Add time:09/24/2019         Source:sciencedirect.com

Publisher SummaryRibulose-l,5-bisphosphate carboxylase/oxygenase (Rubisco) is the most abundant enzyme on the planet and plays one of the most important roles in the ecosystem. It catalyzes the covalent addition of carbon dioxide to ribulose-l,5-bisphosphate, producing two molecules of 3-phosphoglycerate (3PGA). The function and the abundance of the enzyme provide a major link between inorganic and organic carbon in our biosphere. The fixed carbon is then converted into sugars and other cell material, which will ultimately be utilized as the carbon and energy source of virtually all heterotrophic organisms. The significance of Rubisco has attracted scientists for decades, consequently leading to an extraordinary accumulation of knowledge on the enzyme. Rubisco is found predominantly in higher plants, algae, cyanobacteria, and photosynthetic bacteria. In these organisms, Rubisco has been found to catalyze a second reaction in the presence of oxygen; ribulose-l,5-bisphosphate and oxygen are converted to one molecule of 3PGA and one molecule of 2-phosphoglycolate (2PG). 2PG is metabolized oxidatively in the glycolate pathway, thereby leading to a significant decrease in net efficiency of photosynthesis. A gene similar to Rubisco was detected on the chromosome of the hyperthermophilic archaeon Thermococcus kodakaraensis KOD1. The Rubisco gene of T. kodakaraensis KOD1 (Tk-rbcl) has a length of 1332 bp, encoding a protein (Tk-Rubisco) of 444 amino acid residues.

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