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… 
Structure and function of Rubisco.
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This review discusses Rubisco function in the context of structural variations at all levels--amino acid sequence, fold, tertiary and quaternary structure--with an evolutionary perspective and an emphasis on the structural features of the enzyme that may determine its function as a carboxylase.
Catalysis and regulation in Rubisco.
  • I. Andersson
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    Journal of experimental botany
  • 2008
Ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) catalyses the incorporation of inorganic CO(2) into the organic molecules of life. Rubisco is extremely inefficient as a catalyst and its
Structural framework for catalysis and regulation in ribulose-1,5-bisphosphate carboxylase/oxygenase.
TLDR
A critical review of the field is given and recent results from structural studies of Rubisco are summarized.
Rubisco regulation: a role for inhibitors.
TLDR
The regulation ofRubisco activity in higher plants is reviewed here, including the role of Rubisco activase, tight binding inhibitors, and the impact of abiotic stress upon them.
Structural dynamics of ribulose-1,5-bisphosphate carboxylase/oxygenase
TLDR
The migration of the gaseous substrates, CO2 and O2 in and around Rubisco, was investigated using molecular dynamics simulations and indicated that at equal concentrations of the gas, Rubisco has a preference for binding CO2 over O2.
Structure of green-type Rubisco activase from tobacco
TLDR
The 2.95-Å crystal structure of Nicotiana tabacum Rubisco activase (Rca), the enzyme that facilitates the removal of inhibitory sugar phosphates, is reported.
Isolation of ribulose-1,5-bisphosphate carboxylase/oxygenase from leaves.
TLDR
This chapter describes procedures for rapid and efficient purification of Rubisco from leaves of several species.
Rubisco activity and regulation as targets for crop improvement.
TLDR
As the rate-limiting step in carbon assimilation, even modest improvements in the overall performance of Rubisco pose a viable pathway for obtaining significant gains in plant yield, particularly under stressful environmental conditions.
The Hidden Face of Rubisco.
TLDR
These RbcS belong to a cluster named T (for trichome), phylogenetically distant from cluster M, which gathers well-characterized RBCS expressed in mesophyll or bundle-sheath tissues, indicating an ancient origin.
In silico Analysis for Enhancing the Rubisco Activity among the C3 Plants of Poaceae Family
  • Boopathi Subramani, K. Hwa
  • Chemistry
    2010 2nd International Conference on Information Technology Convergence and Services
  • 2010
Ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) is the key enzyme involved in CO_2 fixation. It is an important enzyme for biomass production, especially for alternate energy production.
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References

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The mechanism of Rubisco activase: Insights from studies of the properties and structure of the enzyme
TLDR
This review discusses the need for and function of Rubisco activase and summarizes information about the properties and structure of Rubisol activase, evaluated in the context of the mechanism of Rubiso activase.
Genetic Engineering of Rubisco
TLDR
Several regions outside the active site have now been identified that control catalytic efficiency and can be used to investigate the nucleus- and chloroplast-encoded Rubisco subunits, which likely serve as the best models for ultimately engineering the Rubisco of crop plants.
Questions about the complexity of chloroplast ribulose-1,5-bisphosphate carboxylase/oxygenase
TLDR
The complexity of chloroplast Rubisco in land plants cannot be completely addressed with the existing model organisms, and attempts to engineer or discover a better Rubisco may be futile if one cannot transfer the better enzyme to a compatible host.
Microbial ribulose 1,5-bisphosphate carboxylase/oxygenase: A different perspective
TLDR
This review considers the major issues of Rubisco biochemistry and regulation in photosynthetic microoganisms including proteob bacteria, cyanobacteria, marine nongreen algae, as well as other interesting prokaryotic and eukaryotic microbial systems recently shown to possess this enzyme.
Directed Mutagenesis of Chloroplast Ribulose-1,5-bisphosphate Carboxylase/Oxygenase
TLDR
Interactions between loop 6 and other structural regions are likely to be responsible for both holoenzyme stability and catalytic efficiency in higher plant Rubisco enzymes.
Rubisco: Assembly and Mechanism
Ribulose-bisphosphate carboxylase/oxygenase (Rubisco, E.C. 4.1.1.39) is unique to photosynthetic metabolism. Two intensively studied aspects of Rubisco physiology are covered in this chapter, its
The crystal structure of rubisco from Alcaligenes eutrophus reveals a novel central eight-stranded beta-barrel formed by beta-strands from four subunits.
TLDR
The present structure is the first which has been solved for a red-like rubisco and is likely to represent a fold which is common for this group, and the new quaternary structure in the oligomer of the present structure are likely to contribute even more to this stabilization of the assembled rubisco protein.
Species variation in the specificity of ribulose biphosphate carboxylase/oxygenase
The balance between photosynthesis and photorespiration in many species, including most crop plants, is determined by the kinetic properties of ribulose-l,5-bisphosphate (RuBP)
Mechanism of light regulation of Rubisco: a specific role for the larger Rubisco activase isoform involving reductive activation by thioredoxin-f.
  • N. Zhang, A. Portis
  • Biology, Medicine
    Proceedings of the National Academy of Sciences of the United States of America
  • 1999
TLDR
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.
The regulation of Rubisco by Rubisco activase
The activity of Rubisco depends on the conversion of the inactive form (E) to the active form (ECM); the binding of the inhibitors CA1P and RuBP to ECM and E, respectively; and the catalytic
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