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| {{STRUCTURE_1llf| PDB=1llf | SIZE=350| SCENE= |right|CAPTION=Cholesterol esterase dimer complex with bile acid [[1llf]] }}
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| | <StructureSection load='1llf' size='350' side='right' caption='Cholesterol esterase dimer complex with bile acid (PDB entry [[1llf]])' scene=''> |
| == Function == | | == Function == |
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Revision as of 10:59, 7 December 2015
| Function
Cholesterol esterase (ChoE) also named bile-acid activated lipase catalyzes the hydrolytic cleavage of cholesterol, other sterol esters and triglycerides.
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 and has the catalytic triad Ser-His-Glu at the opening and hydrophobic residues lining the bottom cup.[1]
- ↑ 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 07-December-2015
{"openlevels":0}
- Cholesterol esterase
- 1akn – bChoE – bovine
- 2bce – bChoE (mutant)
- 1jmy – hChoE - human
- 1f6w – hChoE catalytic domain (mutant)
- Cholesterol esterase complex with bile acids
- 1cle – CcChoE + cholesteryl linoleate – Candida cylindracea
- 1llf – CcChoE + tricosanoic acid
- 1aql – bChoE + taurocholate
References
