| Function
Cholesterol esterase (ChoE) also named bile-acid 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 ligand-binding tunnel is ca. 30 A long (Hydrophobic, Polar). ChoE has the polar catalytic triad Ser-His-Glu at the opening and hydrophobic residues lining the bottom cup.[2]
- ↑ 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
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3D structures of cholesterol esterase
Updated on 12-February-2019
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- Cholesterol esterase
- 1akn – bChoE – bovine
- 2bce – bChoE (mutant)
- 1jmy – hChoE - human
- 1f6w – hChoE catalytic domain (mutant)
- 4be9, 4be4 – OpChoE – Ophiostoma piceae
- 4upd – OpChoE (mutant)
- Cholesterol esterase complex with bile acids
- 1cle – CcChoE + cholesteryl linoleate – Candida cylindracea
- 1llf – CcChoE + tricosanoic acid
- 1aql – bChoE + taurocholate
References
