10326-52-0Relevant academic research and scientific papers
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 (1999)
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.
ENZYMIC SYNTHESIS OF STEROID SULFATES XVI. SPECIFICITY AND REGULATION OF HUMAN ADRENAL HYDROXYSTEROID SULFOTRANSFERASE
Adams, J. B.,McDonald, D.
, p. 575 - 586 (2007/10/02)
Pure hydroxysteroid sulfotransferase (EG 2.8.2.2) of human adrenal glands possesses a wide substrate specificity towards steroids.This wide specificity has now been found to extend to simple alcohols; normal aliphatic alcohols from C3 onwards acting as substrates with C9 showing the highest rate.Increased rate was accompanied by a decrease in Km.In marked contrast to the sulfurylation of steroids such as dehydroepiandrosterone, which exhibit wave-like kinetics, the kinetics with simple alcohols were of the normal Michaelis-Menten type.By means of enzyme antibody and enzyme stability studies evidence was provided that one and the same enzyme was responsible for sulfurylation of hydroxyls on the 3- and 17-positions of steroids and simple alcohols.The data lend support to previous evidence that the enzyme controls the secretion of dehydroepiandrosterone sulfate via steroid-specific binding sites, enabling self-regulation in response to ACTH action.
