Human schistosomiasis is a disease which globally affects over 229 million people. Three major species affecting humans are Schistosoma mansoni, S. haematobium and S. japonicum. Previous treatment of S. mansoni includes the use of oxamniquine (OXA), a prodrug that is enzymatically activated in S. mansoni but is ineffective against S. haematobium and S. japonicum. The OXA activating enzyme was identified and crystallized, as being a S. mansoni sulfotransferase (SmSULT). S. haematobium and S. japonicum possess homologs of SmSULT (ShSULT and SjSULT) begging the question; why does oxamniquine fail to kill S. haematobium and S. japonicum adult worms? Investigation of the molecular structures of the sulfotransferases indicates that structural differences, specifically in OXA contact residues, do not abrogate OXA binding in the active sites as previously hypothesized. Data presented argue that the ability of SULTs to sulfate and thus activate OXA and its derivatives is linked to the ability of OXA to fit in the binding pocket to allow the transfer of a sulfur group.

人类血吸虫病是一种全球影响超过2.29亿人的疾病。影响人类的三种主要物种是曼氏血吸虫，血吸虫和日本血吸虫。曼氏葡萄球菌的先前治疗方法包括使用氧杂苯醌（oxaniquine，OXA），该药是在曼氏葡萄球菌中被酶激活的，但对血吸虫和日本血吸虫无效。OXA活化酶被鉴定并结晶，为曼氏曼陀罗磺基转移酶（Sm SULT）。血吸虫和日本血吸虫具有Sm SULT（ShSULT和Sj SULT）乞求问题；为什么草酸喹喔啉不能杀死血吸虫和日本血吸虫成虫？对磺基转移酶分子结构的研究表明，结构上的差异，特别是在OXA接触残基方面，并未消除先前假设的在活性位点的OXA结合。所提供的数据表明，SULTs产生硫酸盐并因此激活OXA及其衍生物的能力与OXA装配在结合袋中以允许硫基转移的能力有关。