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Ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) is a copper-containing enzyme involved in the first major step of carbon fixation. It is the central enzyme of photosynthesis and probably the most abundant protein on Earth.
The CO2-fixing enzyme Rubisco from Paniceae grasses shows extensive variation in kinetic responses. Amino acid substitutions in the large subunit could be a route to tailoring the properties of crop Rubiscos to suit future climates.
Rubisco catalyses the conversion of atmospheric CO2 into organic compounds in photosynthesis, and therefore plays a pivotal role in plant metabolism. The complex cellular machineries invovled in the assembly and metabolic repair of this most abundant enzyme are explored in this Review.
Rubisco catalyses the conversion of atmospheric CO2 to organic compounds in photosynthetic organisms. Biochemical and structural analyses suggest that a selective sugar phosphatase found in plants and algae degrades a potent Rubisco inhibitor.
The CO2-fixing enzyme rubisco requires motor proteins known as rubisco activases to remove inhibitors bound to its active site. Here the authors describe a new class of rubisco activase present in chemoautotrophic bacteria that belongs to the MoxR family of AAA+ ATPases.
The plant enzyme Rubisco is the main enzyme converting atmospheric carbon dioxide into biological compounds, however, this enzymatic process is inefficient in vascular plants; this study demonstrates that tobacco plants can be engineered to fix carbon with a faster cyanobacterial Rubisco, thus potentially improving plant photosynthesis.
Photosynthesis in C3 plants is limited by the kinetics of the CO2-fixing enzyme Rubisco. Natural variation in Rubisco can be exploited to provide new avenues for adapting photosynthetic performance to a changing climate while reducing the environmental footprint of agriculture.
Rubisco catalyses the first step in photosynthetic carbon fixation, but it can be easily poisoned by side-products of its activity. Structural and functional analyses of a protein conserved across plants, algae and bacteria shows how one such blockage is both removed and recycled.