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Annu Rev Plant Biol. 2017 Apr 28;68:29-60. doi: 10.1146/annurev-arplant-043015-111633. Epub 2017 Jan 11.

Biogenesis and Metabolic Maintenance of Rubisco.

Author information

1
Department of Cellular Biochemistry, Max Planck Institute of Biochemistry, 82152 Martinsried, Germany ; email: bracher@biochem.mpg.de , uhartl@biochem.mpg.de , mhartl@biochem.mpg.de.
2
Research School of Biology, Australian National University, Acton, Australian Capital Territory 2601, Australia; email: spencer.whitney@anu.edu.au.

Abstract

Ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) mediates the fixation of atmospheric CO2 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 CO2 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.

KEYWORDS:

Rubisco; Rubisco activase; assembly chaperone; chaperonin; metabolic repair

[Indexed for MEDLINE]

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