| Structural highlights
Function
[ST1D1_MOUSE] Sulfotransferase with broad substrate specificity that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the sulfate conjugation of catecholamines, such as dopamine, prostaglandins, leukotriene E4, drugs and xenobiotic compounds. Has sulfotransferase activity towards p-nitrophenol, 2-naphthylamine and minoxidil (in vitro). Sulfonation increases the water solubility of most compounds, and therefore their renal excretion, but it can also result in bioactivation to form active metabolites.[1] [2] [3] [4] [5]
Evolutionary Conservation
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Publication Abstract from PubMed
In mammals, sulfonation as mediated by specific cytosolic sulfotransferases (SULTs) plays an important role in the homeostasis of dopamine and other catecholamines. To gain insight into the structural basis for dopamine recognition/binding, we determined the crystal structure of a mouse dopamine-sulfating SULT, mouse SULT1D1 (mSULT1D1). Data obtained indicated that mSULT1D1 comprises of a single alpha/beta domain with a five-stranded parallel beta-sheet. In contrast to the structure of the human SULT1A3 (hSULT1A3)-dopamine complex previously reported, molecular modeling and mutational analysis revealed that a water molecule plays a critical role in the recognition of the amine group of dopamine by mSULT1D1. These results imply differences in substrate binding between dopamine-sulfating SULTs from different species.
Crystal structure of mSULT1D1, a mouse catecholamine sulfotransferase.,Teramoto T, Sakakibara Y, Inada K, Kurogi K, Liu MC, Suiko M, Kimura M, Kakuta Y FEBS Lett. 2008 Nov 26;582(28):3909-14. Epub 2008 Oct 31. PMID:18977225[6]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Shimada M, Terazawa R, Kamiyama Y, Honma W, Nagata K, Yamazoe Y. Unique properties of a renal sulfotransferase, St1d1, in dopamine metabolism. J Pharmacol Exp Ther. 2004 Aug;310(2):808-14. Epub 2004 Apr 15. PMID:15087475 doi:http://dx.doi.org/10.1124/jpet.104.065532
- ↑ Teramoto T, Sakakibara Y, Inada K, Kurogi K, Liu MC, Suiko M, Kimura M, Kakuta Y. Crystal structure of mSULT1D1, a mouse catecholamine sulfotransferase. FEBS Lett. 2008 Nov 26;582(28):3909-14. Epub 2008 Oct 31. PMID:18977225 doi:S0014-5793(08)00867-3
- ↑ Wong S, Tan K, Carey KT, Fukushima A, Tiganis T, Cole TJ. Glucocorticoids stimulate hepatic and renal catecholamine inactivation by direct rapid induction of the dopamine sulfotransferase Sult1d1. Endocrinology. 2010 Jan;151(1):185-94. doi: 10.1210/en.2009-0590. Epub 2009 Dec, 4. PMID:19966186 doi:http://dx.doi.org/10.1210/en.2009-0590
- ↑ Sakakibara Y, Yanagisawa K, Takami Y, Nakayama T, Suiko M, Liu MC. Molecular cloning, expression, and functional characterization of novel mouse sulfotransferases. Biochem Biophys Res Commun. 1998 Jun 29;247(3):681-6. PMID:9647753 doi:http://dx.doi.org/10.1006/bbrc.1998.8872
- ↑ Liu MC, Sakakibara Y, Liu CC. Bacterial expression, purification, and characterization of a novel mouse sulfotransferase that catalyzes the sulfation of eicosanoids. Biochem Biophys Res Commun. 1999 Jan 8;254(1):65-9. PMID:9920733 doi:http://dx.doi.org/10.1006/bbrc.1998.9872
- ↑ Teramoto T, Sakakibara Y, Inada K, Kurogi K, Liu MC, Suiko M, Kimura M, Kakuta Y. Crystal structure of mSULT1D1, a mouse catecholamine sulfotransferase. FEBS Lett. 2008 Nov 26;582(28):3909-14. Epub 2008 Oct 31. PMID:18977225 doi:S0014-5793(08)00867-3
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