Enhancing the Catalytic Activity of <i>Thermococcus kodakarensis</i> RuBisCo via Computer-Aided Rational Design
H NMR results demonstrated that the Y168L-A361P mutation enhances the carboxylation rate to a much greater extent than does the oxygenation rate. Molecular-dynamics simulations revealed that Y168L and A361P─although neither contacts the substrate directly─augment binding of the carboxylation intermediate EI II through an extended interaction network that strengthens hydrogen bonds to the substrate carboxylate.
Authors
- Lishan Yao (ORCID: https://orcid.org/0000-0003-1797-922X)
- Jingfei Chen
- Sainan Li (ORCID: https://orcid.org/0000-0002-1880-6294)
- Jin Zhou (ORCID: https://orcid.org/0000-0002-1534-2279)
- Xiangfei Song (ORCID: https://orcid.org/0000-0002-1471-1175)
- Yefei Wang (ORCID: https://orcid.org/0000-0002-7228-7712)
Institutions
- Energy Institute (GB)
- Chinese Academy of Sciences (CN)
- Shandong Lianxing Energy Group (China) (CN)
- Qingdao Institute of Bioenergy and Bioprocess Technology (CN)
- University of Chinese Academy of Sciences (CN)
Publication Details
- Journal
- Journal of Agricultural and Food Chemistry
- Published
- 2026-04-27
- DOI
- https://doi.org/10.1021/acs.jafc.5c17734
- Primary Topic
- Microbial Metabolic Engineering and Bioproduction
- Type
- article
- Field-Weighted Citation Impact
- 0.00
Funders
- Shandong Energy Institute, Chinese Academy of Sciences
- National Natural Science Foundation of China
- Natural Science Foundation of Shandong Province
- Taishan Scholar Project of Shandong Province