吉林大学学报(理学版)

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6A,6A′-苯胺-6B,6B′-硒桥联-β-CD底物的特异性

吕绍武1, 吕冰聪1, 宗慧1, 陶进2, 王宏龄2   

  1. 1. 吉林大学 分子酶学工程教育部重点实验室, 长春 130012; 2. 玉米深加工国家工程研究中心, 长春 130033
  • 收稿日期:2013-03-11 出版日期:2013-09-26 发布日期:2013-09-17
  • 通讯作者: 吕绍武 E-mail:lvsw@jlu.edu.cn

Substrate Specificity of 6A,6A′-Dianilino-6B,6B′-diselenide-bis-β-cyclodextrin

LV Shaowu1, LV  Bingcong1, ZONG Hui 1, TAO Jin2, WANG Hongling2   

  1. 1. Key Laboratory for Molecular Enzymology and Engineering of the Ministry of Education,Jilin University, Changchun 130012, China;2. National Engineering Research Center of Maize Further Processing, Changchun 130033, China
  • Received:2013-03-11 Online:2013-09-26 Published:2013-09-17
  • Contact: LV Shaowu E-mail:lvsw@jlu.edu.cn

摘要:

运用双酶偶联体系分别测定6A,6A′-二苯胺-6B,6B′-二硒桥联-β-CD(6-AnSeCD)催化谷胱甘肽(GSH)还原过氧化氢(H2O2)、 叔丁基过氧化氢(t-BuOOH)和枯烯过氧化氢(CumOOH)3种结构不同氢过氧化物的谷胱甘肽过氧化物酶(GPx)活力, 并考察6-AnSeCD催化这3种氢过氧化物的稳态动力学. 结果表明: 6AnSeCD还原CumOOH的GPx活力最高; 6-AnSeCD的催化机制为乒乓机制; 6AnSeCD的假一级反应速度常数(kmax)、 米氏常数(Km)和二级反应速率常数(k)均显示CumOOH为6-AnSeCD的最适底物.

关键词: 谷胱甘肽过氧化物酶, 模拟物, 环糊精, 稳态动力学

Abstract:

The gluathione peroxidase (GPx) activities of 6A,6A′-dianilino-6B,6B′-diselenide-bis-β-cyclodextrin (6-AnSeCD) in the reduction of H2O2, tertbutylhydroperoxide (t-BuOOH) and cumenyl hydroperoxide (CumOOH) by glutathione (GSH) were assessed in classical coupled reductase assay, and the steadystate kinetics of 6AnSeCD in the reduction of three hydrogen peroxides was studied. The 6-AnSeCD displayed best GPx activity for the reduction of CumOOH by GSH. A pingpong mechanism was observed in the steadystate kinetic studies on the 6-AnSeCDcatalyzed reactions. We further compared kmax, Km and secondorder rate constant of 6-AnSeCD. The results show the CumOOH is the most preferred substrate for 6-AnSeCD.

Key words: gluathione peroxidase, mimic, cyclodextrin, steady state kinetics

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