| IED ID | IndEnz0010001070 |
| Enzyme Type ID | esterase001070 |
| Protein Name |
Serum paraoxonase/arylesterase 1 PON 1 EC 3.1.1.2 EC 3.1.1.81 EC 3.1.8.1 Aromatic esterase 1 A-esterase 1 Serum aryldialkylphosphatase 1 |
| Gene Name | PON1 PON |
| 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 | MAKLTALTLLGLGLALFDGQKSSFQTRFNVHREVTPVELPNCNLVKGIDNGSEDLEILPNGLAFISAGLKYPGIMSFDPDKPGKILLMDLNEKDPVVLELSITGSTFDLSSFNPHGISTFTDEDNIVYLMVVNHPDSKSTVELFKFQEKEKSLLHLKTIRHKLLPSVNDIVAVGPEHFYATNDHYFIDPYLKSWEMHLGLAWSFVTYYSPNDVRVVAEGFDFANGINISPDGKYVYIAELLAHKIHVYEKHANWTLTPLKSLDFNTLVDNISVDPVTGDLWVGCHPNGMRIFYYDPKNPPASEVLRIQDILSKEPKVTVAYAENGTVLQGSTVAAVYKGKMLVGTVFHKALYCELSQAN |
| Enzyme Length | 359 |
| Uniprot Accession Number | P27170 |
| Absorption | |
| Active Site | ACT_SITE 115; /note=Proton acceptor; /evidence=ECO:0000250|UniProtKB:P27169 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=a phenyl acetate + H2O = a phenol + acetate + H(+); Xref=Rhea:RHEA:17309, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30089, ChEBI:CHEBI:33853, ChEBI:CHEBI:140310; EC=3.1.1.2; Evidence={ECO:0000269|PubMed:1718413}; CATALYTIC ACTIVITY: Reaction=An aryl dialkyl phosphate + H(2)O = dialkyl phosphate + an aryl alcohol.; EC=3.1.8.1; Evidence={ECO:0000269|PubMed:1718413}; CATALYTIC ACTIVITY: Reaction=an N-acyl-L-homoserine lactone + H2O = an N-acyl-L-homoserine + H(+); Xref=Rhea:RHEA:22576, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:55474, ChEBI:CHEBI:58921; EC=3.1.1.81; Evidence={ECO:0000269|PubMed:1718413}; |
| DNA Binding | |
| EC Number | 3.1.1.2; 3.1.1.81; 3.1.8.1 |
| Enzyme Function | FUNCTION: Hydrolyzes the toxic metabolites of a variety of organophosphorus insecticides. Capable of hydrolyzing a broad spectrum of organophosphate substrates and lactones, and a number of aromatic carboxylic acid esters. Mediates an enzymatic protection of low density lipoproteins against oxidative modification. {ECO:0000269|PubMed:11266077}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (1); Disulfide bond (1); Erroneous termination (1); Glycosylation (4); Initiator methionine (1); Metal binding (8); Natural variant (3); Sequence conflict (4); Signal peptide (1) |
| Keywords | Antioxidant;Calcium;Direct protein sequencing;Disulfide bond;Glycoprotein;HDL;Hydrolase;Metal-binding;Reference proteome;Secreted;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted, extracellular space. |
| Modified Residue | |
| Post Translational Modification | PTM: Glycosylated.; PTM: The signal sequence is not cleaved. |
| Signal Peptide | SIGNAL 2..?; /note=Not cleaved |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 40,010 |
| Kinetics | |
| Metal Binding | METAL 53; /note=Calcium 1; catalytic; /evidence=ECO:0000250|UniProtKB:P27169; METAL 54; /note=Calcium 2; /evidence=ECO:0000250|UniProtKB:P27169; METAL 117; /note=Calcium 2; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P27169; METAL 168; /note=Calcium 1; catalytic; /evidence=ECO:0000250|UniProtKB:P27169; METAL 169; /note=Calcium 2; /evidence=ECO:0000250|UniProtKB:P27169; METAL 224; /note=Calcium 1; catalytic; /evidence=ECO:0000250|UniProtKB:P27169; METAL 269; /note=Calcium 1; catalytic; /evidence=ECO:0000250|UniProtKB:P27169; METAL 270; /note=Calcium 1; catalytic; /evidence=ECO:0000250|UniProtKB:P27169 |
| Rhea ID | RHEA:17309; RHEA:22576 |
| Cross Reference Brenda | 3.1.1.2;3.1.8.1; |