651-48-9Relevant articles and documents
Testosterone sulfotransferase: Evidence in the guinea pig that this reaction is carried out by 3α-hydroxysteroid sulfotransferase
Park, Byoung C.,Lee, Young C.,Strott, Charles A.
, p. 510 - 517 (2007/10/03)
During the course of isolating, characterizing, and cloning estrogen and 3-hydroxysteroid sulfotransferases from the guinea pig adrenal gland, it was noted that cytosolic preparations from this tissue would also sulfonate testosterone. Therefore, we set out to isolate and clone the enzyme that performs this reaction. Testosterone sulfotransferase (TST) was isolated from the guinea pig adrenal by using the standard procedures of ion exchange, affinity, and high-performance liquid chromatography. When purified, TST was examined by liquid-phase nondenaturing isoelectric focusing, it was found that the TST activity profile completely overlapped with the activity profile of the 3α-hydroxysteroid sulfotransferase (3αHST) isoform, but not the 3β-hydroxysteroid sulfotransferase (3βHST) isoform. This finding was further investigated by overexpressing the cDNAs for 3αHST and 3βHST in Escherichia coli and examining the expressed proteins for TST activity. This experiment confirmed that 3αHST does indeed function as a TST. In addition, 3αHST was also found to sulfonate estradiol but not estrone, a finding that further suggested that 3αHST may function as a general 17β-hydroxysteroid sulfotransferase. Copyright (C) 1999.
Mouse steroid sulfotransferases. Substrate specificity and preliminary X-ray crystallographic analysis
Kakuta, Yoshimitsu,Pedersen, Lars C.,Chae, Kun,Song, Wen-Chao,Leblanc, Darryl,London, Robert,Carter, Charles W.,Negishi, Masahiko
, p. 313 - 317 (2007/10/03)
Three mouse cytosolic sulfotransferases were expressed in Escherichia coli cells in order to study their substrate specificities toward natural as well as synthetic steroid hormones. The K(m) and V(max) values confirmed the high substrate specificity of estrogen and hydroxysteroid sulfotransferases toward estradiol and dehydroepiandrosterone, respectively. In sharp contrast, the synthetic estrogen diethylstilbestrol was metabolized efficiently by both enzymes to its disulfate ester. These sulfotransferases display highly stereospecific sulfotransferase activity for sulfating only the trans-isomer of diethylstilbestrol. Crystals suitable for high-resolution structure determination of estrogen sulfotransferase were grown with polyethylene glycol. The crystals belong to the orthorhombic space group P21212, and diffracted to 2.5 A.
ENZYMATIC SULFATION OF CHOLESTEROL BY RAT GASTRIC MUCOSA
Lin, Y. N.,Horowitz, M. I.
, p. 697 - 708 (2007/10/02)
A sulfotransferase which catalyzes transfer of the sulfate group from 3'-phosphoadenosine-5'phosphosulfate to cholesterol has been demonstrated in the rat gastric mucosa.The product of the reaction was characterized as cholesterol sulfate by two-dimensional thin-layer chromatography behavior, and gas-liquid chromatography of cholesterol after acid solvolysis.The bulk of enzyme activity was found in the cytosol fraction.Sulfation of cholesterol did not require added Mg+2, Mn+2, or Ca+2, and was unaffected by ethylenediaminetetraacetate.Triton X-100 moderatly enhanced the enzyme activity.A broad pH optimum from pH 6.0 - 9.0 was exhibited with a maximum at pH 7.0 - 7.5.The apparent Km for PAPS was 0.8 x 10-6M.The possible function of cholesterol sulfate in gastric mucosa is discussed.