Reversible photocontrol of oxidase activity by inserting a photosensitive domain into the oxidase
| Autor: | Yuhong Ren, Baoqi Zhang, Tongjing Sun, Jinping Lin |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2019 |
| Předmět: |
AsLOV2
Conformational change Photoinhibition lcsh:Biotechnology Biomedical Engineering lcsh:Chemical technology lcsh:Technology Cofactor Biological pathway lcsh:TP248.13-248.65 lcsh:TP1-1185 Enzyme activity Insertion chemistry.chemical_classification Oxidase test biology Renewable Energy Sustainability and the Environment lcsh:T Photocontrol Light intensity Metabolic pathway Enzyme chemistry Biophysics biology.protein Oxidase Food Science Biotechnology |
| Zdroj: | Bioresources and Bioprocessing, Vol 6, Iss 1, Pp 1-6 (2019) |
| ISSN: | 2197-4365 |
| Popis: | Background Photocontrol of protein activity has become a helpful strategy for regulating biological pathways. Herein, a method for the precise and reversible photocontrol of oxidase activity was developed by using the conformational change of the AsLOV2 domain. Results The AsLOV2 domain was inserted into the nonconserved sites exposed on the surface of the AdhP protein, and the alov9 fusion was successfully screened for subsequent optical experiments under the assumption that neither of these actions affected the original activity of AdhP protein. The activity of alov9 was noticeably inhibited when the fusion was exposed to 470 nm blue light and recovered within 30 min. As a result, we could precisely and reversibly photocontrol alov9 activity through the optimization of several parameters, including cofactor concentration, light intensity, and illumination time. Conclusions An efficient method was developed for the photoinhibition of enzymatic activity based on the insertion of the light-sensitive AsLOV2 domain, providing new ideas for photocontrolling metabolic pathways without carriers in the future. |
| Databáze: | OpenAIRE |
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