3otq
From Proteopedia
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{{STRUCTURE_3otq| PDB=3otq | SCENE= }} | {{STRUCTURE_3otq| PDB=3otq | SCENE= }} | ||
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===Soluble Epoxide Hydrolase in complex with pyrazole antagonist=== | ===Soluble Epoxide Hydrolase in complex with pyrazole antagonist=== | ||
| + | {{ABSTRACT_PUBMED_20934334}} | ||
| - | + | ==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> | |
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==About this Structure== | ==About this Structure== | ||
| - | + | [[3otq]] 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=3OTQ OCA]. | |
==Reference== | ==Reference== | ||
| - | <ref group="xtra">PMID: | + | <ref group="xtra">PMID:020934334</ref><references group="xtra"/><references/> |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Soluble epoxide hydrolase]] | [[Category: Soluble epoxide hydrolase]] | ||
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[[Category: Epoxide hydrolase]] | [[Category: Epoxide hydrolase]] | ||
[[Category: Hydrolase]] | [[Category: Hydrolase]] | ||
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| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Nov 3 11:23:01 2010'' | ||
Revision as of 08:37, 2 May 2013
Contents |
Soluble Epoxide Hydrolase in complex with pyrazole antagonist
Template:ABSTRACT PUBMED 20934334
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
3otq is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
- Lo HY, Man CC, Fleck RW, Farrow NA, Ingraham RH, Kukulka A, Proudfoot JR, Betageri R, Kirrane T, Patel U, Sharma R, Hoermann MA, Kabcenell A, Lombaert SD. Substituted pyrazoles as novel sEH antagonist: investigation of key binding interactions within the catalytic domain. Bioorg Med Chem Lett. 2010 Nov 15;20(22):6379-83. Epub 2010 Sep 19. PMID:20934334 doi:10.1016/j.bmcl.2010.09.095
- ↑ 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
