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 <10% among C₃ plant enzymes. Limited variation in S_C/O forces a strong positive correlation between the catalytic efficiencies (k_cat/K_M) for carboxylation and oxygenation, consistent with a model of Rubisco catalysis in which increasing the rate of addition of CO₂ to the enzyme-substrate complex requires an equal increase in the O₂ addition rate. Altogether, these data suggest that Rubisco evolution is tightly constrained by the physicochemical limits of CO₂/O₂ discrimination.

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