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ToxSci Advance Access published online on December 1, 2005
Toxicological Sciences, doi:10.1093/toxsci/kfj061
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© The Author 2005. Published by Oxford University Press on behalf of the Society of Toxicology. All rights reserved. For Permissions, please email: journals.permissions@oxfordjournals.org
Received September 21, 2005
Accepted November 28, 2005

Review

Human Sulfotransferases and their Role in Chemical Metabolism

Niranjali Gamage 1, Amanda Barnett 1, Nadine Hempel 2, Ronald G. Duggleby 3, Kelly F. Windmill 4, Jennifer L. Martin 5, and Michael E. McManus 1 *

1 School of Biomedical Sciences, University of Queensland, Queensland 4072, Australia
2 Department of Medicine/Oncology, Duke University Medical Center, Durham NC 27710, USA
3 School of Molecular and Microbial Sciences, University of Queensland, Queensland 4072, Australia
4 School of Exercise and Health Sciences, Deakin University, Australia
5 School of Molecular and Microbial Sciences, University of Queensland, Queensland 4072, Australia; Institute for Molecular Bioscience, University of Queensland, Queensland 4072, Australia

* To whom correspondence should be addressed.
Michael E. McManus, E-mail: m.mcmanus{at}uq.edu.au


  Abstract

Sulfonation is an important reaction in the metabolism of numerous xenobiotics, drugs and endogenous compounds. A supergene family of enzymes called sulfotransferases (SULTs) catalyze this reaction. In most cases, the addition of a sulfonate moiety to a compound increases its water solubility and decreases its biological activity. However, many of these enzymes are also capable of bioactivating procarcinogens to reactive electrophiles. In humans three SULT families, SULT1, SULT2 and SULT4, have been identified that contain at least thirteen distinct members. SULTs have a wide tissue distribution and act as a major detoxification enzyme system in adult and the developing human fetus. Nine crystal structures of human cytosolic SULTs have now been determined and together with site-directed mutagenesis experiments and molecular modeling, we are now beginning to understand the factors that govern distinct but overlapping substrate specificities. These studies have also provided insight into the enzyme kinetics and inhibition characteristics of these enzymes. The regulation of human SULTs remains as one of the least explored areas of research in the field though there have been some recent advances on the molecular transcription mechanism controlling the individual SULT promoters. Inter-individual variation in sulfonation capacity may be important in determining an individual's response to xenobiotics and recent studies have begun to suggest roles for SULT polymorphism in disease susceptibility. This review aims to provide a summary of our present understanding of the function of human cytosolic sulfotransferases.


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