ArticleMolecular systems biology2010
Tradeoff between enzyme and metabolite efficiency maintains metabolic homeostasis upon perturbations in enzyme capacity.
Article in Molecular systems biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 84 papers.
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Who cites it
84 citing papers in PubMed, 170 citations in OpenAlex.
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- Resource allocation accounts for the large variability of rate-yield phenotypes across bacterial strains.eLife · 2023Article
- Metabolomics: Going Deeper, Going Broader, Going Further.Methods in molecular biology (Clifton, N.J.) · 2023Review
- Lactate mediated metabolic crosstalk between cancer and immune cells and its therapeutic implications.Frontiers in oncology · 2023Review
- A functional analysis of 180 cancer cell lines reveals conserved intrinsic metabolic programs.Molecular systems biology · 2022Article
- Structural Thermokinetic Modelling.Metabolites · 2022Article
- Two major metabolic factors for an efficient NADP-malic enzyme type C4 photosynthesis.Plant physiology · 2022Article
- On the optimality of the enzyme-substrate relationship in bacteria.PLoS biology · 2021Article
- Extensive regulation of enzyme activity by phosphorylation in Escherichia coli.Nature communications · 2021Article
24 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
What is the relationship between enzymes and metabolites, the two major constituents of metabolic networks? We propose three alternative relationships between enzyme capacity and metabolite concentration alterations based on a Michaelis-Menten kinetic; that is enzyme capacities, metabolite concentrations, or both could limit the metabolic reaction rates. These relationships imply different correlations between changes in enzyme capacity and metabolite concentration, which we tested by quantifying metabolite, transcript, and enzyme abundances upon local (single-enzyme modulation) and global (GCR2 transcription factor mutant) perturbations in Saccharomyces cerevisiae. Our results reveal an inverse relationship between fold-changes in substrate metabolites and their catalyzing enzymes. These data provide evidence for the hypothesis that reaction rates are jointly limited by enzyme capacity and metabolite concentration. Hence, alteration in one network constituent can be efficiently buffered by converse alterations in the other constituent, implying a passive mechanism to maintain metabolic homeostasis upon perturbations in enzyme capacity.
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