The moderately efficient enzyme: evolutionary and physicochemical trends shaping enzyme parameters.
By A. Bar‐Even, Elad Noor, Y. Savir, Wolfram Liebermeister, D. Davidi, Dan S. Tawfik, Ron Milo. Biochemistry, 2011
982 citations recorded by the source corpus.
Subfields: Molecular Biology
View Paper: https://www.semanticscholar.org/paper/e2cfab6abfc9a91a9d9f8e4b9afa2834f92a53d8
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In Molecular Biology
- D. Moorhead
- R. Sinsabaugh
- B. Hill
- A. Bar‐Even
- Jose M. Sanchez-Ruiz
- Hector Garcia-Seisdedos
- Beatriz Ibarra-Molero
- Jens Nielsen
Citations in the corpus
- Probing the Mutational Interplay between Primary and Promiscuous Protein Functions: A Computational-Experimental Approach (2012, background): “Interestingly, a very recent analysis of the catalytic parameters for several thousand enzymes [57] indicates that Figure 10.”
- Extracellular enzyme kinetics scale with resource availability (2014, background): “Consequently, the two parameters are only weakly correlated (Bar-Even et al. 2011).”
- Improving the phenotype predictions of a yeast genome‐scale metabolic model by incorporating enzymatic constraints (2017, methodology): “This is in agreement with previous observations (Bar-Even et al, 2011) that identified central carbon metabolism enzymes as the most efficient in metabolism, most likely due to evolutionary pressure on this part of metabolism to operate with high fluxes.”
- Pathway Thermodynamics Highlights Kinetic Obstacles in Central Metabolism (2014, background): “Thus, the high turnover number of malate dehydrogenase (well above 1000 s(21) [31]) might have evolved to compensate for its low driving force.”