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MGP000973

UniProt Annotations

Entry Information
Gene Nameepoxide hydrolase 2, cytoplasmic
Protein EntryHYES_HUMAN
UniProt IDP34913
SpeciesHuman
Comments
Comment typeDescription
Alternative ProductsEvent=Alternative splicing; Named isoforms=3; Name=1; IsoId=P34913-1; Sequence=Displayed; Name=2; IsoId=P34913-2; Sequence=VSP_045598; Note=No experimental confirmation available.; Name=3; IsoId=P34913-3; Sequence=VSP_045597; Note=No experimental confirmation available.;
Biophysicochemical PropertiesKinetic parameters: KM=21 uM for threo-9,10-phosphonooxy-hydroxy-octadecanoic acid {ECO:0000269|PubMed:12574508, ECO:0000269|PubMed:12574510, ECO:0000269|PubMed:15196990}; KM=1.1 mM for p-nitrophenyl phosphate {ECO:0000269|PubMed:12574508, ECO:0000269|PubMed:12574510, ECO:0000269|PubMed:15196990}; Vmax=338 nmol/min/mg enzyme with threo-9,10-phosphonooxy- hydroxy-octadecanoic acid {ECO:0000269|PubMed:12574508, ECO:0000269|PubMed:12574510, ECO:0000269|PubMed:15196990}; Vmax=5.8 nmol/min/mg enzyme with p-nitrophenyl phosphate {ECO:0000269|PubMed:12574508, ECO:0000269|PubMed:12574510, ECO:0000269|PubMed:15196990};
Catalytic Activity(9S,10S)-10-hydroxy-9- (phosphonooxy)octadecanoate + H(2)O = (9S,10S)-9,10- dihydroxyoctadecanoate + phosphate.
Catalytic ActivityAn epoxide + H(2)O = a glycol.
CofactorName=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:12574510};
DomainThe N-terminal domain has phosphatase activity. The C- terminal domain has epoxide hydrolase activity.
FunctionBifunctional enzyme. The C-terminal domain has epoxide hydrolase activity and acts on epoxides (alkene oxides, oxiranes) and arene oxides. Plays a role in xenobiotic metabolism by degrading potentially toxic epoxides. Also determines steady-state levels of physiological mediators. The N-terminal domain has lipid phosphatase activity, with the highest activity towards threo- 9,10-phosphonooxy-hydroxy-octadecanoic acid, followed by erythro- 9,10-phosphonooxy-hydroxy-octadecanoic acid, 12-phosphonooxy- octadec-9Z-enoic acid, 12-phosphonooxy-octadec-9E-enoic acid, and p-nitrophenyl phospate. {ECO:0000269|PubMed:12574508, ECO:0000269|PubMed:12574510}.
InductionBy compounds that cause peroxisome proliferation such as clofibrate, tiadenol and fenofibrate.
PtmThe covalent modification of cysteine by 15-deoxy-Delta12,14- prostaglandin-J2 is autocatalytic and reversible. It may occur as an alternative to other cysteine modifications, such as S- nitrosylation and S-palmitoylation (Probable). {ECO:0000305}.
PtmThe N-terminus is blocked.
SimilarityBelongs to the AB hydrolase superfamily. Epoxide hydrolase family. {ECO:0000305}.
Subcellular LocationCytoplasm. Peroxisome.
SubunitHomodimer. {ECO:0000269|PubMed:15096040, ECO:0000269|PubMed:19969453, ECO:0000269|PubMed:20934334}.
Web ResourceName=NIEHS-SNPs; URL="http://egp.gs.washington.edu/data/ephx2/";
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