Revisiting Trade-offs between Rubisco Kinetic Parameters

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...

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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
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cited_by cdi_FETCH-LOGICAL-a538t-8af06a6eca6784f45c5019a3f55b02fcb0f2f118d30515f4193da9411b52c6ee3
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container_issue 31
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container_title Biochemistry (Easton)
container_volume 58
creator Flamholz, Avi I
Prywes, Noam
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Savage, David
Milo, Ron
description 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
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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 &lt;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. 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title Revisiting Trade-offs between Rubisco Kinetic Parameters
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