Mechanistic studies of beta-arylsulfotransferase IV

Proc Natl Acad Sci U S A. 2003 Feb 4;100(3):910-5. doi: 10.1073/pnas.0337638100. Epub 2003 Jan 23.

Abstract

Sulfotransferases are an important class of enzymes that catalyze the transfer of a sulfuryl group to a hydroxyl or amine moiety on various molecules including small-molecule drugs, steroids, hormones, carbohydrates, and proteins. They have been implicated in a number of disease states but remain poorly understood, complicating the design of specific, small-molecule inhibitors. A linear free-energy analysis in both the forward and reverse directions indicates that the transfer of a sulfuryl group to an aryl hydroxyl group catalyzed by beta-arylsulfotransferase IV likely proceeds by a dissociative (sulfotrioxide-like) mechanism. Values for the Brønsted coefficients (beta(nuc) and beta(lg)) are +0.33 and -0.45, giving Leffler alpha values of 0.19 and 0.61 for the forward and reverse reactions, respectively.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Arylsulfotransferase / chemistry*
  • Arylsulfotransferase / metabolism*
  • Binding Sites
  • Catalysis
  • Cytosol / enzymology
  • Fluorine / pharmacology
  • Hydrogen-Ion Concentration
  • Kinetics
  • Models, Chemical
  • Molecular Sequence Data
  • Mutagenesis, Site-Directed
  • Oxygen / chemistry
  • Protein Structure, Tertiary
  • Sequence Homology, Amino Acid
  • Thermodynamics

Substances

  • Fluorine
  • Arylsulfotransferase
  • Oxygen