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Sulfatase
From Proteopedia
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<StructureSection load='1vz4' size='340' side='right' caption='Alkylsulfatase complex with succinate and Fe+2 ion (PDB code [[1vz4]])' scene=''> | <StructureSection load='1vz4' size='340' side='right' caption='Alkylsulfatase complex with succinate and Fe+2 ion (PDB code [[1vz4]])' scene=''> | ||
| - | + | __TOC__ | |
== Function == | == Function == | ||
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* '''Estrone sulfatase''' hydrolyzes sulfated steroids.<br /> | * '''Estrone sulfatase''' hydrolyzes sulfated steroids.<br /> | ||
* '''N-acetylgalactosamine-6-sulfatase''' hydrolyzes chondroitin sulfate and keratin sulfate. For details see [[Molecular Playground/Human Galactosamine-6-sulfatase]].<br /> | * '''N-acetylgalactosamine-6-sulfatase''' hydrolyzes chondroitin sulfate and keratin sulfate. For details see [[Molecular Playground/Human Galactosamine-6-sulfatase]].<br /> | ||
| + | * '''Choline sulfatase''' hydrolyzes alkyl sulfate choline-O-sulfate<ref>PMID:29458126</ref>.<br /> | ||
| + | * '''Iota-carrageenan sulfatase''' hydrolyzes sulfated polysaccharides<ref>PMID:25207269</ref>.<br /> | ||
== Disease == | == Disease == | ||
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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/ | + | *<scene name='72/725358/Cv/3'>Succinate/Fe+2 ion binding site</scene>. |
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== 3D Structures of sulfatase == | == 3D Structures of sulfatase == | ||
| + | [[Sulfatase 3D structures]] | ||
| - | + | </StructureSection> | |
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| - | **[[4fdi]] – hGalNS <br /> | ||
| - | **[[4fdj]] – hGalNS + GalNac<br /> | ||
| - | }} | ||
== References == | == References == | ||
<references/> | <references/> | ||
[[Category:Topic Page]] | [[Category:Topic Page]] | ||
Current revision
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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
- ↑ van Loo B, Schober M, Valkov E, Heberlein M, Bornberg-Bauer E, Faber K, Hyvonen M, Hollfelder F. Structural and Mechanistic Analysis of the Choline Sulfatase from Sinorhizobium melliloti: A Class I Sulfatase Specific for an Alkyl Sulfate Ester. J Mol Biol. 2018 Feb 16. pii: S0022-2836(18)30081-0. doi:, 10.1016/j.jmb.2018.02.010. PMID:29458126 doi:http://dx.doi.org/10.1016/j.jmb.2018.02.010
- ↑ Genicot SM, Groisillier A, Rogniaux H, Meslet-Cladiere L, Barbeyron T, Helbert W. Discovery of a novel iota carrageenan sulfatase isolated from the marine bacterium Pseudoalteromonas carrageenovora. Front Chem. 2014 Aug 26;2:67. doi: 10.3389/fchem.2014.00067. eCollection 2014. PMID:25207269 doi:http://dx.doi.org/10.3389/fchem.2014.00067
- ↑ 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

