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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...

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Autores principales: Orr, Douglas J, Robijns, Alice K J, Baker, Christopher R, Niyogi, Krishna K, Carmo-Silva, Elizabete
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Oxford University Press 2022
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.
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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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