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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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Reversible covalent inhibition of a phenol sulfotransferase by coenzyme A.

Phenol sulfotransferases (SULTs), which normally bind 3'-phosphoadenosine-5'-phosphosulfate as the donor substrate, are inhibited by CoA and its thioesters. Here, we report that inhibition of bovine SULT1A1 by CoA is time-dependent at neutral pH under non-reducing conditions. The rates of inactivation by CoA indicate an initial reversible SULT:CoA complex with a dissociation constant of 5.7muM and an inactivation rate constant of 0.07min(-1). Titrations with CoA and prolonged incubations reveal that inactivation of the dimeric enzyme is stoichiometric, consistent with the observation of complete conversion of the protein to a slightly decreased electrophoretic mobility. Both activity and normal electrophoretic migration are restored by 2-mercaptoethanol. Mutagenesis demonstrated that Cys168 is the site of CoA adduction, and a consistent model was constructed that reveals a new SULT molecular dynamic. Cysteine reaction kinetics with Ellman's reagent revealed a PAPS-induced structural change consistent with the model that accounts for binding of CoA.[1]

References

  1. Reversible covalent inhibition of a phenol sulfotransferase by coenzyme A. Chodavarapu, S., Hertema, H., Huynh, T., Odette, J., Miller, R., Fullerton, A., Alkirwi, J., Hartsfield, D., Padmanabhan, K., Woods, C., Beckmann, J.D. Arch. Biochem. Biophys. (2007) [Pubmed]
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