Article
Reversible covalent inhibition of a phenol sulfotransferase by coenzyme A.
Archives of biochemistry and biophysics - 15 Jan 2007
Chodavarapu Sundari, Hertema Heather, Huynh Tien, Odette Jessica, Miller Rachel, Fullerton Aaron, Alkirwi Jason, Hartsfield D'Juan, Padmanabhan Kaillathe, Woods Caleb, Beckmann Joe D
Abstract excerpt
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 5.7 microM and an...
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