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Updated: Jun 29, 2025

Anaerobic Protein Purification and Kinetic Analysis via Oxygen Electrode for Studying DesB Dioxygenase Activity and Inhibition
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Anaerobic Protein Purification and Kinetic Analysis via Oxygen Electrode for Studying DesB Dioxygenase Activity and Inhibition

Published on: October 3, 2018

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重建动态关联网络,通过设计远端链间二硫化物键,同时提高2,3-butanediol脱酶的活性和稳定性

Zhongji Pu1, Jiawen Cao2, Wenhui Wu3

  • 1Institute of Bioengineering, College of Chemical and Biological Engineering, Zhejiang University, Hangzhou, Zhejiang 310027, China; ZJU-Hangzhou Global Scientific and Technological Innovation Centre, Hangzhou, Zhejiang 311200, China; Xianghu Laboratory, Hangzhou 311231, China.

International journal of biological macromolecules
|April 6, 2024
PubMed
概括

通过引入二硫化键,工程师提高了酶的稳定性和活性,从而增强了2,3-butanediol脱酶 (2,3-BDH) 的功能. 这种策略重建了酶.

关键词:
2,3-布坦二醇脱酶的使用方法活动稳定性的权衡.双硫化物键是一种二硫化物键.酶工程是什么?酶工程是什么?模拟MDMD的模拟

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Metabolic Mapping: Quantitative Enzyme Cytochemistry and Histochemistry to Determine the Activity of Dehydrogenases in Cells and Tissues08:36

Metabolic Mapping: Quantitative Enzyme Cytochemistry and Histochemistry to Determine the Activity of Dehydrogenases in Cells and Tissues

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Stability of Conjugated Dienes

Introduction
A comparison of the enthalpies of hydrogenation of dienes reveals that conjugated dienes release less heat on hydrogenation, rendering them more stable than their nonconjugated analogs.
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Diels–Alder Reaction: Characteristics of Dienes

The Diels–Alder reaction brings together a diene and a dienophile to form a six-membered ring. Both components have unique characteristics that influence the rate of the reaction.
Characteristics of the diene
Conformation
The simplest example of a diene is 1,3-butadiene, an acyclic conjugated π system. At room temperature, the molecule exists as a mixture of s-cis and s-trans conformers by virtue of rotation around the carbon–carbon single bond. Although the s-trans isomer is...
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Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand binds to any of these subunits, it triggers a conformational change that affects the binding sites in the other subunits; this can change the affinity of the other sites for their respective ligands. The ability of the protein to change the shape of its binding site is attributed to the presence of a mix of flexible and stable segments in the...
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