| IED ID | IndEnz0010001075 |
| Enzyme Type ID | esterase001075 |
| Protein Name |
Serum paraoxonase/arylesterase 2 PON 2 EC 3.1.1.2 EC 3.1.1.81 Aromatic esterase 2 A-esterase 2 Serum aryldialkylphosphatase 2 |
| Gene Name | PON2 |
| 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 | MGRLVAVGLLGIALALLGERLLALRNRLKASREVESVDLPHCHLIKGIEAGSEDIDILPNGLAFFSVGLKFPGLHSFAPDKPGGILMMDLKEEKPRARELRISRGFDLASFNPHGISTFIDNDDTVYLFVVNHPEFKNTVEIFKFEEAENSLLHLKTVKHELLPSVNDITAVGPAHFYATNDHYFSDPFLKYLETYLNLHWANVVYYSPNEVKVVAEGFDSANGINISPDDKYIYVADILAHEIHVLEKHTNMNLTQLKVLELDTLVDNLSIDPSSGDIWVGCHPNGQKLFVYDPNNPPSSEVLRIQNILSEKPTVTTVYANNGSVLQGSSVASVYDGKLLIGTLYHRALYCEL |
| Enzyme Length | 354 |
| Uniprot Accession Number | Q15165 |
| Absorption | |
| Active Site | ACT_SITE 114; /note=Proton acceptor; /evidence=ECO:0000250 |
| 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:15772423}; 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:15772423}; |
| DNA Binding | |
| EC Number | 3.1.1.2; 3.1.1.81 |
| Enzyme Function | FUNCTION: Capable of hydrolyzing lactones and a number of aromatic carboxylic acid esters. Has antioxidant activity. Is not associated with high density lipoprotein. Prevents LDL lipid peroxidation, reverses the oxidation of mildly oxidized LDL, and inhibits the ability of MM-LDL to induce monocyte chemotaxis. {ECO:0000269|PubMed:11579088, ECO:0000269|PubMed:15772423}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Alternative sequence (2); Chain (1); Disulfide bond (1); Glycosylation (3); Metal binding (8); Natural variant (3); Sequence conflict (6); Signal peptide (1) |
| Keywords | Alternative splicing;Calcium;Disulfide bond;Glycoprotein;Hydrolase;Membrane;Metal-binding;Reference proteome;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:11579088}; Peripheral membrane protein {ECO:0000269|PubMed:11579088}. |
| Modified Residue | |
| Post Translational Modification | PTM: The signal sequence is not cleaved. {ECO:0000250}. |
| Signal Peptide | SIGNAL 1..?; /note=Not cleaved; /evidence=ECO:0000250 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 11206400; 11257265; 11512679; 11676977; 11692002; 11768721; 11803456; 11918623; 12082592; 12151850; 12433026; 12442067; 12454802; 12561466; 12588779; 12778447; 12939804; 12955589; 14636952; 14741412; 14984433; 14996478; 15001326; 15039125; 15232408; 15256524; 15345661; 15359538; 15544923; 15776585; 16030523; 16078734; 16080611; 16117861; 16135439; 16141008; 16164576; 16185677; 16319130; 16411107; 16551349; 16614106; 16767666; 16776623; 16822964; 16822965; 16891303; 16926679; 17096118; 17137217; 17299970; 17309646; 17404154; 17406108; 17428620; 17436100; 17557249; 17601350; 17664137; 17854416; 17916643; 17940058; 18020951; 18063859; 18258817; 18347034; 18361900; 18413200; 18427977; 18436804; 18513389; 18569577; 18635682; 18691157; 18695162; 18720901; 18759523; 18776646; 18818748; 18977241; 18977341; 19019335; 19082953; 19091699; 19131662; 19151417; 19152805; 19166692; 19254215; 19263529; 19371607; 19401157; 19479237; 19497963; 19527514; 19540141; 19546579; 19575027; 19578796; 19587357; 19654933; 19818126; 19840942; 19865538; 19878569; 19913121; 19930448; 19939821; 19948975; 20099504; 20381198; 20430392; 20458436; 20485444; 20529763; 20530481; 20536507; 20565774; 20582942; 20628086; 20839225; 20934178; 21118365; 21127310; 21146823; 21223581; 21368884; 21561808; 21620813; 21672555; 21757906; 21765051; 21988832; 22016051; 22183305; 22190034; 22534874; 22860094; 22964087; 23053877; 23225229; 23327886; 23487294; 23742759; 24088404; 24100645; 24189400; 24301778; 24421402; 24636586; 24727057; 24807171; 24816800; 24845160; 25038992; 25210784; 25708945; 25740199; 25913154; 25953737; 26056385; 26227792; 26656916; 26978533; 27322774; 27578362; 27609416; 27623343; 27771368; 28108734; 28430636; 28433610; 28509526; 28566152; 28637359; 28768768; 28803777; 28862184; 28954597; 29308836; 29439952; 29531225; 30138371; 30607774; 31338708; 31835890; 32306677; 32382056; 33210737; 33531346; 34710487; 35092416; |
| Motif | |
| Gene Encoded By | |
| Mass | 39,381 |
| Kinetics | |
| Metal Binding | METAL 53; /note=Calcium 1; catalytic; /evidence=ECO:0000250; METAL 54; /note=Calcium 2; /evidence=ECO:0000250; METAL 116; /note=Calcium 2; via carbonyl oxygen; /evidence=ECO:0000250; METAL 167; /note=Calcium 1; catalytic; /evidence=ECO:0000250; METAL 168; /note=Calcium 2; /evidence=ECO:0000250; METAL 223; /note=Calcium 1; catalytic; /evidence=ECO:0000250; METAL 268; /note=Calcium 1; catalytic; /evidence=ECO:0000250; METAL 269; /note=Calcium 1; catalytic; /evidence=ECO:0000250 |
| Rhea ID | RHEA:17309; RHEA:22576 |
| Cross Reference Brenda | 3.1.1.2;3.1.1.25; |