Sulfatase
From Proteopedia
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Mutations in arylsulfatase result in lysosomal storage disorders. Sulfatases are implicated in pathophysiological conditions in hormone-dependent cancer, developmental abnormalities and bacterial pathogenesis<ref>PMID:12757705</ref>. | Mutations in arylsulfatase result in lysosomal storage disorders. Sulfatases are implicated in pathophysiological conditions in hormone-dependent cancer, developmental abnormalities and bacterial pathogenesis<ref>PMID:12757705</ref>. | ||
| + | *<scene name='72/725358/Cv/2'>Succinate/Fe+2 ion binding site</scene>. | ||
</StructureSection> | </StructureSection> | ||
Revision as of 11:37, 4 June 2017
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3D Structures of sulfatase
Updated on 04-June-2017
References
- ↑ Hanson SR, Best MD, Wong CH. Sulfatases: structure, mechanism, biological activity, inhibition, and synthetic utility. Angew Chem Int Ed Engl. 2004 Nov 5;43(43):5736-63. PMID:15493058 doi:http://dx.doi.org/10.1002/anie.200300632
- ↑ Dierks T, Schmidt B, Borissenko LV, Peng J, Preusser A, Mariappan M, von Figura K. Multiple sulfatase deficiency is caused by mutations in the gene encoding the human C(alpha)-formylglycine generating enzyme. Cell. 2003 May 16;113(4):435-44. PMID:12757705
