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Freedom of assembly: metabolic enzymes come together

Many different enzymes in intermediate metabolism dynamically assemble filamentous polymers in cells, often in response to changes in physiological conditions. Most of the enzyme filaments known to date have only been observed in cells, but in a handful of cases structural and biochemical studies ha...

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Detalles Bibliográficos
Autores principales: Simonet, Jacqueline C., Burrell, Anika L., Kollman, Justin M., Peterson, Jeffrey R.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: The American Society for Cell Biology 2020
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7353150/
https://www.ncbi.nlm.nih.gov/pubmed/32463766
http://dx.doi.org/10.1091/mbc.E18-10-0675
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author Simonet, Jacqueline C.
Burrell, Anika L.
Kollman, Justin M.
Peterson, Jeffrey R.
author_facet Simonet, Jacqueline C.
Burrell, Anika L.
Kollman, Justin M.
Peterson, Jeffrey R.
author_sort Simonet, Jacqueline C.
collection PubMed
description Many different enzymes in intermediate metabolism dynamically assemble filamentous polymers in cells, often in response to changes in physiological conditions. Most of the enzyme filaments known to date have only been observed in cells, but in a handful of cases structural and biochemical studies have revealed the mechanisms and consequences of assembly. In general, enzyme polymerization functions as a mechanism to allosterically tune enzyme kinetics, and it may play a physiological role in integrating metabolic signaling. Here, we highlight some principles of metabolic filaments by focusing on two well-studied examples in nucleotide biosynthesis pathways—inosine-5’-monophosphate (IMP) dehydrogenase and cytosine triphosphate (CTP) synthase.
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spelling pubmed-73531502020-08-17 Freedom of assembly: metabolic enzymes come together Simonet, Jacqueline C. Burrell, Anika L. Kollman, Justin M. Peterson, Jeffrey R. Mol Biol Cell Perspective Many different enzymes in intermediate metabolism dynamically assemble filamentous polymers in cells, often in response to changes in physiological conditions. Most of the enzyme filaments known to date have only been observed in cells, but in a handful of cases structural and biochemical studies have revealed the mechanisms and consequences of assembly. In general, enzyme polymerization functions as a mechanism to allosterically tune enzyme kinetics, and it may play a physiological role in integrating metabolic signaling. Here, we highlight some principles of metabolic filaments by focusing on two well-studied examples in nucleotide biosynthesis pathways—inosine-5’-monophosphate (IMP) dehydrogenase and cytosine triphosphate (CTP) synthase. The American Society for Cell Biology 2020-06-01 /pmc/articles/PMC7353150/ /pubmed/32463766 http://dx.doi.org/10.1091/mbc.E18-10-0675 Text en © 2020 Simonet et al. “ASCB®,” “The American Society for Cell Biology®,” and “Molecular Biology of the Cell®” are registered trademarks of The American Society for Cell Biology. http://creativecommons.org/licenses/by-nc-sa/3.0 This article is distributed by The American Society for Cell Biology under license from the author(s). Two months after publication it is available to the public under an Attribution–Noncommercial–Share Alike 3.0 Unported Creative Commons License.
spellingShingle Perspective
Simonet, Jacqueline C.
Burrell, Anika L.
Kollman, Justin M.
Peterson, Jeffrey R.
Freedom of assembly: metabolic enzymes come together
title Freedom of assembly: metabolic enzymes come together
title_full Freedom of assembly: metabolic enzymes come together
title_fullStr Freedom of assembly: metabolic enzymes come together
title_full_unstemmed Freedom of assembly: metabolic enzymes come together
title_short Freedom of assembly: metabolic enzymes come together
title_sort freedom of assembly: metabolic enzymes come together
topic Perspective
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7353150/
https://www.ncbi.nlm.nih.gov/pubmed/32463766
http://dx.doi.org/10.1091/mbc.E18-10-0675
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