Rens-Domiano S S, Roth J A
J Neurochem. 1987 May;48(5):1411-5. doi: 10.1111/j.1471-4159.1987.tb05679.x.
Structural analogues of the sulfate donor 3'-phosphoadenosine-5'-phosphosulfate (3',5'-PAPS) were examined for their ability to inhibit dopamine and phenol sulfation by the M and P forms of phenol sulfotransferase (PST), respectively. The Ki values for each of the adenosine derivatives were calculated from the rate equation for PST. For both M and P PST, the naturally occurring product 3'-phosphoadenosine-5'-phosphate, (3',5'-PAP), was shown to be the most effective inhibitor. The weakest inhibitors of the two sulfotransferases were 5'-adenosine phosphosulfate and the three AMP derivatives, which were less than 1,000 times as effective as 3',5'-PAP. 5'-ATP, 2',5'-PAPS, 2',5'-PAP, and 5'-ADP were similar in their inhibition of M and P PST and were all approximately 100 times less effective than the natural end product. These data reveal that there is a rigid structural requirement for binding of the ribose portion of adenosine to both M and P PST that involves the groups on both the 3' and 5' positions. The effectiveness of binding to the two enzymes may depend on both steric factors as well as the distribution of negative charges on the ribose ring.
研究了硫酸盐供体3'-磷酸腺苷-5'-磷酸硫酸酯（3',5'-PAPS）的结构类似物分别抑制酚硫酸转移酶（PST）的M型和P型对多巴胺和苯酚进行硫酸化的能力。根据PST的速率方程计算了每种腺苷衍生物的Ki值。对于M型和P型PST，天然存在的产物3'-磷酸腺苷-5'-磷酸（3',5'-PAP）被证明是最有效的抑制剂。这两种硫酸转移酶最弱的抑制剂是5'-腺苷磷酸硫酸酯和三种AMP衍生物，它们的效力不到3',5'-PAP的1000倍。5'-ATP、2',5'-PAPS、2',5'-PAP和5'-ADP对M型和P型PST的抑制作用相似，且效力均比天然终产物低约100倍。这些数据表明，腺苷核糖部分与M型和P型PST结合存在严格的结构要求，涉及3'和5'位上的基团。与这两种酶结合的有效性可能取决于空间因素以及核糖环上负电荷的分布。
