Structural highlights
Function
SQHC_ALIAD Catalyzes the cyclization of squalene into hopene.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The binding structures of 11 human oxidosqualene cyclase inhibitors designed as cholesterol-lowering agents were determined for the squalene-hopene cyclase from Alicyclobacillus acidocaldarius, which is the only structurally known homologue of the human enzyme. The complexes were produced by cocrystallization, and the structures were elucidated by X-ray diffraction analyses. All inhibitors were bound in the large active center cavity. The detailed binding structures are presented and discussed in the light of the IC50 values of these 11 as well as 17 other inhibitors. They provide a consistent picture for the inhibition of the bacterial enzyme and can be used to adjust and improve homology models of the human enzyme. The detailed active center structures of the two enzymes are too different to show an IC50 correlation.
Binding structures and potencies of oxidosqualene cyclase inhibitors with the homologous squalene-hopene cyclase.,Lenhart A, Reinert DJ, Aebi JD, Dehmlow H, Morand OH, Schulz GE J Med Chem. 2003 May 22;46(11):2083-92. PMID:12747780[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Lenhart A, Reinert DJ, Aebi JD, Dehmlow H, Morand OH, Schulz GE. Binding structures and potencies of oxidosqualene cyclase inhibitors with the homologous squalene-hopene cyclase. J Med Chem. 2003 May 22;46(11):2083-92. PMID:12747780 doi:http://dx.doi.org/10.1021/jm0211218
