed:9799112}; Vmax=0.27 nmol/min/ug enzyme with 3'-D-valyl-floxuridine as substrate {ECO:0000269|PubMed:16223870, ECO:0000269|PubMed:9490062, ECO:0000269|PubMed:9799112}; Vmax=283.52 nmol/min/ug enzyme with 3'-L-phenylalanyl-gemcitabine as substrate {ECO:0000269|PubMed:16223870, ECO:0000269|PubMed:9490062, ECO:0000269|PubMed:9799112}; Vmax=406.92 nmol/min/ug enzyme with 3'-D-phenylalanyl-gemcitabine as substrate {ECO:0000269|PubMed:16223870, ECO:0000269|PubMed:9490062, ECO:0000269|PubMed:9799112}; Vmax=3.25 nmol/min/ug enzyme with 5'-L-phenylalanyl-gemcitabine as substrate {ECO:0000269|PubMed:16223870, ECO:0000269|PubMed:9490062, ECO:0000269|PubMed:9799112}; Vmax=3.19 nmol/min/ug enzyme with 5'-D-phenylalanyl-gemcitabine as substrate {ECO:0000269|PubMed:16223870, ECO:0000269|PubMed:9490062, ECO:0000269|PubMed:9799112}; Vmax=0.35 nmol/min/ug enzyme with 3'-L-valyl-gemcitabine as substrate {ECO:0000269|PubMed:16223870, ECO:0000269|PubMed:9490062, ECO:0000269|PubMed:9799112}; Vmax=0.24 nmol/min/ug enzyme with 3'-L-isoleucyl-gemcitabine as substrate {ECO:0000269|PubMed:16223870, ECO:0000269|PubMed:9490062, ECO:0000269|PubMed:9799112}; Vmax=0.32 nmol/min/ug enzyme with 3'-D-valyl-gemcitabine as substrate {ECO:0000269|PubMed:16223870, ECO:0000269|PubMed:9490062, ECO:0000269|PubMed:9799112}; Vmax=0.09 nmol/min/ug enzyme with 5'-L-isoleucyl-gemcitabine as substrate {ECO:0000269|PubMed:16223870, ECO:0000269|PubMed:9490062, ECO:0000269|PubMed:9799112}; Vmax=0.13 nmol/min/ug enzyme with 5'-D-valyl-gemcitabine as substrate {ECO:0000269|PubMed:16223870, ECO:0000269|PubMed:9490062, ECO:0000269|PubMed:9799112}; Vmax=0.12 nmol/min/ug enzyme with 5'-L-valyl-gemcitabine as substrate {ECO:0000269|PubMed:16223870, ECO:0000269|PubMed:9490062, ECO:0000269|PubMed:9799112}; Vmax=2.33 nmol/min/ug enzyme with 5'-L-phenylalanyl-BDCRB as substrate {ECO:0000269|PubMed:16223870, ECO:0000269|PubMed:9490062, ECO:0000269|PubMed:9799112}; Vmax=1.60 nmol/min/ug enzyme with 5'-D-phenylalanyl-BDCRB as substrate {ECO:0000269|PubMed:16223870, ECO:0000269|PubMed:9490062, ECO:0000269|PubMed:9799112}; Vmax=82.25 nmol/min/ug enzyme with pNPB as substrate {ECO:0000269|PubMed:16223870, ECO:0000269|PubMed:9490062, ECO:0000269|PubMed:9799112}; Vmax=60.45 nmol/min/ug enzyme with pNPA as substrate {ECO:0000269|PubMed:16223870, ECO:0000269|PubMed:9490062, ECO:0000269|PubMed:9799112}; Vmax=11859.78 nmol/min/ug enzyme with PHEE as substrate {ECO:0000269|PubMed:16223870, ECO:0000269|PubMed:9490062, ECO:0000269|PubMed:9799112}; Vmax=7.24 nmol/min/ug enzyme with PHBE as substrate {ECO:0000269|PubMed:16223870, ECO:0000269|PubMed:9490062, ECO:0000269|PubMed:9799112}; Vmax=1.29 nmol/min/ug enzyme with AcPHEE as substrate {ECO:0000269|PubMed:16223870, ECO:0000269|PubMed:9490062, ECO:0000269|PubMed:9799112}; Vmax=4.00 nmol/min/ug enzyme with 5' cinn-floxuridine as substrate {ECO:0000269|PubMed:16223870, ECO:0000269|PubMed:9490062, ECO:0000269|PubMed:9799112}; Vmax=0.03 nmol/min/ug enzyme with CPT-11 as substrate {ECO:0000269|PubMed:16223870, ECO:0000269|PubMed:9490062, ECO:0000269|PubMed:9799112};
Metal Binding
Rhea ID RHEA:21164
Cross Reference Brenda