Cargando…
Tradeoff between enzyme and metabolite efficiency maintains metabolic homeostasis upon perturbations in enzyme capacity
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 concentra...
Autores principales: | , , , , , |
---|---|
Formato: | Texto |
Lenguaje: | English |
Publicado: |
European Molecular Biology Organization
2010
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2872607/ https://www.ncbi.nlm.nih.gov/pubmed/20393576 http://dx.doi.org/10.1038/msb.2010.11 |
_version_ | 1782181238931456000 |
---|---|
author | Fendt, Sarah-Maria Buescher, Joerg Martin Rudroff, Florian Picotti, Paola Zamboni, Nicola Sauer, Uwe |
author_facet | Fendt, Sarah-Maria Buescher, Joerg Martin Rudroff, Florian Picotti, Paola Zamboni, Nicola Sauer, Uwe |
author_sort | Fendt, Sarah-Maria |
collection | PubMed |
description | 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 | Text |
id | pubmed-2872607 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2010 |
publisher | European Molecular Biology Organization |
record_format | MEDLINE/PubMed |
spelling | pubmed-28726072010-05-19 Tradeoff between enzyme and metabolite efficiency maintains metabolic homeostasis upon perturbations in enzyme capacity Fendt, Sarah-Maria Buescher, Joerg Martin Rudroff, Florian Picotti, Paola Zamboni, Nicola Sauer, Uwe Mol Syst Biol Article 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. European Molecular Biology Organization 2010-04-13 /pmc/articles/PMC2872607/ /pubmed/20393576 http://dx.doi.org/10.1038/msb.2010.11 Text en Copyright © 2010, EMBO and Macmillan Publishers Limited https://creativecommons.org/licenses/by-nc-sa/3.0/This is an open-access article distributed under the terms of the Creative Commons Attribution Licence, which permits distribution and reproduction in any medium, provided the original author and source are credited. Creation of derivative works is permitted but the resulting work may be distributed only under the same or similar licence to this one. This licence does not permit commercial exploitation without specific permission. |
spellingShingle | Article Fendt, Sarah-Maria Buescher, Joerg Martin Rudroff, Florian Picotti, Paola Zamboni, Nicola Sauer, Uwe Tradeoff between enzyme and metabolite efficiency maintains metabolic homeostasis upon perturbations in enzyme capacity |
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 | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2872607/ https://www.ncbi.nlm.nih.gov/pubmed/20393576 http://dx.doi.org/10.1038/msb.2010.11 |
work_keys_str_mv | AT fendtsarahmaria tradeoffbetweenenzymeandmetaboliteefficiencymaintainsmetabolichomeostasisuponperturbationsinenzymecapacity AT buescherjoergmartin tradeoffbetweenenzymeandmetaboliteefficiencymaintainsmetabolichomeostasisuponperturbationsinenzymecapacity AT rudroffflorian tradeoffbetweenenzymeandmetaboliteefficiencymaintainsmetabolichomeostasisuponperturbationsinenzymecapacity AT picottipaola tradeoffbetweenenzymeandmetaboliteefficiencymaintainsmetabolichomeostasisuponperturbationsinenzymecapacity AT zamboninicola tradeoffbetweenenzymeandmetaboliteefficiencymaintainsmetabolichomeostasisuponperturbationsinenzymecapacity AT saueruwe tradeoffbetweenenzymeandmetaboliteefficiencymaintainsmetabolichomeostasisuponperturbationsinenzymecapacity |