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...

Descripción completa

Guardado en:

Detalles Bibliográficos
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/0e3306f0e85b4afeb0e9973df3446271
Etiquetas:	Agregar Etiqueta Sin Etiquetas, Sea el primero en etiquetar este registro!

id	oai:doaj.org-article:0e3306f0e85b4afeb0e9973df3446271
record_format	dspace
spelling	oai:doaj.org-article:0e3306f0e85b4afeb0e9973df34462712021-11-04T05:34:04ZOn the optimality of the enzyme–substrate relationship in bacteria1544-91731545-7885https://doaj.org/article/0e3306f0e85b4afeb0e9973df34462712021-10-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC8547704/?tool=EBIhttps://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. This study shows that in E. coli, the cellular mass of each metabolite approximately equals the combined mass of the free enzymes waiting to consume it; this simple relationship arises from the optimal utilization of cellular dry mass, and quantitatively describes available experimental data.Hugo DouradoMatteo MoriTerence HwaMartin J. LercherPublic Library of Science (PLoS)articleBiology (General)QH301-705.5ENPLoS Biology, Vol 19, Iss 10 (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. This study shows that in E. coli, the cellular mass of each metabolite approximately equals the combined mass of the free enzymes waiting to consume it; this simple relationship arises from the optimal utilization of cellular dry mass, and quantitatively describes available experimental data.
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/0e3306f0e85b4afeb0e9973df3446271
work_keys_str_mv	AT hugodourado ontheoptimalityoftheenzymesubstraterelationshipinbacteria AT matteomori ontheoptimalityoftheenzymesubstraterelationshipinbacteria AT terencehwa ontheoptimalityoftheenzymesubstraterelationshipinbacteria AT martinjlercher ontheoptimalityoftheenzymesubstraterelationshipinbacteria
_version_	1718445192141340672

On the optimality of the enzyme–substrate relationship in bacteria

Ejemplares similares