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Revisiting Trade-offs between Rubisco Kinetic Parameter

Authors :
Yinon M. Bar-On
Luke M. Oltrogge
Uri Moran
Noam Prywes
Ron Milo
David F. Savage
Avi I. Flamholz
Dan Davidi
Rui Alves
Source :
Repositorio Abierto de la UdL, Universitad de Lleida, Biochemistry
Publication Year :
2019
Publisher :
American Chemical Society, 2019.

Abstract

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, SC/O, and maximum carboxylation rate, kcat,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 kcat,C and SC/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 kcat,C values are between 1 and 10 s-1, and no measured kcat,C exceeds 15 s-1. Similarly, SC/O varies by only 30% among Form I Rubiscos and

Details

Database :
OpenAIRE
Journal :
Repositorio Abierto de la UdL, Universitad de Lleida, Biochemistry
Accession number :
edsair.doi.dedup.....dcbf585f9a1f078d12370742e630d96b