Engineering Rubisco to enhance CO2 utilization
Ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) is a pivotal enzyme that mediates the fixation of CO2. As the most abundant protein on earth, Rubisco has a significant impact on global carbon, water, and nitrogen cycles. However, the significantly low carboxylation activity and competing o...
| Main Authors: | , , , |
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| Format: | Article |
| Language: | English |
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KeAi Communications Co., Ltd.
2024-03-01
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| Series: | Synthetic and Systems Biotechnology |
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| Online Access: | http://www.sciencedirect.com/science/article/pii/S2405805X23001138 |
| _version_ | 1797272404376944640 |
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| author | Lei Zhao Zhen Cai Yin Li Yanping Zhang |
| author_facet | Lei Zhao Zhen Cai Yin Li Yanping Zhang |
| author_sort | Lei Zhao |
| collection | DOAJ |
| description | Ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) is a pivotal enzyme that mediates the fixation of CO2. As the most abundant protein on earth, Rubisco has a significant impact on global carbon, water, and nitrogen cycles. However, the significantly low carboxylation activity and competing oxygenase activity of Rubisco greatly impede high carbon fixation efficiency. This review first summarizes the current efforts in directly or indirectly modifying plant Rubisco, which has been challenging due to its high conservation and limitations in chloroplast transformation techniques. However, recent advancements in understanding Rubisco biogenesis with the assistance of chaperones have enabled successful heterologous expression of all Rubisco forms, including plant Rubisco, in microorganisms. This breakthrough facilitates the acquisition and evaluation of modified proteins, streamlining the measurement of their activity. Moreover, the establishment of a screening system in E. coli opens up possibilities for obtaining high-performance mutant enzymes through directed evolution. Finally, this review emphasizes the utilization of Rubisco in microorganisms, not only expanding their carbon-fixing capabilities but also holding significant potential for enhancing biotransformation processes. |
| first_indexed | 2024-03-07T14:28:51Z |
| format | Article |
| id | doaj.art-316ffc3a878344b5ad6e9a1f93dfb5f9 |
| institution | Directory Open Access Journal |
| issn | 2405-805X |
| language | English |
| last_indexed | 2024-03-07T14:28:51Z |
| publishDate | 2024-03-01 |
| publisher | KeAi Communications Co., Ltd. |
| record_format | Article |
| series | Synthetic and Systems Biotechnology |
| spelling | doaj.art-316ffc3a878344b5ad6e9a1f93dfb5f92024-03-06T05:27:57ZengKeAi Communications Co., Ltd.Synthetic and Systems Biotechnology2405-805X2024-03-01915568Engineering Rubisco to enhance CO2 utilizationLei Zhao0Zhen Cai1Yin Li2Yanping Zhang3CAS Key Laboratory of Microbial Physiological and Metabolic Engineering, State Key Laboratory of Microbial Resources, Institute of Microbiology, Chinese Academy of Sciences, Beijing, 100101, China; University of Chinese Academy of Sciences, Beijing, 100049, ChinaCAS Key Laboratory of Microbial Physiological and Metabolic Engineering, State Key Laboratory of Microbial Resources, Institute of Microbiology, Chinese Academy of Sciences, Beijing, 100101, ChinaCAS Key Laboratory of Microbial Physiological and Metabolic Engineering, State Key Laboratory of Microbial Resources, Institute of Microbiology, Chinese Academy of Sciences, Beijing, 100101, ChinaCAS Key Laboratory of Microbial Physiological and Metabolic Engineering, State Key Laboratory of Microbial Resources, Institute of Microbiology, Chinese Academy of Sciences, Beijing, 100101, China; Corresponding author.Ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) is a pivotal enzyme that mediates the fixation of CO2. As the most abundant protein on earth, Rubisco has a significant impact on global carbon, water, and nitrogen cycles. However, the significantly low carboxylation activity and competing oxygenase activity of Rubisco greatly impede high carbon fixation efficiency. This review first summarizes the current efforts in directly or indirectly modifying plant Rubisco, which has been challenging due to its high conservation and limitations in chloroplast transformation techniques. However, recent advancements in understanding Rubisco biogenesis with the assistance of chaperones have enabled successful heterologous expression of all Rubisco forms, including plant Rubisco, in microorganisms. This breakthrough facilitates the acquisition and evaluation of modified proteins, streamlining the measurement of their activity. Moreover, the establishment of a screening system in E. coli opens up possibilities for obtaining high-performance mutant enzymes through directed evolution. Finally, this review emphasizes the utilization of Rubisco in microorganisms, not only expanding their carbon-fixing capabilities but also holding significant potential for enhancing biotransformation processes.http://www.sciencedirect.com/science/article/pii/S2405805X23001138RubiscoPlant CO2 fixationMicrobialCarbon fixation pathwaySynthetic biologyEnzyme engineering |
| spellingShingle | Lei Zhao Zhen Cai Yin Li Yanping Zhang Engineering Rubisco to enhance CO2 utilization Synthetic and Systems Biotechnology Rubisco Plant CO2 fixation Microbial Carbon fixation pathway Synthetic biology Enzyme engineering |
| title | Engineering Rubisco to enhance CO2 utilization |
| title_full | Engineering Rubisco to enhance CO2 utilization |
| title_fullStr | Engineering Rubisco to enhance CO2 utilization |
| title_full_unstemmed | Engineering Rubisco to enhance CO2 utilization |
| title_short | Engineering Rubisco to enhance CO2 utilization |
| title_sort | engineering rubisco to enhance co2 utilization |
| topic | Rubisco Plant CO2 fixation Microbial Carbon fixation pathway Synthetic biology Enzyme engineering |
| url | http://www.sciencedirect.com/science/article/pii/S2405805X23001138 |
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