Inhibition of human liver and duodenum sulfotransferases by drugs and dietary chemicals: a review of the literature.

  title={Inhibition of human liver and duodenum sulfotransferases by drugs and dietary chemicals: a review of the literature.},
  author={Gian Maria Pacifici},
  journal={International journal of clinical pharmacology and therapeutics},
  volume={42 9},
  • G. Pacifici
  • Published 1 September 2004
  • Biology, Chemistry, Medicine
  • International journal of clinical pharmacology and therapeutics
Sulfotransferase catalyzes the transfer of sulfate, donated by 3'-phosphoadenosine-5'-phosphosulfate, to an acceptor substrate that may be a hydroxy group or an amine group. Man is exposed daily to drugs and dietary chemicals that can inhibit sulfotransferase activity. The aim of this study was to review the literature concerning the inhibition of sulfotransferases by drugs and dietary chemicals in the human liver and duodenum. The IC50 value of mefenamic acid for human liver phenol… 
para-Nitrophenyl Sulfate Activation of Human Sulfotransferase 1A1 Is Consistent with Intercepting the E·PAP Complex and Reformation of E·PAPS*
On the basis of activation of SULT1A1 by para-nitrophenyl sulfate (pNPS), an ordered bypass mechanism has been proposed where pNPS sulfates PAP prior to its release from the E·PAP complex regenerating E· PAPS.
Caffeine induction of sulfotransferases in rat liver and intestine
It is suggested that consumption of caffeine can induce drug metabolizing SULTs in drug detoxification tissues in a dose‐dependent manner and may be affected by different hormone secretion patterns and levels.
Identification and localization of soluble sulfotransferases in the human gastrointestinal tract.
SULTs are abundant in the gastrointestinal tract of man and it is suspected that they are involved in the presystemic elimination of bioactive food-borne components, including aglycones released by gut microbiota, as well as the bioactivation of some procarcinogens.
Isotope exchange at equilibrium indicates a steady state ordered kinetic mechanism for human sulfotransferase.
First-order kinetics, observed for all the is otopic exchange reactions studied over the entire time scale that was monitored, indicates that the system was truly at equilibrium prior to addition of an isotopic pulse.
Structural and Chemical Profiling of the Human Cytosolic Sulfotransferases
The family-wide analysis of the screening and structural data provides a comprehensive, high-level view of the determinants of substrate binding, the mechanisms of inhibition by substrates and environmental toxins, and the functions of the orphan family members SULT1C3 and SULT4A1.
The structure of the catechin-binding site of human sulfotransferase 1A1
The structure of an SULT allosteric binding site is presented—the catechin-binding site of SULT1A1 bound to epigallocatechin gallate (EGCG), which offers a molecular explanation for the isozyme specificity of EGCG, which is corroborated experimentally.
Opicapone Sulfation: Sulfotransferase Isoforms Characterization
The kinetics for the conversion of opicapone into sulfated metabolite by intestinal, kidney and liver S9 fractions and by human recombinant SULTs were characterized, using sensitive and specific Liquid Chromatography tandem Mass Spectrometry (LC-MS/MS) equipment.