Download MendeleyStructure of a human lysosomal sulfatase.
Bond, C.S., Clements, P.R., Ashby, S.J., Collyer, C.A., Harrop, S.J., Hopwood, J.J., Guss, J.M.(1997) Structure 5: 277-289
- PubMed: 9032078
- DOI: https://doi.org/10.1016/s0969-2126(97)00185-8
- Primary Citation of Related Structures:
1FSU - PubMed Abstract:
. Sulfatases catalyze the hydrolysis of sulfuric acid esters from a wide variety of substrates including glycosaminoglycans, glycolipids and steroids. There is sufficient common sequence similarity within the class of sulfatase enzymes to indicate that they have a common structure. Deficiencies of specific lysosomal sulfatases that are involved in the degradation of glycosamino-glycans lead to rare inherited clinical disorders termed mucopolysaccharidoses. In sufferers of multiple sulfatase deficiency, all sulfatases are inactive because an essential post-translational modification of a specific active-site cysteine residue to oxo-alanine does not occur. Studies of this disorder have contributed to location and characterization of the sulfatase active site. To understand the catalytic mechanism of sulfatases, and ultimately the determinants of their substrate specificities, we have determined the structure of N-acetylgalactosamine-4-sulfatase.
Organizational Affiliation:
Department of Biochemistry, University of Sydney, NSW 2006 Australia.
