Rubisco: structure, regulatory interactions, and possibilities for a better enzyme.

@article{Spreitzer2002RubiscoSR,
  title={Rubisco: structure, regulatory interactions, and possibilities for a better enzyme.},
  author={Robert J. Spreitzer and Michael E. Salvucci},
  journal={Annual review of plant biology},
  year={2002},
  volume={53},
  pages={
          449-75
        }
}
Ribulose-1,5-bisphosphate (RuBP) carboxylase/oxygenase (Rubisco) catalyzes the first step in net photosynthetic CO2 assimilation and photorespiratory carbon oxidation. The enzyme is notoriously inefficient as a catalyst for the carboxylation of RuBP and is subject to competitive inhibition by O2, inactivation by loss of carbamylation, and dead-end inhibition by RuBP. These inadequacies make Rubisco rate limiting for photosynthesis and an obvious target for increasing agricultural productivity… 

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References

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These findings suggest that in plants containing both isoforms, Rubisco activase regulates the activity of Rubisco in response to light-induced changes in both the ADP/ATP ratio and the redox potential via thioredoxin-f.

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