The role of dynamic enzyme assemblies and substrate channelling in metabolic regulation

Transient physical association between enzymes appears to be a cardinal feature of metabolic systems, yet the purpose of this metabolic organisation remains enigmatic. It is generally assumed that substrate channelling occurs in these complexes. However, there is a lack of information concerning the...

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Autores principales: Sweetlove, Lee J., Fernie, Alisdair R.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group UK 2018
Materias:
Review Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5976638/
https://www.ncbi.nlm.nih.gov/pubmed/29849027
http://dx.doi.org/10.1038/s41467-018-04543-8
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author Sweetlove, Lee J.
Fernie, Alisdair R.
author_facet Sweetlove, Lee J.
Fernie, Alisdair R.
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description Transient physical association between enzymes appears to be a cardinal feature of metabolic systems, yet the purpose of this metabolic organisation remains enigmatic. It is generally assumed that substrate channelling occurs in these complexes. However, there is a lack of information concerning the mechanisms and extent of substrate channelling and confusion regarding the consequences of substrate channelling. In this review, we outline recent advances in the structural characterisation of enzyme assemblies and integrate this with new insights from reaction–diffusion modelling and synthetic biology to clarify the mechanistic and functional significance of the phenomenon.
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spelling pubmed-59766382018-06-01 The role of dynamic enzyme assemblies and substrate channelling in metabolic regulation Sweetlove, Lee J. Fernie, Alisdair R. Nat Commun Review Article Transient physical association between enzymes appears to be a cardinal feature of metabolic systems, yet the purpose of this metabolic organisation remains enigmatic. It is generally assumed that substrate channelling occurs in these complexes. However, there is a lack of information concerning the mechanisms and extent of substrate channelling and confusion regarding the consequences of substrate channelling. In this review, we outline recent advances in the structural characterisation of enzyme assemblies and integrate this with new insights from reaction–diffusion modelling and synthetic biology to clarify the mechanistic and functional significance of the phenomenon. Nature Publishing Group UK 2018-05-30 /pmc/articles/PMC5976638/ /pubmed/29849027 http://dx.doi.org/10.1038/s41467-018-04543-8 Text en © The Author(s) 2018 Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.
spellingShingle Review Article
Sweetlove, Lee J.
Fernie, Alisdair R.
The role of dynamic enzyme assemblies and substrate channelling in metabolic regulation
title The role of dynamic enzyme assemblies and substrate channelling in metabolic regulation
title_full The role of dynamic enzyme assemblies and substrate channelling in metabolic regulation
title_fullStr The role of dynamic enzyme assemblies and substrate channelling in metabolic regulation
title_full_unstemmed The role of dynamic enzyme assemblies and substrate channelling in metabolic regulation
title_short The role of dynamic enzyme assemblies and substrate channelling in metabolic regulation
title_sort role of dynamic enzyme assemblies and substrate channelling in metabolic regulation
topic Review Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5976638/
https://www.ncbi.nlm.nih.gov/pubmed/29849027
http://dx.doi.org/10.1038/s41467-018-04543-8
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