Tradeoff between enzyme and metabolite efficiency maintains metabolic homeostasis upon perturbations in enzyme capacity
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...
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| Main Authors: | , , , , , |
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| Format: | Article |
| Language: | English |
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Springer Nature
2010-04-01
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| Series: | Molecular Systems Biology |
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| Online Access: | https://doi.org/10.1038/msb.2010.11 |
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| _version_ | 1849225757106110464 |
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| author | Sarah‐Maria Fendt Joerg Martin Buescher Florian Rudroff Paola Picotti Nicola Zamboni Uwe Sauer |
| author_facet | Sarah‐Maria Fendt Joerg Martin Buescher Florian Rudroff Paola Picotti Nicola Zamboni Uwe Sauer |
| author_sort | Sarah‐Maria Fendt |
| collection | DOAJ |
| description | 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. |
| format | Article |
| id | doaj-art-4381c931a8a34df2be583626db6bcb0d |
| institution | Kabale University |
| issn | 1744-4292 |
| language | English |
| publishDate | 2010-04-01 |
| publisher | Springer Nature |
| record_format | Article |
| series | Molecular Systems Biology |
| spelling | doaj-art-4381c931a8a34df2be583626db6bcb0d2025-08-24T12:00:48ZengSpringer NatureMolecular Systems Biology1744-42922010-04-016111110.1038/msb.2010.11Tradeoff between enzyme and metabolite efficiency maintains metabolic homeostasis upon perturbations in enzyme capacitySarah‐Maria Fendt0Joerg Martin Buescher1Florian Rudroff2Paola Picotti3Nicola Zamboni4Uwe Sauer5Institute of Molecular Systems BiologyInstitute of Molecular Systems BiologyInstitute of Molecular Systems BiologyInstitute of Molecular Systems BiologyInstitute of Molecular Systems BiologyInstitute of Molecular Systems BiologyAbstract 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.https://doi.org/10.1038/msb.2010.11design principlemetabolic networkmetabolomicsproteomicstranscriptome |
| spellingShingle | Sarah‐Maria Fendt Joerg Martin Buescher Florian Rudroff Paola Picotti Nicola Zamboni Uwe Sauer Tradeoff between enzyme and metabolite efficiency maintains metabolic homeostasis upon perturbations in enzyme capacity Molecular Systems Biology design principle metabolic network metabolomics proteomics transcriptome |
| title | Tradeoff between enzyme and metabolite efficiency maintains metabolic homeostasis upon perturbations in enzyme capacity |
| title_full | Tradeoff between enzyme and metabolite efficiency maintains metabolic homeostasis upon perturbations in enzyme capacity |
| title_fullStr | Tradeoff between enzyme and metabolite efficiency maintains metabolic homeostasis upon perturbations in enzyme capacity |
| title_full_unstemmed | Tradeoff between enzyme and metabolite efficiency maintains metabolic homeostasis upon perturbations in enzyme capacity |
| title_short | Tradeoff between enzyme and metabolite efficiency maintains metabolic homeostasis upon perturbations in enzyme capacity |
| title_sort | tradeoff between enzyme and metabolite efficiency maintains metabolic homeostasis upon perturbations in enzyme capacity |
| topic | design principle metabolic network metabolomics proteomics transcriptome |
| url | https://doi.org/10.1038/msb.2010.11 |
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