A novel amino acid modification in sulfatases that is defective in multiple sulfatase deficiency
Multiple sulfatase deficiency (MSD) is a lysosomal storage disorder characterized by a decreased activity of all known sulfatases. The deficiency of sulfatases was proposed to result from the lack of a co- or posttranslational modification that is common to all sulfatases and required for their cata...
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| Veröffentlicht in: | Cell 1995-07, Vol.82 (2), p.271-278 |
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| creator | Schmidt, Bernhard Selmer, Thorsten Ingendoh, Arnd Figurat, Kurt von |
| description | Multiple sulfatase deficiency (MSD) is a lysosomal storage disorder characterized by a decreased activity of all known sulfatases. The deficiency of sulfatases was proposed to result from the lack of a co- or posttranslational modification that is common to all sulfatases and required for their catalytic activity. Structural analysis of two catalytically active sulfatases revealed that a cysteine residue that is predicted from the cDNA sequence and conserved among all known sulfatases is replaced by a 2-amino-3-oxopropionic acid residue, while in sulfatases derived from MSD cells, this cysteine residue is retained. It is proposed that the co- or posttranslational conversion of a cysteine to 2-amino3-oxopropionic acid is required for generating catalytically active sulfatases and that deficiency of this protein modification is the cause of MSD. |
| doi_str_mv | 10.1016/0092-8674(95)90314-3 |
| format | Article |
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Selmer, Thorsten ; Ingendoh, Arnd ; Figurat, Kurt von</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c434t-442f1014d8b952f98aeb4fbf8be779c6243c456db3a7ab450ff25ec8aea2e6f13</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1995</creationdate><topic>Alanine - analogs & derivatives</topic><topic>Aldehydes</topic><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Cell Line</topic><topic>cerebroside-sulfatase</topic><topic>Conserved Sequence</topic><topic>Cysteine</topic><topic>DNA, Complementary</topic><topic>Fibroblasts - enzymology</topic><topic>Humans</topic><topic>Lysosomal Storage Diseases - enzymology</topic><topic>Lysosomal Storage Diseases - genetics</topic><topic>man</topic><topic>Molecular Sequence Data</topic><topic>multiple sulfatase deficiency</topic><topic>Mutation</topic><topic>N-acetylgalactosamine-4-sulfatase</topic><topic>protein modification</topic><topic>Sequence Homology, Amino Acid</topic><topic>Sulfatases - deficiency</topic><topic>Sulfatases - genetics</topic><topic>Sulfatases - isolation & purification</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Schmidt, Bernhard</creatorcontrib><creatorcontrib>Selmer, Thorsten</creatorcontrib><creatorcontrib>Ingendoh, Arnd</creatorcontrib><creatorcontrib>Figurat, Kurt von</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Human Genome Abstracts</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Cell</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Schmidt, Bernhard</au><au>Selmer, Thorsten</au><au>Ingendoh, Arnd</au><au>Figurat, Kurt von</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>A novel amino acid modification in sulfatases that is defective in multiple sulfatase deficiency</atitle><jtitle>Cell</jtitle><addtitle>Cell</addtitle><date>1995-07-28</date><risdate>1995</risdate><volume>82</volume><issue>2</issue><spage>271</spage><epage>278</epage><pages>271-278</pages><issn>0092-8674</issn><eissn>1097-4172</eissn><abstract>Multiple sulfatase deficiency (MSD) is a lysosomal storage disorder characterized by a decreased activity of all known sulfatases. The deficiency of sulfatases was proposed to result from the lack of a co- or posttranslational modification that is common to all sulfatases and required for their catalytic activity. Structural analysis of two catalytically active sulfatases revealed that a cysteine residue that is predicted from the cDNA sequence and conserved among all known sulfatases is replaced by a 2-amino-3-oxopropionic acid residue, while in sulfatases derived from MSD cells, this cysteine residue is retained. It is proposed that the co- or posttranslational conversion of a cysteine to 2-amino3-oxopropionic acid is required for generating catalytically active sulfatases and that deficiency of this protein modification is the cause of MSD.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>7628016</pmid><doi>10.1016/0092-8674(95)90314-3</doi><tpages>8</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | Cell, 1995-07, Vol.82 (2), p.271-278 |
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| source | MEDLINE; Elsevier ScienceDirect Journals Complete; Cell Press Free Archives; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals |
| subjects | Alanine - analogs & derivatives Aldehydes Amino Acid Sequence Animals Cell Line cerebroside-sulfatase Conserved Sequence Cysteine DNA, Complementary Fibroblasts - enzymology Humans Lysosomal Storage Diseases - enzymology Lysosomal Storage Diseases - genetics man Molecular Sequence Data multiple sulfatase deficiency Mutation N-acetylgalactosamine-4-sulfatase protein modification Sequence Homology, Amino Acid Sulfatases - deficiency Sulfatases - genetics Sulfatases - isolation & purification |
| title | A novel amino acid modification in sulfatases that is defective in multiple sulfatase deficiency |
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