Cholesterol esterase
From Proteopedia
(Difference between revisions)
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== Function == | == Function == | ||
| - | '''Cholesterol esterase''' (ChoE) also named '''bile-acid activated lipase''' catalyzes the hydrolytic cleavage of cholesterol, other sterol esters and triglycerides.<ref>PMID:11563913</ref> | + | '''Cholesterol esterase''' (ChoE) also named '''bile-acid activated lipase''' or '''sterol esterase''' catalyzes the hydrolytic cleavage of cholesterol, other sterol esters and triglycerides.<ref>PMID:11563913</ref> |
== Disease == | == Disease == | ||
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**[[2bce]] – bChoE (mutant)<br /> | **[[2bce]] – bChoE (mutant)<br /> | ||
**[[1jmy]] – hChoE - human<br /> | **[[1jmy]] – hChoE - human<br /> | ||
| - | **[[1f6w]] – hChoE catalytic domain (mutant) | + | **[[1f6w]] – hChoE catalytic domain (mutant) <br /> |
| + | **[[4be9]], [[4be4]] – OpChoE – ''Ophiostoma piceae''<br /> | ||
| + | **[[4upd]] – OpChoE (mutant) <br /> | ||
*Cholesterol esterase complex with bile acids | *Cholesterol esterase complex with bile acids | ||
Revision as of 08:02, 20 December 2018
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3D structures of cholesterol esterase
Updated on 20-December-2018
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
