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1: Cell. 1995 Jul 28;82(2):271-8.Click here to read Links

A novel amino acid modification in sulfatases that is defective in multiple sulfatase deficiency.

Schmidt B, Selmer T, Ingendoh A, von Figura K.

Universität Göttingen, Federal Republic of Germany.

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.

PMID: 7628016 [PubMed - indexed for MEDLINE]