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Annual Review of Plant Biology

Volume 68, 2017

Biogenesis and Metabolic Maintenance of Rubisco*

Abstract

Ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) mediates the fixation of atmospheric CO in photosynthesis by catalyzing the carboxylation of the 5-carbon sugar ribulose-1,5-bisphosphate (RuBP). Rubisco is a remarkably inefficient enzyme, fixing only 2–10 CO molecules per second. Efforts to increase crop yields by bioengineering Rubisco remain unsuccessful, owing in part to the complex cellular machinery required for Rubisco biogenesis and metabolic maintenance. The large subunit of Rubisco requires the chaperonin system for folding, and recent studies have shown that assembly of hexadecameric Rubisco is mediated by specific assembly chaperones. Moreover, Rubisco function can be inhibited by a range of sugar-phosphate ligands, including RuBP. Metabolic repair depends on remodeling of Rubisco by the ATP-dependent Rubisco activase and hydrolysis of inhibitory sugar phosphates by specific phosphatases. Here, we review our present understanding of the structure and function of these auxiliary factors and their utilization in efforts to engineer more catalytically efficient Rubisco enzymes.

Keyword(s): assembly chaperone, chaperonin, metabolic repair, Rubisco, Rubisco activase
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2017-04-28
2024-04-19
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Biogenesis and Metabolic Maintenance of Rubisco*
Annual Review of Plant Biology 68, 29 (2017); https://doi.org/10.1146/annurev-arplant-043015-111633
/content/journals/10.1146/annurev-arplant-043015-111633
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