Regular ArticleRedox Control of Aryl Sulfotransferase Specificity
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Sulfotransferases
2018, Comprehensive Toxicology: Third EditionA nano switch mechanism for the redox-responsive sulfotransferase
2012, Biochemical PharmacologySubstrate inhibition in human hydroxysteroid sulfotransferase SULT2A1: Studies on the formation of catalytically non-productive enzyme complexes
2011, Archives of Biochemistry and BiophysicsCitation Excerpt :Studies on the catalytic mechanism of cytosolic sulfotransferases have been primarily focused on the SULT1 family (previously known as either as phenol or aryl sulfotransferases). Kinetic and crystallographic studies on these enzymes have elucidated several general principles regarding the chemical mechanism of sulfuryl transfer from PAPS to an acceptor substrate [1,24–31], that, based on three-dimensional structural homologies, may be applicable to members of other SULT families. Details of the kinetic mechanisms for individual SULTs, however, continue to provide information on the substrate-dependent differences in sulfation reactions that define the specificities and functions of these enzymes.
Physicochemical properties of hydroxylated polychlorinated biphenyls aid in predicting their interactions with rat sulfotransferase 1A1 (rSULT1A1)
2011, Chemico-Biological InteractionsCitation Excerpt :This substrate inhibition is due to the formation of dead end complexes between the substrate, enzyme and the co-product of sulfation, adenosine-3′,5′-diphosphate (PAP) [26,27]. The release of PAP from these dead-end complexes becomes a rate-limiting component of the rSULT1A1-catalyzed reaction [27], and changes in the conformation at the PAP/PAPS-binding site of the enzyme may affect catalytic function and inhibition through facilitation of PAP-release [2,27]. Thus the present studies are focused on molecular characteristics of OHPCB-substrates that influence the rate of reaction, the use of calculated estimates of physicochemical parameters in the prediction of interactions of OHPCBs as substrates and inhibitors, and the potential role of the redox status of the enzyme in determining its binding interactions with OHPCBs and PAP.
Sulfotransferases
2010, Comprehensive Toxicology, Second EditionNrf2 the rescue: Effects of the antioxidative/electrophilic response on the liver
2010, Toxicology and Applied Pharmacology
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Present address: Novartis Institute for Medical Sciences, 5 Gower Place, London WC1E 6BN, UK.
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To whom correspondence should be addressed at the National Institutes of Health, Building 8, Room 311, Bethesda, MD 20892. Fax: (301) 480-0040. E-mail: [email protected].