...
首页> 外文期刊>Biochemistry >On the Mechanism of Interaction of Organic Solvents with the Active Site of alpha-Chymotrypsin
【24h】

On the Mechanism of Interaction of Organic Solvents with the Active Site of alpha-Chymotrypsin

机译:有机溶剂与α-胰凝乳蛋白酶活性位点相互作用的机理

获取原文
获取原文并翻译 | 示例
           

摘要

Kinetic behavior of alpha-chymotrypsin in the reaction of hydrolysis of the N-acetyl-L-tyrosine derivatives was investigated in non-denaturing water-dimethylsulfoxide and water-ethanol mixtures. Similar specific interactions between the two solvents and the active site of alpha-chymotrypsin were shown to result in similar kinetic effects. It is proposed that the changes in the active site structure of the enzyme caused by the interaction with the organic solvents ("conformational isomer" formation) resulted in two parallel processes-acceleration of the acyl-enzyme formation step and a decrease in the deacylation rate. The possible molecular mechanism of this phenomenon and an adequate kinetic model describing the data are discussed.
机译:在非变性水-二甲基亚砜和水-乙醇混合物中研究了α-胰凝乳蛋白酶在N-乙酰基-L-酪氨酸衍生物水解反应中的动力学行为。两种溶剂与α-胰凝乳蛋白酶的活性位点之间的相似特异性相互作用显示出相似的动力学效应。提出由与有机溶剂的相互作用引起的酶活性位点结构的改变(“构象异构体”的形成)导致两个平行的过程-酰基-酶形成步骤的加速和脱酰率的降低。 。讨论了该现象的可能分子机理和描述数据的适当动力学模型。

著录项

相似文献

  • 外文文献
  • 中文文献
  • 专利
获取原文

客服邮箱:kefu@zhangqiaokeyan.com

京公网安备:11010802029741号 ICP备案号:京ICP备15016152号-6 六维联合信息科技 (北京) 有限公司©版权所有
  • 客服微信

  • 服务号