Understanding Robustness in Glyoxylate Bypass Regulation
Author Information
Author(s): Guy Shinar, Joshua D. Rabinowitz, Uri Alon
Primary Institution: Weizmann Institute of Science
Hypothesis
What mechanisms explain the robustness of isocitrate dehydrogenase activity in E. coli's glyoxylate bypass regulation?
Conclusion
The study proposes a new mechanism for the robustness of isocitrate dehydrogenase activity that relies on the formation of a ternary complex involving a bifunctional enzyme.
Supporting Evidence
- The IDH system regulates carbon flux in E. coli, which is crucial for growth on two-carbon compounds.
- Robustness was experimentally tested, showing less than 20% change in active IDH levels despite a 15-fold variation in total IDH concentration.
- The proposed mechanism suggests that a ternary complex formation is key to maintaining IDH activity.
Takeaway
This study looks at how a specific enzyme system in bacteria can keep working well even when the amount of proteins changes a lot.
Methodology
The study uses mathematical modeling and numerical simulations to analyze the robustness of the IDH system.
Limitations
The proposed model relies on specific biochemical features that may not apply universally to all systems.
Digital Object Identifier (DOI)
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