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The PEP-pyruvate-oxaloacetate node: variation at the heart of metabolism
At the junction between the glycolysis and the tricarboxylic acid cycle—as well as various other metabolic pathways—lies the phosphoenolpyruvate (PEP)-pyruvate-oxaloacetate node (PPO-node). These three metabolites form the core of a network involving at least eleven different types of enzymes, each...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Oxford University Press
2020
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8100219/ https://www.ncbi.nlm.nih.gov/pubmed/33289792 http://dx.doi.org/10.1093/femsre/fuaa061 |
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author | Koendjbiharie, Jeroen G van Kranenburg, Richard Kengen, Servé W M |
author_facet | Koendjbiharie, Jeroen G van Kranenburg, Richard Kengen, Servé W M |
author_sort | Koendjbiharie, Jeroen G |
collection | PubMed |
description | At the junction between the glycolysis and the tricarboxylic acid cycle—as well as various other metabolic pathways—lies the phosphoenolpyruvate (PEP)-pyruvate-oxaloacetate node (PPO-node). These three metabolites form the core of a network involving at least eleven different types of enzymes, each with numerous subtypes. Obviously, no single organism maintains each of these eleven enzymes; instead, different organisms possess different subsets in their PPO-node, which results in a remarkable degree of variation, despite connecting such deeply conserved metabolic pathways as the glycolysis and the tricarboxylic acid cycle. The PPO-node enzymes play a crucial role in cellular energetics, with most of them involved in (de)phosphorylation of nucleotide phosphates, while those responsible for malate conversion are important redox enzymes. Variations in PPO-node therefore reflect the different energetic niches that organisms can occupy. In this review, we give an overview of the biochemistry of these eleven PPO-node enzymes. We attempt to highlight the variation that exists, both in PPO-node compositions, as well as in the roles that the enzymes can have within those different settings, through various recent discoveries in both bacteria and archaea that reveal deviations from canonical functions. |
format | Online Article Text |
id | pubmed-8100219 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2020 |
publisher | Oxford University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-81002192021-05-10 The PEP-pyruvate-oxaloacetate node: variation at the heart of metabolism Koendjbiharie, Jeroen G van Kranenburg, Richard Kengen, Servé W M FEMS Microbiol Rev Review Article At the junction between the glycolysis and the tricarboxylic acid cycle—as well as various other metabolic pathways—lies the phosphoenolpyruvate (PEP)-pyruvate-oxaloacetate node (PPO-node). These three metabolites form the core of a network involving at least eleven different types of enzymes, each with numerous subtypes. Obviously, no single organism maintains each of these eleven enzymes; instead, different organisms possess different subsets in their PPO-node, which results in a remarkable degree of variation, despite connecting such deeply conserved metabolic pathways as the glycolysis and the tricarboxylic acid cycle. The PPO-node enzymes play a crucial role in cellular energetics, with most of them involved in (de)phosphorylation of nucleotide phosphates, while those responsible for malate conversion are important redox enzymes. Variations in PPO-node therefore reflect the different energetic niches that organisms can occupy. In this review, we give an overview of the biochemistry of these eleven PPO-node enzymes. We attempt to highlight the variation that exists, both in PPO-node compositions, as well as in the roles that the enzymes can have within those different settings, through various recent discoveries in both bacteria and archaea that reveal deviations from canonical functions. Oxford University Press 2020-12-08 /pmc/articles/PMC8100219/ /pubmed/33289792 http://dx.doi.org/10.1093/femsre/fuaa061 Text en © The Author(s) 2020. Published by Oxford University Press on behalf of FEMS. https://creativecommons.org/licenses/by/4.0/This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/ (https://creativecommons.org/licenses/by/4.0/) ), which permits unrestricted reuse, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Review Article Koendjbiharie, Jeroen G van Kranenburg, Richard Kengen, Servé W M The PEP-pyruvate-oxaloacetate node: variation at the heart of metabolism |
title | The PEP-pyruvate-oxaloacetate node: variation at the heart of metabolism |
title_full | The PEP-pyruvate-oxaloacetate node: variation at the heart of metabolism |
title_fullStr | The PEP-pyruvate-oxaloacetate node: variation at the heart of metabolism |
title_full_unstemmed | The PEP-pyruvate-oxaloacetate node: variation at the heart of metabolism |
title_short | The PEP-pyruvate-oxaloacetate node: variation at the heart of metabolism |
title_sort | pep-pyruvate-oxaloacetate node: variation at the heart of metabolism |
topic | Review Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8100219/ https://www.ncbi.nlm.nih.gov/pubmed/33289792 http://dx.doi.org/10.1093/femsre/fuaa061 |
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