Abstract
Sulfate conjugation is an important pathway in the biotransformation of many drugs, xenobiotic compounds, neurotransmitters, and hormones. Sulfation increases the water solubility of most compounds and, therefore, their renal excretion. It also usually results in a decrease in biological activity, but, in some cases, sulfate conjugation is required to “activate” drugs such as the antihypertensive medication minoxidil (Johnson et al. 1982; Meisheri et al. 1988). It can also play a role in the bioactivation of procarcinogens (Watabe et al. 1982). Even though sulfation was discovered by Baumann (1876) over a century ago, only within the past 30 years has the enzymology of this important reaction been studied in detail. One important step in that process was the development of accurate assays for the measurement of the activities of sulfotransferase (ST) enzymes, followed by characterization of the reactions catalyzed by those enzymes in tissue preparations. Simultaneously, attempts were made to separate and purify ST enzymes to make it possible to characterize the molecular species that catalyzed specific reactions. Unfortunately, overlap in substrate specificities of these enzymes has led to confusion with regard to their number and properties. That confusion has been compounded by the existence of at least two broad streams of ST research, one involving the biotransformation of drugs and xenobiotic compounds and the other involving the sulfation of hormones, especially steroid hormones.
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Weinshilboum, R., Otterness, D. (1994). Sulfotransferase Enzymes. In: Kauffman, F.C. (eds) Conjugation—Deconjugation Reactions in Drug Metabolism and Toxicity. Handbook of Experimental Pharmacology, vol 112. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-78429-3_2
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