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3koo
From Proteopedia
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{{STRUCTURE_3koo| PDB=3koo | SCENE= }} | {{STRUCTURE_3koo| PDB=3koo | SCENE= }} | ||
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===Crystal Structure of soluble epoxide Hydrolase=== | ===Crystal Structure of soluble epoxide Hydrolase=== | ||
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{{ABSTRACT_PUBMED_19969453}} | {{ABSTRACT_PUBMED_19969453}} | ||
| - | == | + | ==Function== |
| - | + | [[http://www.uniprot.org/uniprot/HYES_HUMAN HYES_HUMAN]] Bifunctional 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.<ref>PMID:12574508</ref> <ref>PMID:12574510</ref> | |
==About this Structure== | ==About this Structure== | ||
| - | + | [[3koo]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3KOO OCA]. | |
==Reference== | ==Reference== | ||
| - | <ref group="xtra">PMID: | + | <ref group="xtra">PMID:019969453</ref><references group="xtra"/><references/> |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Soluble epoxide hydrolase]] | [[Category: Soluble epoxide hydrolase]] | ||
[[Category: Farrow, N A.]] | [[Category: Farrow, N A.]] | ||
[[Category: Hydrolase]] | [[Category: Hydrolase]] | ||
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| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Apr 28 10:47:40 2010'' | ||
Revision as of 02:33, 4 April 2013
Contents |
Crystal Structure of soluble epoxide Hydrolase
Template:ABSTRACT PUBMED 19969453
Function
[HYES_HUMAN] Bifunctional 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.[1] [2]
About this Structure
3koo is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
- Eldrup AB, Soleymanzadeh F, Farrow NA, Kukulka A, De Lombaert S. Optimization of piperidyl-ureas as inhibitors of soluble epoxide hydrolase. Bioorg Med Chem Lett. 2010 Jan 15;20(2):571-5. Epub 2009 Nov 22. PMID:19969453 doi:10.1016/j.bmcl.2009.11.091
- ↑ Cronin A, Mowbray S, Durk H, Homburg S, Fleming I, Fisslthaler B, Oesch F, Arand M. The N-terminal domain of mammalian soluble epoxide hydrolase is a phosphatase. Proc Natl Acad Sci U S A. 2003 Feb 18;100(4):1552-7. Epub 2003 Feb 6. PMID:12574508 doi:10.1073/pnas.0437829100
- ↑ Newman JW, Morisseau C, Harris TR, Hammock BD. The soluble epoxide hydrolase encoded by EPXH2 is a bifunctional enzyme with novel lipid phosphate phosphatase activity. Proc Natl Acad Sci U S A. 2003 Feb 18;100(4):1558-63. Epub 2003 Feb 6. PMID:12574510 doi:10.1073/pnas.0437724100
