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Cholesterol esterase
From Proteopedia
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<StructureSection load='1llf' size='350' side='right' caption='Glycosylated cholesterol esterase dimer complex with bile acid (PDB entry [[1llf]])' scene=''> | <StructureSection load='1llf' size='350' side='right' caption='Glycosylated cholesterol esterase dimer complex with bile acid (PDB entry [[1llf]])' scene=''> | ||
== Function == | == Function == | ||
| - | '''Cholesterol esterase''' (ChoE) also named bile-acid activated lipase catalyzes the hydrolytic cleavage of cholesterol, other sterol esters and triglycerides. | + | '''Cholesterol esterase''' (ChoE) also named bile-acid activated lipase catalyzes the hydrolytic cleavage of cholesterol, other sterol esters and triglycerides.<ref>PMID:11563913</ref> |
== Disease == | == Disease == | ||
Revision as of 11:12, 7 December 2015
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3D structures of cholesterol esterase
Updated on 07-December-2015
References
- ↑ 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
- ↑ 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
