3ant
From Proteopedia
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{{STRUCTURE_3ant| PDB=3ant | SCENE= }} | {{STRUCTURE_3ant| PDB=3ant | SCENE= }} | ||
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===Human soluble epoxide hydrolase in complex with a synthetic inhibitor=== | ===Human soluble epoxide hydrolase in complex with a synthetic inhibitor=== | ||
| + | {{ABSTRACT_PUBMED_21192659}} | ||
| - | + | ==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== | ||
| - | [[3ant]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/ | + | [[3ant]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ANT OCA]. |
==Reference== | ==Reference== | ||
| - | <ref group="xtra">PMID:021192659</ref><references group="xtra"/> | + | <ref group="xtra">PMID:021192659</ref><references group="xtra"/><references/> |
| - | [[Category: | + | [[Category: Human]] |
[[Category: Soluble epoxide hydrolase]] | [[Category: Soluble epoxide hydrolase]] | ||
[[Category: Chiyo, N.]] | [[Category: Chiyo, N.]] | ||
Revision as of 05:58, 22 January 2014
Contents |
Human soluble epoxide hydrolase in complex with a synthetic inhibitor
Template:ABSTRACT PUBMED 21192659
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
3ant is a 2 chain structure with sequence from Human. Full crystallographic information is available from OCA.
Reference
- Tanaka D, Tsuda Y, Shiyama T, Nishimura T, Chiyo N, Tominaga Y, Sawada N, Mimoto T, Kusunose N. A Practical Use of Ligand Efficiency Indices Out of the Fragment-Based Approach: Ligand Efficiency-Guided Lead Identification of Soluble Epoxide Hydrolase Inhibitors. J Med Chem. 2010 Dec 30. PMID:21192659 doi:10.1021/jm101273e
- ↑ 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
