A novel amino acid modification in sulfatases that is defective in multiple sulfatase deficiency
1995 | journal article. A publication with affiliation to the University of Göttingen.
Jump to: Cite & Linked | Documents & Media | Details | Version history
Documents & Media
Details
- Authors
- Schmidt, Bernhard; Selmer, Thorsten; Ingendoh, Arnd; Figura, Kurt von
- 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 Mp. cells, this cysteine residue is retained. It is proposed that the co- or posttranslational conversion of a cysteine to 2-amino- 3-oxopropionic acid is required for generating catalytically active sulfatases and that deficiency of this protein modification is the cause of MSD.
- Issue Date
- 1995
- Publisher
- Cell Press
- Journal
- Cell
- File Format
- application/pdf
- ISSN
- 0092-8674
- Language
- English