Bouthillier M, Chapdelaine A, Bleau G, Roberts K D
Steroids. 1981 Nov;38(5):523-35. doi: 10.1016/0039-128x(81)90052-0.
Steroid sulfotransferase activity is present in the cytosol fraction of hamster epididymis. The activity of this enzyme is increased by magnesium ion. Cysteine is essential to assure optimal activity. Adenosine-3'-phosphate-5'-phosphosulfate is required as sulfate donor and an apparent Km of 62 microM was calculated. Inhibition studies suggest that this enzyme preferentially catalyzes the sulfurylation of the 3 beta-hydroxyl group of delta 5-steroids. An unusual feature of the enzyme is a pH optimum at pH 10.
类固醇硫酸转移酶活性存在于仓鼠附睾的胞质溶胶部分。该酶的活性可被镁离子增强。半胱氨酸对于确保最佳活性至关重要。需要3'-磷酸腺苷-5'-磷酸硫酸酯作为硫酸盐供体，计算得出的表观Km为62微摩尔。抑制研究表明，该酶优先催化δ5-类固醇3β-羟基的硫酸化。该酶的一个不寻常特征是最适pH值为10。
