Fernando P H, Sakakibara Y, Nakatsu S, Suiko M, Han J R, Liu M C
Department of Biological Resource Sciences, Miyazaki University, Japan.
Biochem Mol Biol Int. 1993 Jul;30(3):433-41.
A novel phenol sulfotransferase (PST) was detected in bovine liver microsomal membrane fraction. The enzyme was found to be capable of catalyzing the sulfation of simple phenolic compounds, with 3'-phosphoadenosine-5'-phosphosulfate as the sulfate donor. Detergent extracted PST showed a pH optimum of 5.7 and, among the simple phenols tested, the PST exhibited highest activity toward alpha-naphthol. No activities were detected when tyrosine and its derivatives were used as substrates. Both 2,6-dichloro-4-nitrophenol and chlorpromazine were capable of inhibiting the activity of the PST toward p-nitrophenol with inhibition Coefficient50 values of 100 nM and 4 mM, respectively.
在牛肝微粒体膜组分中检测到一种新型酚磺基转移酶（PST）。发现该酶能够以3'-磷酸腺苷-5'-磷酸硫酸酯作为硫酸供体催化简单酚类化合物的硫酸化反应。经去污剂提取的PST的最适pH为5.7，在所测试的简单酚类中，PST对α-萘酚的活性最高。当使用酪氨酸及其衍生物作为底物时未检测到活性。2,6-二氯-4-硝基苯酚和氯丙嗪均能够抑制PST对对硝基苯酚的活性，其抑制系数50值分别为100 nM和4 mM。
