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Systematic exploration of bacterial form I rubisco maximal carboxylation rates

de Pins, B.; Greenspoon, L.; Bar-On, Y. M.; Shamshoum, M.; Ben-Nissan, R.; Milshtein, E.; Davidi, D.; Sharon, I.; Mueller-Cajar, O.; Noor, E.; Milo, R.

2023-10-29 systems biology
10.1101/2023.07.27.550689 bioRxiv
Show abstract

Autotrophy is the basis for complex life on Earth. Central to this process is rubisco - the enzyme that catalyzes almost all carbon fixation on the planet. Yet, with only a small fraction of rubisco diversity kinetically characterized so far, the underlying biological factors driving the evolution of fast rubiscos in nature remain unclear. We conducted a high-throughput kinetic characterization of over 100 bacterial form I rubiscos, the most ubiquitous group of rubisco sequences in nature, to uncover the determinants of rubiscos carboxylation velocity. We show that the presence of a carboxysome CO2 concentrating mechanism correlates with faster rubiscos with a median 5-fold higher rate. In contrast to prior studies, we find that rubiscos originating from -cyanobacteria exhibit the highest carboxylation rates among form I enzymes ({approx}10 s-1 median versus <7 s-1 in other groups). Our study systematically reveals biological and environmental properties associated with kinetic variation across rubiscos from nature.

Published in The EMBO Journal (predicted rank #20) · training set

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