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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.
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.
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 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.