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Rapid CommunicationMinireview

Design and Interpretation of Human Sulfotransferase 1A1 Assays

Ting Wang, Ian Cook and Thomas S. Leyh
Drug Metabolism and Disposition April 2016, 44 (4) 481-484; DOI: https://doi.org/10.1124/dmd.115.068205
Ting Wang
Department of Microbiology and Immunology, Albert Einstein College of Medicine, Bronx, New York
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Ian Cook
Department of Microbiology and Immunology, Albert Einstein College of Medicine, Bronx, New York
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Thomas S. Leyh
Department of Microbiology and Immunology, Albert Einstein College of Medicine, Bronx, New York
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This article has a correction. Please see:

  • Correction to “Design and Interpretation of Human Sulfotransferase A1 Assays” - April 01, 2016

Abstract

The human sulfotransferases (SULTs) regulate the activities of hundreds, if not thousands, of small molecule metabolites via transfer of the sulfuryl-moiety (-SO3) from the nucleotide donor, 3′-phosphoadenosine 5′-phosphosulfate (PAPS) to the hydroxyls and amines of the recipients. Our understanding of the molecular basis of SULT catalysis has expanded considerably in recent years. The basic kinetic mechanism of these enzymes, previously thought to be ordered, has been redefined as random for SULT2A1, a representative member of the superfamily. An active-site cap whose structure and dynamics are highly responsive to nucleotides was discovered and shown to be critical in determining SULT selectivity, a topic of longstanding interest to the field. We now realize that a given SULT can operate in two specificity modes—broad and narrow—depending on the disposition of the cap. More recent work has revealed that the caps of the SULT1A1 are controlled by homotropic allosteric interactions between PAPS molecules bound at the dimer’s active sites. These interactions cause the catalytic efficiency of SULT1A1 to vary in a substrate-dependent fashion by as much as two orders of magnitude over a range of PAPS concentrations that spans those found in human tissues. SULT catalysis is further complicated by the fact that these enzymes are frequently inhibited by their substrates. This review provides an overview of the mechanistic features of SULT1A1 that are important for the design and interpretation of SULT1A1 assays.

Footnotes

    • Received November 2, 2015.
    • Accepted December 7, 2015.
  • This work was supported by the National Institutes of Health General Medical Sciences [GM106158].

  • dx.doi.org/10.1124/dmd.115.068205.

  • Copyright © 2016 by The American Society for Pharmacology and Experimental Therapeutics
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Drug Metabolism and Disposition: 44 (4)
Drug Metabolism and Disposition
Vol. 44, Issue 4
1 Apr 2016
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Rapid CommunicationMinireview

Designing SULT1A1 Assays

Ting Wang, Ian Cook and Thomas S. Leyh
Drug Metabolism and Disposition April 1, 2016, 44 (4) 481-484; DOI: https://doi.org/10.1124/dmd.115.068205

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Rapid CommunicationMinireview

Designing SULT1A1 Assays

Ting Wang, Ian Cook and Thomas S. Leyh
Drug Metabolism and Disposition April 1, 2016, 44 (4) 481-484; DOI: https://doi.org/10.1124/dmd.115.068205
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