Ribulose-1,5-bisphosphate carboxylase/oxygenase from thermophilic cyanobacterium Thermosynechococcus elongatus |
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Authors: | Beata Gubernator Rafal Bartoszewski Jaroslaw Kroliczewski Guenter Wildner Andrzej Szczepaniak |
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Institution: | (1) Department of Biotechnology, University of Wroclaw, Przybyszewskiego 63/77, Wroclaw, 51-148, Poland;(2) Department of Biology, Ruhr-University Bochum, Bochum, 44780, Germany;(3) Present address: Department of Biochemistry and Molecular Biophysics, University of Arizona, Tucson, AZ 85718, USA |
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Abstract: | Ribulose-1,5-bisphosphate carboxylase/oxygenase (rubisco) can be divided into two branches: the “red-like type” of marine
algae and the “green-like type” of cyanobacteria, green algae, and higher plants. We found that the “green-like type” rubisco
from the thermophilic cyanobacterium Thermosynechococcus elongatus has an almost 2-fold higher specificity factor compared with rubiscos of mesophilic cyanobacteria, reaching the values of
higher plants, and simultaneously revealing an improvement in enzyme thermostability. The difference in the activation energies
at the transition stages between the oxygenase and carboxylase reactions for Thermosynechococcus elongatus rubisco is very close to that of Galdieria partita and significantly higher than that of spinach. This is the first characterization of a “green-like type” rubisco from thermophilic
organism. |
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Keywords: | Rubisco Specificity factor Thermostability Thermophilic cyanobacteria |
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