Human Sulfotransferases and Their Role in Chemical Metabolism

Gamage, Niranjali, Barnett, Amanda, Hempel, Nadine, Duggleby, Ronald, Windmill, Kelly, Martin, Jennifer and McManus, Michael 2006, Human Sulfotransferases and Their Role in Chemical Metabolism, Toxicologial sciences, vol. 90, no. 1, pp. 5-22, doi: 10.1093/toxsci/kfj061.

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Title Human Sulfotransferases and Their Role in Chemical Metabolism
Author(s) Gamage, Niranjali
Barnett, Amanda
Hempel, Nadine
Duggleby, Ronald
Windmill, Kelly
Martin, Jennifer
McManus, Michael
Journal name Toxicologial sciences
Volume number 90
Issue number 1
Start page 5
End page 22
Publisher Oxford University Press
Place of publication Oxford, England
Publication date 2006-03
ISSN 1096-6080
Keyword(s) human sulfotransferases
SULT1A1 regulation
SULT crystal structures
Summary 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. Interindividual 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.
Language eng
DOI 10.1093/toxsci/kfj061
Field of Research 060107 Enzymes
HERDC Research category C1.1 Refereed article in a scholarly journal
Copyright notice ©2005, Published by Oxford University Press on behalf of the Society of Toxicology
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