Mechanistic studies of β-arylsulfotransferase IV

Eli Chapman, Marian C. Bryan, Chi Huey Wong

Research output: Contribution to journalArticle

24 Scopus citations

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 β-arylsulfotransferase IV likely proceeds by a dissociative (sulfotrioxide-like) mechanism. Values for the Broønsted coefficients (βnuc and βlg) are +0.33 and -0.45, giving Leffler α values of 0.19 and 0.61 for the forward and reverse reactions, respectively.

Original languageEnglish (US)
Pages (from-to)910-915
Number of pages6
JournalProceedings of the National Academy of Sciences of the United States of America
Volume100
Issue number3
DOIs
StatePublished - Feb 4 2003

Keywords

  • Linear free energy
  • Mechanism
  • Sulfotransferase

ASJC Scopus subject areas

  • General

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