On the optimality of the enzyme-substrate relationship in bacteria.

Much recent progress has been made to understand the impact of proteome allocation on bacterial growth; much less is known about the relationship between the abundances of the enzymes and their substrates, which jointly determine metabolic fluxes. Here, we report a correlation between the concentrat...

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Autores principales:	Hugo Dourado, Matteo Mori, Terence Hwa, Martin J Lercher
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2021
Materias:	Biology (General) QH301-705.5
Acceso en línea:	https://doaj.org/article/a0a0c6ecac2e4803b038943df6157b0b
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spelling	oai:doaj.org-article:a0a0c6ecac2e4803b038943df6157b0b2021-12-02T19:54:26ZOn the optimality of the enzyme-substrate relationship in bacteria.1544-91731545-788510.1371/journal.pbio.3001416https://doaj.org/article/a0a0c6ecac2e4803b038943df6157b0b2021-10-01T00:00:00Zhttps://doi.org/10.1371/journal.pbio.3001416https://doaj.org/toc/1544-9173https://doaj.org/toc/1545-7885Much recent progress has been made to understand the impact of proteome allocation on bacterial growth; much less is known about the relationship between the abundances of the enzymes and their substrates, which jointly determine metabolic fluxes. Here, we report a correlation between the concentrations of enzymes and their substrates in Escherichia coli. We suggest this relationship to be a consequence of optimal resource allocation, subject to an overall constraint on the biomass density: For a cellular reaction network composed of effectively irreversible reactions, maximal reaction flux is achieved when the dry mass allocated to each substrate is equal to the dry mass of the unsaturated (or "free") enzymes waiting to consume it. Calculations based on this optimality principle successfully predict the quantitative relationship between the observed enzyme and metabolite abundances, parameterized only by molecular masses and enzyme-substrate dissociation constants (Km). The corresponding organizing principle provides a fundamental rationale for cellular investment into different types of molecules, which may aid in the design of more efficient synthetic cellular systems.Hugo DouradoMatteo MoriTerence HwaMartin J LercherPublic Library of Science (PLoS)articleBiology (General)QH301-705.5ENPLoS Biology, Vol 19, Iss 10, p e3001416 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Biology (General) QH301-705.5
spellingShingle	Biology (General) QH301-705.5 Hugo Dourado Matteo Mori Terence Hwa Martin J Lercher On the optimality of the enzyme-substrate relationship in bacteria.
description	Much recent progress has been made to understand the impact of proteome allocation on bacterial growth; much less is known about the relationship between the abundances of the enzymes and their substrates, which jointly determine metabolic fluxes. Here, we report a correlation between the concentrations of enzymes and their substrates in Escherichia coli. We suggest this relationship to be a consequence of optimal resource allocation, subject to an overall constraint on the biomass density: For a cellular reaction network composed of effectively irreversible reactions, maximal reaction flux is achieved when the dry mass allocated to each substrate is equal to the dry mass of the unsaturated (or "free") enzymes waiting to consume it. Calculations based on this optimality principle successfully predict the quantitative relationship between the observed enzyme and metabolite abundances, parameterized only by molecular masses and enzyme-substrate dissociation constants (Km). The corresponding organizing principle provides a fundamental rationale for cellular investment into different types of molecules, which may aid in the design of more efficient synthetic cellular systems.
format	article
author	Hugo Dourado Matteo Mori Terence Hwa Martin J Lercher
author_facet	Hugo Dourado Matteo Mori Terence Hwa Martin J Lercher
author_sort	Hugo Dourado
title	On the optimality of the enzyme-substrate relationship in bacteria.
title_short	On the optimality of the enzyme-substrate relationship in bacteria.
title_full	On the optimality of the enzyme-substrate relationship in bacteria.
title_fullStr	On the optimality of the enzyme-substrate relationship in bacteria.
title_full_unstemmed	On the optimality of the enzyme-substrate relationship in bacteria.
title_sort	on the optimality of the enzyme-substrate relationship in bacteria.
publisher	Public Library of Science (PLoS)
publishDate	2021
url	https://doaj.org/article/a0a0c6ecac2e4803b038943df6157b0b
work_keys_str_mv	AT hugodourado ontheoptimalityoftheenzymesubstraterelationshipinbacteria AT matteomori ontheoptimalityoftheenzymesubstraterelationshipinbacteria AT terencehwa ontheoptimalityoftheenzymesubstraterelationshipinbacteria AT martinjlercher ontheoptimalityoftheenzymesubstraterelationshipinbacteria
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On the optimality of the enzyme-substrate relationship in bacteria.

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