The Chymotrypsin-Catalyzed Hydrolysis of Sultones
The Chymotrypsin-Catalyzed Hydrolysis of Sultones
复制标题
胰凝乳蛋白酶催化磺内酯水解
DOI：
10.1021/ja00978a057
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发表时间：
1967
影响因子：
15
通讯作者：
E. Kaiser
中科院分区：
文献类型：
--
作者：
J. Heidema;E. Kaiser
最近我们研究了含硫酸酯的碱催化水解反应。我们发现某些五元环含硫酯对碱的侵蚀特别不稳定。112例如，五元环磺酸盐，2-羟基-α-甲苯磺酸磺内酯（I），比开链类似物苯基-甲苯磺酸盐经历快106倍的氢氧根离子催化水解。我们现在希望报告我们对硝基取代的磺内酯Ⅱ 3与不同类型的亲核物质，蛋白水解酶α-糜蛋白酶（CT）的异常反应性的观察，以及发现Ⅱ可用于滴定CT的活性位点。
Recently we have been engaged in an investigation of the base-catalyzed hydrolyses of esters of sulfur-con-taining acids. We have found that certain five-mem-bered cyclicsulfur-containing esters are extraordinarily labile to alkaline attack. 112 For example, the five-membered cyclic sulfonate, 2-hydroxy-a-toluenesul-fonic acid sultone (I), undergoes hydroxide ion catalyzed hydrolysis 106 times faster than does the open-chain analog, phenyl-toluenesulfonate. We now wish to report our observations on the unusualreactivity of the nitro-substituted sultone II3 with a different type of nucleophilic species, the proteolytic enzyme a-chymotrypsin (CT), and the finding that II can be used to ti-trate the active sites of CT.