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Human sulfatases: a structural perspective to catalysis.

D Ghosh1

  • 1Hauptman-Woodward Medical Research Institute and Roswell Park Cancer Institute, 700 Ellicott Street, Buffalo, NY 14203, USA. ghosh@hwi.buffalo.edu

Cellular and Molecular Life Sciences : CMLS
|June 15, 2007
PubMed
Summary
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Sulfatase enzymes, crucial for breaking sulfate bonds, share conserved catalytic mechanisms. Structural analysis reveals unique membrane interactions for steroid sulfatase (STS), distinct from other sulfatases.

Area of Science:

  • Biochemistry
  • Enzymology
  • Structural Biology

Background:

  • Sulfatases are enzymes that hydrolyze sulfate ester bonds.
  • Seventeen sulfatase genes exist, with mutations causing genetic disorders.
  • All sulfatases share conserved catalytic cysteine residues, modified to formylglycine, essential for activity.

Purpose of the Study:

  • To compare and contrast the structures of human sulfatases.
  • To re-evaluate the catalytic mechanism using structural and functional data.
  • To investigate the unique characteristics of steroid sulfatase (STS) structure and function.

Main Methods:

  • Analysis of crystal structures of human arylsulfatases A and B (ARSA, ARSB), and steroid sulfatase (STS).
  • Comparison of structural features, active site characteristics, and substrate-binding interactions.

Related Experiment Videos

  • Functional data interpretation in the context of determined structures.

    • Main Results:

    • ARSA and ARSB are water-soluble, while STS is an integral membrane protein with a hydrophobic domain.
    • The active site of STS exhibits substrate-specific interactions, including an estrogen-recognition motif.
    • The lipid bilayer plays a critical role in the constitution of the STS active site due to its membrane proximity.

    Conclusions:

    • Sulfatase structures are generally similar, but STS possesses unique features due to its membrane association.
    • The catalytic mechanism of sulfatases is conserved, but STS's active site is influenced by its membrane environment.
    • Structural insights into STS can inform understanding of its role in biological processes and associated disorders.