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/lp/annual-reviews/biogenesis-and-metabolic-maintenance-of-rubisco-SpB60vt9zU
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- Publisher
- Annual Reviews
- Copyright
- Copyright 2017 Annual Reviews. All rights reserved
- ISSN
- 1040-2519
- DOI
- 10.1146/annurev-arplant-043015-111633
- pmid
- 28125284
- Publisher site
- See Article on Publisher Site
Abstract
Ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) mediates the fixation of atmospheric CO 2 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 2 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.
Journal
Annual Review of Plant Physiology and Plant Molecular Biology – Annual Reviews
Published: Apr 28, 2017