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0HYEP_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NameEPHX1
DescriptionEpoxide hydrolase 1 (ec 3.3.2.3) (microsomal epoxide hydrolase) (epoxide hydratase).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0004301 epoxide hydrolase activity (TAS)
Domain Architecture (Details)
InterPro domains unassigned to SynO:
This entry represents the N-terminal region of the eukaryotic epoxide hydrolase protein. Epoxide hydrolases () comprise a group of functionally related enzymes that catalyse the addition of water to oxirane compounds (epoxides).hereby usually generating vicinal trans-diols. EHs have been found in all types of living organisms.ncluding mammals.nvertebrates.lants.ungi and bacteria. In animals.he major interest in EH is directed towards their detoxification capacity for epoxides since they are important safeguards against the cytotoxic and genotoxic potential of oxirane derivatives that are often reactive electrophiles because of the high tension of the three-membered ring system and the strong polarisation of the C--O bonds. This is of significant relevance because epoxides are frequent intermediary metabolites.hich arise during the biotransformation of foreign compounds . This domain is often found in conjunction with .
  IPR010497:Epoxide hydrolase, N-terminal
The alpha/beta hydrolase fold is common to a number of hydrolytic enzymesof widely differing phylogenetic origin and catalytic function. The coreof each enzyme is an alpha/beta-sheet (rather than a barrel).ontaining 8strands connected by helices . The enzymes are believed to have divergedfrom a common ancestor.reserving the arrangement of the catalyticresidues. All have a catalytic triad.he elements of which are borne onloops.hich are the best conserved structural features of the fold.
  IPR000073:Alpha/beta hydrolase fold-1
The alpha/beta hydrolase fold is common to a number of hydrolytic enzymes of widely differing phylogeneticorigin and catalytic function. The core of each enzyme is an alpha/beta-sheet (rather than a barrel).ontaining8 strands connected by helices . The enzymes are believed to have diverged from a common ancestor.reserving the arrangement of the catalytic residues. All have a catalytic triad.he elements of which are borneon loops.hich are the best conserved structural features of the fold. The epoxide hydrolases (EH) add water toepoxides.orming the corresponding diol. On the basis of sequence similarity.t has been proposed that themammalian soluble EHs contain 2 evolutionarily distinct domains.he N-terminal domain is similar to bacterialhaloacid dehalogenase.hile the C-terminal domain is similar to soluble plant EH.icrosomal EH.nd bacterialhaloalkane dehalogenase (HLD) . The mechanism of HLD.stablished by X-ray crystallographic analysisof an HDL-substrate intermediate .nvolves nucleophilic attack of Asp-124 on the halogen-substitutedterminal carbon of the substrate.orming a covalently-bound ester intermediate. The Asp-260/His-289 pairactivate a water molecule that hydrolyses the ester intermediate to release the product. The similarity of EH toHLD is important for deducing a catalytic mechanism for EH. Mutagenesis experiments on murine soluble EHconfirmed the crucial role of nucleophile Asp-333 and His-523 in the catalytic mechanism and the importance ofconserved His-263 and His-332 .
  IPR000639:Epoxide hydrolase
IPR010497:EHN 
Evalue:-64.0362091064453 
Location:48-161IPR000073:Abhydrolase_1 
Evalue:-30.5850257873535 
Location:178-396IPR000639:EPOXHYDRLASE 
Evalue:0 
Location:426-448
SequencesProtein: HYEP_HUMAN (455 aa)
mRNA: NM_000120
Local Annotation
Synapse Ontology
Typical ecretory organelles, some 50 nm in diameter, of presynaptic nerve terminals; accumulate high concentrations of nonpeptide neurotransmitters and secrete these into the synaptic cleft by fusion with the 'active zone' of the presynaptic plasma membrane.
sdb:0094 typical synaptic vesicle  (Evidence:keywords)
KO assignmentK01253
  Level 3 annotation:
    epoxide hydrolase
  Level 2 annotation:
    Tetrachloroethene degradation
    Metabolism of xenobiotics by cytochrome P450
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 91 residues, 224079598-224079868Exon2: 64 residues, 224083048-224083236Exon3: 62 residues, 224086102-224086283Exon4: 78 residues, 224092977-224093205Exon5: 45 residues, 224093540-224093670Exon6: 71 residues, 224094152-224094361Exon7: 38 residues, 224096689-224096798Exon8: 44 residues, 224098821-224098947Exon9: 140 residues, 224099469-224099883Exon10: 2 residues, -Jump to HYEP_HUMAN  
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Loci Cluster (Details)Loci: 3865 224399004-224441046 ~-42K 4033(ACBD3)(-)Loci: 2594 224079598-224099883 ~-20K 4021(EPHX1)(+)Link out to UCSC