Emily K Schutsky

University of Pennsylvania, Filadelfia, Pennsylvania, United States

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Publications (3)12.87 Total impact

  • Source
    Christopher S Nabel · Emily K Schutsky · Rahul M Kohli ·
    Cell cycle (Georgetown, Tex.) 11/2013; 13(2). DOI:10.4161/cc.27036 · 4.57 Impact Factor
  • Source
    Yadilette Rivera-Colon · Emily K. Schutsky · Scott C. Garman ·
    Biophysical Journal 02/2013; 104(2):566-. DOI:10.1016/j.bpj.2012.11.3143 · 3.97 Impact Factor
  • [Show abstract] [Hide abstract]
    ABSTRACT: Lysosomal enzymes catalyze the breakdown of macromolecules in the cell. In humans, loss of activity of a lysosomal enzyme leads to an inherited metabolic defect known as a lysosomal storage disorder. The human lysosomal enzyme galactosamine-6-sulfatase (GALNS, also known as N-acetylgalactosamine-6-sulfatase and GalN6S; E.C. is deficient in patients with the lysosomal storage disease mucopolysaccharidosis IV A (also known as MPS IV A and Morquio A). Here, we report the three-dimensional structure of human GALNS, determined by X-ray crystallography at 2.2Å resolution. The structure reveals a catalytic gem diol nucleophile derived from modification of a cysteine side chain. The active site of GALNS is a large, positively charged trench suitable for binding polyanionic substrates such as keratan sulfate and chondroitin-6-sulfate. Enzymatic assays on the insect-cell-expressed human GALNS indicate activity against synthetic substrates and inhibition by both substrate and product. Mapping 120 MPS IV A missense mutations onto the structure reveals that a majority of mutations affect the hydrophobic core of the structure, indicating that most MPS IV A cases result from misfolding of GALNS. Comparison of the structure of GALNS to paralogous sulfatases shows a wide variety of active-site geometries in the family but strict conservation of the catalytic machinery. Overall, the structure and the known mutations establish the molecular basis for MPS IV A and for the larger MPS family of diseases.
    Journal of Molecular Biology 08/2012; 423(5):736-51. DOI:10.1016/j.jmb.2012.08.020 · 4.33 Impact Factor

Publication Stats

22 Citations
12.87 Total Impact Points


  • 2013
    • University of Pennsylvania
      • Perelman School of Medicine
      Filadelfia, Pennsylvania, United States
  • 2012–2013
    • University of Massachusetts Amherst
      • Department of Biochemistry and Molecular Biology
      Amherst Center, Massachusetts, United States