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Dynamics of Rubisco regulation by sugar phosphate derivatives and their phosphatases
Regulating the central CO(2)-fixing enzyme Rubisco is as complex as its ancient reaction mechanism and involves interaction with a series of cofactors and auxiliary proteins that activate catalytic sites and maintain activity. A key component among the regulatory mechanisms is the binding of sugar p...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Oxford University Press
2022
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9833046/ https://www.ncbi.nlm.nih.gov/pubmed/36173669 http://dx.doi.org/10.1093/jxb/erac386 |
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author | Orr, Douglas J Robijns, Alice K J Baker, Christopher R Niyogi, Krishna K Carmo-Silva, Elizabete |
author_facet | Orr, Douglas J Robijns, Alice K J Baker, Christopher R Niyogi, Krishna K Carmo-Silva, Elizabete |
author_sort | Orr, Douglas J |
collection | PubMed |
description | Regulating the central CO(2)-fixing enzyme Rubisco is as complex as its ancient reaction mechanism and involves interaction with a series of cofactors and auxiliary proteins that activate catalytic sites and maintain activity. A key component among the regulatory mechanisms is the binding of sugar phosphate derivatives that inhibit activity. Removal of inhibitors via the action of Rubisco activase is required to restore catalytic competency. In addition, specific phosphatases dephosphorylate newly released inhibitors, rendering them incapable of binding to Rubisco catalytic sites. The best studied inhibitor is 2-carboxy-d-arabinitol 1-phosphate (CA1P), a naturally occurring nocturnal inhibitor that accumulates in most species during darkness and low light, progressively binding to Rubisco. As light increases, Rubisco activase removes CA1P from Rubisco, and the specific phosphatase CA1Pase dephosphorylates CA1P to CA, which cannot bind Rubisco. Misfire products of Rubisco’s complex reaction chemistry can also act as inhibitors. One example is xylulose-1,5-bisphosphate (XuBP), which is dephosphorylated by XuBPase. Here we revisit key findings related to sugar phosphate derivatives and their specific phosphatases, highlighting outstanding questions and how further consideration of these inhibitors and their role is important for better understanding the regulation of carbon assimilation. |
format | Online Article Text |
id | pubmed-9833046 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | Oxford University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-98330462023-01-12 Dynamics of Rubisco regulation by sugar phosphate derivatives and their phosphatases Orr, Douglas J Robijns, Alice K J Baker, Christopher R Niyogi, Krishna K Carmo-Silva, Elizabete J Exp Bot Review Papers Regulating the central CO(2)-fixing enzyme Rubisco is as complex as its ancient reaction mechanism and involves interaction with a series of cofactors and auxiliary proteins that activate catalytic sites and maintain activity. A key component among the regulatory mechanisms is the binding of sugar phosphate derivatives that inhibit activity. Removal of inhibitors via the action of Rubisco activase is required to restore catalytic competency. In addition, specific phosphatases dephosphorylate newly released inhibitors, rendering them incapable of binding to Rubisco catalytic sites. The best studied inhibitor is 2-carboxy-d-arabinitol 1-phosphate (CA1P), a naturally occurring nocturnal inhibitor that accumulates in most species during darkness and low light, progressively binding to Rubisco. As light increases, Rubisco activase removes CA1P from Rubisco, and the specific phosphatase CA1Pase dephosphorylates CA1P to CA, which cannot bind Rubisco. Misfire products of Rubisco’s complex reaction chemistry can also act as inhibitors. One example is xylulose-1,5-bisphosphate (XuBP), which is dephosphorylated by XuBPase. Here we revisit key findings related to sugar phosphate derivatives and their specific phosphatases, highlighting outstanding questions and how further consideration of these inhibitors and their role is important for better understanding the regulation of carbon assimilation. Oxford University Press 2022-09-29 /pmc/articles/PMC9833046/ /pubmed/36173669 http://dx.doi.org/10.1093/jxb/erac386 Text en © The Author(s) 2022. Published by Oxford University Press on behalf of the Society for Experimental Biology. https://creativecommons.org/licenses/by/4.0/This is an Open Access article distributed under the terms of the Creative Commons Attribution License (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 Papers Orr, Douglas J Robijns, Alice K J Baker, Christopher R Niyogi, Krishna K Carmo-Silva, Elizabete Dynamics of Rubisco regulation by sugar phosphate derivatives and their phosphatases |
title | Dynamics of Rubisco regulation by sugar phosphate derivatives and their phosphatases |
title_full | Dynamics of Rubisco regulation by sugar phosphate derivatives and their phosphatases |
title_fullStr | Dynamics of Rubisco regulation by sugar phosphate derivatives and their phosphatases |
title_full_unstemmed | Dynamics of Rubisco regulation by sugar phosphate derivatives and their phosphatases |
title_short | Dynamics of Rubisco regulation by sugar phosphate derivatives and their phosphatases |
title_sort | dynamics of rubisco regulation by sugar phosphate derivatives and their phosphatases |
topic | Review Papers |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9833046/ https://www.ncbi.nlm.nih.gov/pubmed/36173669 http://dx.doi.org/10.1093/jxb/erac386 |
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