Cholesterol esterase

Function

Cholesterol esterase (ChoE) also named bile-salt activated lipase or sterol esterase catalyzes the hydrolytic cleavage of cholesterol, other sterol esters and triglycerides.^[1]

Disease

Deficiency of this enzyme causes Wolman’s disease and cholesteryl ester storage disease.

Structural highlights

ChoE (Hydrophobic, Polar). ChoE has the at the opening and .^[2]

3D structures of cholesterol esterase

Cholesterol esterase 3D structures

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

Drag the structure with the mouse to rotate

ReferencesReferences

↑ 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

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky

[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

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