| A NOVEL AMINO-ACID MODIFICATION IN SULFATASES THAT IS DEFECTIVE IN MULTIPLE SULFATASE DEFICIENCY |
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| Author(s): SCHMIDT B, SELMER T, INGENDOH A, VONFIGURA K |
| Source: CELL Volume: 82 Issue: 2 Pages: 271-278 Published: JUL 28 1995 |
| Times Cited: 167 References: 31 |
| 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 ail 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 5-amino-3-oxopropionic acid is required for generating catalytically active sulfatases and that deficiency of this protein modification is the cause of MSD. |
| Document Type: Article |
| Language: English |
Addresses:
1. UNIV GOTTINGEN, D-37073 GOTTINGEN, GERMANY
2. UNIV MUNSTER, D-48149 MUNSTER, GERMANY |
| Publisher: CELL PRESS, 50 CHURCH ST CIRCULATION DEPT, CAMBRIDGE, MA 02138 |
| Subject Category: Biochemistry & Molecular Biology; Cell Biology |
| IDS Number: RL760 |
| ISSN: 0092-8674 |