IED Industry Enzyme Database

Detail Information for IndEnz0010001456
IED ID IndEnz0010001456
Enzyme Type ID esterase001456
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
K-45
Serum aryldialkylphosphatase 1
Gene Name PON1 PON
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 MAKLIALTLLGMGLALFRNHQSSYQTRLNALREVQPVELPNCNLVKGIETGSEDLEILPNGLAFISSGLKYPGIKSFNPNSPGKILLMDLNEEDPTVLELGITGSKFDVSSFNPHGISTFTDEDNAMYLLVVNHPDAKSTVELFKFQEEEKSLLHLKTIRHKLLPNLNDIVAVGPEHFYGTNDHYFLDPYLQSWEMYLGLAWSYVVYYSPSEVRVVAEGFDFANGINISPDGKYVYIAELLAHKIHVYEKHANWTLTPLKSLDFNTLVDNISVDPETGDLWVGCHPNGMKIFFYDSENPPASEVLRIQNILTEEPKVTQVYAENGTVLQGSTVASVYKGKLLIGTVFHKALYCEL
Enzyme Length 355
Uniprot Accession Number P27169
Absorption
Active Site ACT_SITE 115; /note=Proton acceptor; /evidence=ECO:0000305
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:15098021, ECO:0000269|PubMed:15772423, ECO:0000269|PubMed:1673382, ECO:0000269|PubMed:1718413, ECO:0000269|PubMed:8393742}; CATALYTIC ACTIVITY: Reaction=An aryl dialkyl phosphate + H(2)O = dialkyl phosphate + an aryl alcohol.; EC=3.1.8.1; Evidence={ECO:0000269|PubMed:15098021, ECO:0000269|PubMed:15772423, ECO:0000269|PubMed:1673382, ECO:0000269|PubMed:1718413, ECO:0000269|PubMed:8393742}; 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:15098021, ECO:0000269|PubMed:15772423};
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 and the consequent series of events leading to atheroma formation. {ECO:0000269|PubMed:10479665, ECO:0000269|PubMed:15772423}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (1); Beta strand (27); Chain (1); Disulfide bond (1); Glycosylation (3); Helix (4); Initiator methionine (1); Metal binding (8); Mutagenesis (4); Natural variant (4); Signal peptide (1); Turn (4)
Keywords 3D-structure;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. {ECO:0000269|PubMed:14760718, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218}.; PTM: The signal sequence is not cleaved.; PTM: Present in two forms, form B contains a disulfide bond, form A does not.
Signal Peptide SIGNAL 2..?; /note=Not cleaved
Structure 3D X-ray crystallography (1)
Cross Reference PDB 1V04;
Mapped Pubmed ID 10952224; 10998471; 11073850; 11096050; 11104219; 11151764; 11231922; 11238489; 11239953; 11257264; 11328206; 11341749; 11375798; 11388660; 11395042; 11409295; 11428219; 11472729; 11476678; 11511975; 11511976; 11512679; 11555845; 11557671; 11596674; 11668222; 11676977; 11692002; 11714857; 11740946; 11768721; 11788650; 11810302; 11851721; 11860890; 11880198; 11888532; 11888590; 11889198; 11918278; 11918623; 11935033; 11940319; 11971942; 11993715; 12009854; 12052142; 12052975; 12074827; 12074828; 12080042; 12082503; 12082592; 12139735; 12151850; 12196500; 12204423; 12204800; 12210872; 12241013; 12355548; 12417809; 12433026; 12442067; 12454802; 12466264; 12474066; 12480737; 12480756; 12531885; 12536571; 12545199; 12563177; 12566597; 12575193; 12588779; 12601623; 12615663; 12618279; 12618290; 12621166; 12625227; 12640090; 12645966; 12679462; 12697270; 12706315; 12740482; 12756158; 12777966; 12790379; 12805074; 12824947; 12849920; 12871320; 12889841; 12928148; 12955589; 12957728; 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32148648; 32326787; 32429655; 32472296; 32519276; 32549522; 32556934; 32567023; 32570269; 32583675; 32599353; 32638685; 32674726; 32702814; 32721231; 32729307; 32827712; 32862511; 32902236; 32905659; 32930135; 32940564; 33033318; 33144547; 33164855; 33218342; 33284416; 33325062; 33425072; 33484495; 33485193; 33567022; 33571670; 33579580; 33587860; 33599870; 33628379; 33629320; 33762698; 33831384; 33886674; 34131170; 34351918; 34356595; 34445971; 34593900; 34626508; 34628386; 34634315; 34637171; 34741558; 34762786; 34764653; 9011577; 9414488; 9443862; 9543091;
Motif
Gene Encoded By
Mass 39,731
Kinetics
Metal Binding METAL 53; /note=Calcium 1; catalytic; METAL 54; /note=Calcium 2; METAL 117; /note=Calcium 2; via carbonyl oxygen; METAL 168; /note=Calcium 1; catalytic; METAL 169; /note=Calcium 2; METAL 224; /note=Calcium 1; catalytic; METAL 269; /note=Calcium 1; catalytic; METAL 270; /note=Calcium 1; catalytic
Rhea ID RHEA:17309; RHEA:22576
Cross Reference Brenda 3.1.1.2;3.1.1.25;3.1.1.81;3.1.8.1;3.1.8.2;