A novel amino acid modification in sulfatases that is defective in multiple sulfatase deficiency.
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Schmidt B, Selmer T, Ingendoh A, von Figura K
A novel amino acid modification in sulfatases that is defective in multiple sulfatase deficiency.
Cell. 1995 Jul 28;82(2):271-8.
- PubMed ID
- 7628016 [ View in PubMed]
- 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-amino-3-oxopropionic acid is required for generating catalytically active sulfatases and that deficiency of this protein modification is the cause of MSD.