文献类型：期刊文献

英文题名：Reversible Photocontrol of Lipase Activity by Incorporating a Photoswitch into the Lid Domain

作者：Liu, Ying[1];Gao, Xin[1];Wei, Dongzhi[1];Ren, Yuhong[1]

机构：[1]East China Univ Sci & Technol, State Key Lab Bioreactor Engn, Shanghai 200237, Peoples R China

年份：2017

卷号：1

期号：9

起止页码：393

外文期刊名：CHEMPHOTOCHEM

收录：;EI(收录号：20231413837982);WOS:【SCI-EXPANDED(收录号:WOS:000410556300004)】；

基金：This work was funded by the National Special Fund for the State Key Laboratory of Bioreactor Engineering (2060204). We thank mass spectrometry technique support from the Institutional Technology Service Center of Shanghai Institute of Materia Medica, Chinese Academy of Sciences.

语种：英文

外文关键词：azobenzenes; enzyme activity; lipase; photoisomerization; photoswitch

摘要：Photocontrol of enzymatic activity has become a helpful strategy to control biological processes. Herein, a method for the reversible photocontrol of lipase activity was developed by utilizing the conformational change of the lid structure. A bifunctional azobenzene derivative, whose trans/cis-form photoisomerization processes could be used to control the folded and unfolded conformations of the alpha-helix structure, was cross-linked with two cysteine residues on the lid domain to achieve photocontrol of lipase activity. To screen for the optimum sites of cross-linking, several cysteine-replaced lipase variants were constructed. The variant C127C138 attached with a cross-linker showed a threefold fully reversible activity change after illumination with UV and blue light. Furthermore, the structural change in the alpha-helix of the lipase was confirmed by circular dichroism. This strategy could be applied for photocontrolling activity of other enzymes where an alpha-helix is an important structural component.