Cholesterol esterase

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== Function ==
== Function ==
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'''Cholesterol esterase''' (ChoE) also named bile-acid activated lipase catalyzes the hydrolytic cleavage of cholesterol, other sterol esters and triglycerides.<ref>PMID:11563913</ref>
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'''Cholesterol esterase''' (ChoE) also named '''bile-salt activated lipase''' or '''sterol esterase''' catalyzes the hydrolytic cleavage of cholesterol, other sterol esters and triglycerides.<ref>PMID:11563913</ref>
== Disease ==
== Disease ==
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== Structural highlights ==
== Structural highlights ==
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ChoE ligand-binding tunnel is ca. 30 A long and has the catalytic triad Ser-His-Glu at the opening and hydrophobic residues lining the bottom cup.<ref>PMID:12499539</ref>
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ChoE <scene name='52/525136/Cv/9'>ligand-binding tunnel is ca. 30 A long</scene> ({{Template:ColorKey_Hydrophobic}}, {{Template:ColorKey_Polar}}). ChoE has the <scene name='52/525136/Cv/10'>polar catalytic triad Ser-His-Glu</scene> at the opening and <scene name='52/525136/Cv/11'>hydrophobic residues lining the bottom cup</scene>.<ref>PMID:12499539</ref>
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</StructureSection>
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==3D structures of cholesterol esterase==
==3D structures of cholesterol esterase==
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[[Cholesterol esterase 3D structures]]
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Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
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</StructureSection>
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{{#tree:id=OrganizedByTopic|openlevels=0|
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*Cholesterol esterase
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**[[1akn]] – bChoE – bovine<br />
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**[[2bce]] – bChoE (mutant)<br />
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**[[1jmy]] – hChoE - human<br />
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**[[1f6w]] – hChoE catalytic domain (mutant)
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*Cholesterol esterase complex with bile acids
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**[[1cle]] – CcChoE + cholesteryl linoleate – ''Candida cylindracea''<br />
 
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**[[1llf]] – CcChoE + tricosanoic acid<br />
 
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**[[1aql]] – bChoE + taurocholate
 
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}}
 
== References ==
== References ==
<references/>
<references/>
[[Category:Topic Page]]
[[Category:Topic Page]]

Current revision

Glycosylated cholesterol esterase dimer complex with bile acid (PDB entry 1llf)

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References

  1. ↑ Moore SA, Kingston RL, Loomes KM, Hernell O, Blackberg L, Baker HM, Baker EN. The structure of truncated recombinant human bile salt-stimulated lipase reveals bile salt-independent conformational flexibility at the active-site loop and provides insights into heparin binding. J Mol Biol. 2001 Sep 21;312(3):511-23. PMID:11563913 doi:10.1006/jmbi.2001.4979
  2. ↑ Pletnev V, Addlagatta A, Wawrzak Z, Duax W. Three-dimensional structure of homodimeric cholesterol esterase-ligand complex at 1.4 A resolution. Acta Crystallogr D Biol Crystallogr. 2003 Jan;59(Pt 1):50-6. Epub 2002 Dec, 19. PMID:12499539

Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky

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