Cytosolic sulfotransferase (ST) enzymes catalyze the sulfate conjugation of many drugs, xenobiotic compounds, hormones, and neurotransmitters. Sulfotransferases such as SULT1B1 catalyze the biotransformation of a large number of endogenous compounds such as neurotransmitters, steroids, bile acids, and thyroid hormones, as well as drugs and xenobiotics. SULT1B1 contains a binding site for the sulfate donor, 3-prime-phosphoadenosine 5-prime-phosphosulfate, and a cysteine residue conserved in the ST1 gene family of sulfotransferases. SULT1B1 shares between 51.5% and 56.3% amino acid sequence identity with members of the phenol sulfotransferase gene family. Northern blot analysis detects 4 SULT1B1 transcripts between 79 kb and 13 kb expressed at highest levels in liver, peripheral blood leukocytes, colon, small intestine, and spleen. Lower expression is detected in lung, placenta, and thymus, and no expression is detected in other tissues. Recombinant rat and human SULT1B1, expressed in E. coli, catalyze sulfation of p-nitrophenol, 3,3-prime,5-triiodothyronine (T3), and dopamine, but not of beta-estradiol and dehydroepiandrosterone. SULT1B1 shows higher affinities for formation of T3 sulfate than do the phenol sulfotransferases ST1A3 (SULT1A1) or ST1A5. Bacterially-expressed SULT1B1 sulfates small phenols such as 1-naphthol and p-nitrophenol and thyroid hormones, including 3,3-prime-diiodothyronine, triiodothyronine, reverse triiodothyronine, and thyroxine. No activity is detected against several sterols or dopamine.
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