Nanoreactor is a key enzyme in CO2-fixation cycle.
Carbon dioxide (CO2) is a potent greenhouse gas, and an accessible carbon source that could be converted into high-value products such as biofuels and renewable chemicals. Tobi Erb, Director at the Max Planck Institute for Terrestrial Microbiology in Marburg, Germany and his team focus on identifying novel CO2 converting enzymes and understanding the metabolic pathways involved. In collaboration with JGI, they apply their knowledge to build completely novel CO2-fixation processes that are more efficient than those of plants using synthetic biology.
Atomic structure of Propionyl-CoA synthase and its three parts. (Courtesy of MPI)
Though the JGI’s Community Science Program (CSP) and working with Yasuo Yoshikuni, head of JGI’s DNA Synthesis Science Program, Erb and his colleagues have now reported the structure and function of propionyl-CoA synthase (PCS). PCS is a key enzyme in a CO2-fixation bi-cycle, and one of the smallest multireaction chambers known to exist. The work was recently reported in Nature Chemical Biology.
“It is amazing how nature built this small enzyme reactor that is so sophistically regulated,” said Erb in a MPI Marburg news release. “We hope to exploit this building principle in our efforts to create novel CO2 fixation pathways.”
Proposals for the JGI’s Community Science Program DNA Synthesis Call are reviewed twice a year. Submit by January 15, 2019 to be considered for the next review session.
Publication:
- Bernhardsgrütter I et al. The multicatalytic compartment of propionyl-CoA synthase sequesters a toxic metabolite. Nature Chemical Biology. 2018 Oct 29. doi: https://dx.doi.org/10.1038/s41589-018-0153-x
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