Enzymic synthesis of steroid sulfates XVI. Specificity and regulation of human adrenal hydroxysteroid sulfotransferase.
Pure hydroxysteroid sulfotransferase (EC 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.
D000311:Adrenal Glands / Q000201:enzymology*; D000818:Animals; D002417:Cattle; D002846:Chromatography, Affinity; D006801:Humans; D007700:Kinetics; D008099:Liver / Q000201:enzymology; D013379:Substrate Specificity; D015238:Sulfotransferases; D013466:Sulfurtransferases / Q000302:isolation & purification / Q000378:metabolism*
D013466:Sulfurtransferases; D015238:Sulfotransferases; C028152:alcohol sulfotransferase