Cholesterol esterase

Revision as of 13:16, 12 May 2019 by Michal Harel (talk | contribs)

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

3D structures of cholesterol esterase3D structures of cholesterol esterase

Updated on 12-May-2019

ReferencesReferences

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

Michal Harel, Alexander Berchansky