Gene_Locus Report

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Gene_locus Report for: human-EPHX2

Homo sapiens (Human) epoxide hydrolase 2, Bifunctional epoxide hydrolase 2 cytosolic (EPHX2) (EC 3.3.2.3) Lipid-phosphate phosphatase (EC 3.1.3.76)

Comment
The gene EPXH2 encodes for the soluble epoxide hydrolase (sEH), an enzyme involved in the regulation of cardiovascular and renal physiology containing two distinct domains connected via a proline-rich linker. The C-terminal domain contains the EH catalytic activity. The N-terminal domain, has high homology to the haloacid dehalogenase family of phosphatases (not alpha/beta hydrolase and not included in ESTHER 5MWA is a structure of this part of the protein). Only c-term PfamA Abhydrolase_1 286 540 N-term is HAD haloacid dehalogenase


Relationship
Family|Epoxide_hydrolase
Block| X
Position in NCBI Life Tree|Homo sapiens
(Below N is a link to NCBI taxonomic web page and E link to ESTHER at designed phylum.)
> cellular organisms: N E > Eukaryota: N E > Opisthokonta: N E > Metazoa: N E > Eumetazoa: N E > Bilateria: N E > Deuterostomia: N E > Chordata: N E > Craniata: N E > Vertebrata: N E > Gnathostomata: N E > Teleostomi: N E > Euteleostomi: N E > Sarcopterygii: N E > Dipnotetrapodomorpha: N E > Tetrapoda: N E > Amniota: N E > Mammalia: N E > Theria: N E > Eutheria: N E > Boreoeutheria: N E > Euarchontoglires: N E > Primates: N E > Haplorrhini: N E > Simiiformes: N E > Catarrhini: N E > Hominoidea: N E > Hominidae: N E > Homininae: N E > Homo: N E > Homo sapiens: N E


Molecular evidence
Database
1 mutation: human-EPHX2
109 structures (e.g. : 1S8O, 1VJ5, 1ZD2... more)
No kinetic


Risk factor: Hypercholesterolemia, familial due to LDLR defect, modifier of -


8 substrates (e.g. : 11,12-EET, 12(13)-EpOME, 14,15-EET... more)
95 inhibitors (e.g. : 1,3-Dicyclohexylurea, 15d-PGJ2, 24D... more)
Sequence
Graphical view for this peptide sequence: human-EPHX2
Colored MSA for Epoxide_hydrolase (raw)
HGYVTVKPRVRLHFVELGSGPAVCLCHGFPESWYSWRYQIPALAQAGYRV
LAMDMKGYGESSAPPEIEEYCMEVLCKEMVTFLDKLGLSQAVFIGHDWGG
MLVWYMALFYPERVRAVASLNTPFIPANPNMSPLESIKANPVFDYQLYFQ
EPGVAEAELEQNLSRTFKSLFRASDESVLSMHKVCEAGGLFVNSPEEPSL
SRMVTEEEIQFYVQQFKKSGFRGPLNWYRNMERNWKWACKSLGRKILIPA
LMVTAEKDFVLVPQMSQHMEDWIPHLKRGHIEDCGHWTQMDKPTEVNQIL
IKWLDSDARNPPVVSKM
Legend This sequence has been compared to family alignement (MSA)
red => minority aminoacid
blue => majority aminoacid
color intensity => conservation rate
title => sequence position(MSA position)aminoacid rate
Catalytic site
Catalytic site in the MSA

HGYVTVKPRVRLHFVELGSGPAVCLCHGFPESWYSWRYQIPALAQAGYRV
LAMDMKGYGESSAPPEIEEYCMEVLCKEMVTFLDKLGLSQAVFIGHDWGG
MLVWYMALFYPERVRAVASLNTPFIPANPNMSPLESIKANPVFDYQLYFQ
EPGVAEAELEQNLSRTFKSLFRASDESVLSMHKVCEAGGLFVNSPEEPSL
SRMVTEEEIQFYVQQFKKSGFRGPLNWYRNMERNWKWACKSLGRKILIPA
LMVTAEKDFVLVPQMSQHMEDWIPHLKRGHIEDCGHWTQMDKPTEVNQIL
IKWLDSDARNPPVVSKM


References
49 more
    Title: Kurarinone alleviated Parkinson's disease via stabilization of epoxyeicosatrienoic acids in animal model
    Sun CP, Zhou JJ, Yu ZL, Huo XK, Zhang J, Morisseau C, Hammock BD, Ma XC
    Ref: Proc Natl Acad Sci U S A, 119:, 2022 : PubMed

            

    Title: Structure-Based Design of Dual Partial Peroxisome Proliferator-Activated Receptor gamma Agonists/Soluble Epoxide Hydrolase Inhibitors
    Lillich FF, Willems S, Ni X, Kilu W, Borkowsky C, Brodsky M, Kramer JS, Brunst S, Hernandez-Olmos V and Proschak E <16 more author(s)>
    Ref: Journal of Medicinal Chemistry, :, 2021 : PubMed

            

    Title: Design, Synthesis, and Structure-Activity Relationship Studies of Dual Inhibitors of Soluble Epoxide Hydrolase and 5-Lipoxygenase
    Hiesinger K, Kramer JS, Beyer S, Eckes T, Brunst S, Flauaus C, Wittmann SK, Weizel L, Kaiser A and Proschak E <12 more author(s)>
    Ref: Journal of Medicinal Chemistry, 63:11498, 2020 : PubMed

            


Other Papers


Send your questions or comments to :
Mail to: Nicolas Lenfant, Thierry Hotelier, Yves Bourne, Pascale Marchot and Arnaud Chatonnet.
Please cite: Lenfant 2013 Nucleic.Acids.Res. or Marchot Chatonnet 2012 Prot.Pept Lett.
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