Detail Information for IndEnz0010001073
IED ID IndEnz0010001073
Enzyme Type ID esterase001073
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 Canis lupus familiaris (Dog) (Canis familiaris)
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 Carnivora Caniformia Canidae (dog coyote wolf fox) Canis Canis lupus (Gray wolf) Canis lupus familiaris (Dog) (Canis familiaris)
Enzyme Sequence MGRLLGVGLLGDRWRSWGERLLALRNRLKASREVESVDLPNCHLIKGIEAGADDIDILPNGLAFFSVGLKCPGLHSFSPDKPGGILMMDLKKENPRALELRISRGFNLASFNPHGISTFIDSDDTVYLFVVNHPEFKNTVEIFKFEEEENSLLHLKTIKHELLPSVNDIIAVGPAHFYATNDHYFSDPFLKYLETYLNLHWANVVYYSPDEVKVVAEGFDAANGINISPDKKYIYVADILAHEIHVLEKHPNMNLTQLKVLKLDTLVDNLSIDPSSGDILVGCHPNGQKLFIYDPNNPPSSEVLRIQNILCEKPTVTTVYANNGSVLQGSSVASVYDRKLLIGTLYHRALYCEL
Enzyme Length 354
Uniprot Accession Number P54832
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; 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;
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. {ECO:0000250}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (1); Chain (1); Disulfide bond (1); Glycosylation (3); Metal binding (8); Signal peptide (1)
Keywords Calcium;Disulfide bond;Glycoprotein;Hydrolase;Membrane;Metal-binding;Reference proteome;Signal
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
Modified Residue
Post Translational Modification PTM: Glycosylated. {ECO:0000250}.; PTM: The signal sequence is not cleaved. {ECO:0000250}.
Signal Peptide SIGNAL 1..?; /note=Not cleaved; /evidence=ECO:0000255
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 39,639
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