Revisiting Trade-offs between Rubisco Kinetic Parameters

• Published in: Biochemistry (Easton) 2019-08, Vol.58 (31), p.3365-3376
• Main Authors: Flamholz, Avi I, Prywes, Noam, Moran, Uri, Davidi, Dan, Bar-On, Yinon M, Oltrogge, Luke M, Alves, Rui, Savage, David, Milo, Ron
• Format: Article
• Language: English
• ISSN: 0006-2960; 1520-4995
• DOI: 10.1021/acs.biochem.9b00237

Rubisco is the primary carboxylase of the Calvin cycle, the most abundant enzyme in the biosphere, and one of the best-characterized enzymes. On the basis of correlations between Rubisco kinetic parameters, it is widely posited that constraints embedded in the catalytic mechanism enforce trade-offs between CO2 specificity, S C/O, and maximum carboxylation rate, k cat,C. However, the reasoning that established this view was based on data from ≈20 organisms. Here, we re-examine models of trade-offs in Rubisco catalysis using a data set from ≈300 organisms. Correlations between kinetic parameters are substantially attenuated in this larger data set, with the inverse relationship between k cat,C and S C/O being a key example. Nonetheless, measured kinetic parameters display extremely limited variation, consistent with a view of Rubisco as a highly constrained enzyme. More than 95% of k cat,C values are between 1 and 10 s–1, and no measured k cat,C exceeds 15 s–1. Similarly, S C/O varies by only 30% among Form I Rubiscos and