Dopamine sulfotransferase

Dajani R, Cleasby A, Neu M, Wonacott AJ, Jhoti H, Hood AM, et al. X-ray crystal structure of human dopamine sulfotransferase, SULT1A3. J Biol Chem 1999 53 37862-8. 

Xenobiotic food additives, drugs, and biologically active endogenous compounds can interact and affect body biochemistry. For example, dopamine sulfotransferase activity is strongly inhibited by the colorant tartrazine and flavorant vanillin, and vanillin, erythrosine B, and octyl gallate inhibit the sulfation of 17 alpha-ethinylestradiol, a xenobiotic steroid J75l... 

D and 3D descriptors with K-PLS and also illustrated that the more liberal leave out 50% 100 times behaved similarly (Table 15.1, panels F, G). The dopamine sulfotransferase Km model showed a similar pattern to the epoxide hydrolase models (Table 15.1, panel H). 

Taskinen, R. M. Cooke, G. R. Manchee, and M. W. H. Coughtrie,/. Biol. Chem., 53, 37862 (1999). X-Ray Crystal Structure of Human Dopamine Sulfotransferase, SULT1A3. 

Sulfotransferases (SULTs) are important for the metabolism of a number of drugs, neurotransmitters, and hormones, especially the steroid hormones. The cosubstrate for these reactions is 3 -phosphoadenosine 5 -phosphosulfate (PAPS) (Fig. 4.1). Like the aforementioned enzymes, sulfate conjugation typically renders the compound inactive and more water soluble. However, this process can also result in the activation of certain compounds, such as the antihypertensive minoxidil and several of the steroid hormones. Seven SULT isoforms identified in humans, including SULTs lAl to 1A3, possess activity toward phenolic substrates such as dopamine, estradiol, and acetaminophen. SULTIBI possesses activity toward such endogenous substrates as dopamine and triiodothyronine. SULTIEI has substantial activity toward steroid hormones, especially estradiol and dehydroepiandrosterone, and toward the anti-... 

The assay for monoamine oxidase contained in a final volume of 100 pL to 30 pL of homogenate and 50 pAf [7-14C] dopamine (0.93 mCi/mmol) or [7-,4C] tyramine (3.11 mCi/mmol) in 0.5 M phosphate buffer (pH 7.4). The assay for phenol sulfotransferase was also initiated by adding 30 pL of homogenate. The mixture contained 1.7 pAf [35S] 3 -phosphoadenosine-5 -phosphosulfate (1.51 Ci/mmol) and 50 pAf dopamine, 3,4-dihydroxyphenylacetic acid, or phenol in 10 mAf phosphate buffer (pH 6.4). After various incubation periods, the activity of either enzyme was stopped by addition of 30 pL of 2 N HC1. The resulting mixtures were centrifuged or filtered before analysis by HPLC. 

Figure 9,19 Chromatograms of the cosubstrate (PAPS) and products of liver phenol sulfotransferase activity. Upper tracing a, PAPS, b, sulfate-conjugated dopamine. Middle tracing a, PAPS, b, sufate-conjugated Dopac. Lower tracing a, PAPS, b, sulfate-conjugated phenol. The retention time for sulfate-conjugated dopamine, Dopac, and phenol was 4.5, 6.8, and 7.0 minutes, respectively. (From Sim and Hsu, 1990.)...

Phenolsulfotransferase catalyzes the transfer of active sulfate from 3 -phosphoadensine 5 -phosphosulfate to various phenols and catechols. Honkasalo and Nissinen (1988) developed an assay that is suitable for measuring both the thermolabile (TL) and thermostable (TS) isoforms of phenol sulfotransferase. Both are active toward phenols, while the TL form also conjugates catechols including dopamine. 

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