The reductive pentose phosphate cycle for photosynthetic CO2 assimilation: Enzyme modulation

The reductive pentose phosphate cycle (Benson-Calvin cycle) is the main biochemical pathway for the conversion of atmospheric CO2 to organic compounds. Two unique systems that link light-triggered events in thylakoid membranes with enzyme regulation are located in the soluble portion of chloroplasts...

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Autores principales:	Wolosiuk, R.A., Ballicora, M.A., Hagelin, K.
Formato:	JOUR
Materias:	Benson-Calvin cycle Chloroplasts Enzyme modulation Ferredoxin-thioredoxin system carbon dioxide ferredoxin fructose bisphosphatase glyceraldehyde 3 phosphate dehydrogenase thioredoxin transketolase amino acid sequence carbon dioxide measurement chloroplast enzyme modification enzyme regulation pentose phosphate cycle photosynthesis plant priority journal review Amino Acid Sequence Carbon Dioxide Molecular Sequence Data Pentosephosphate Pathway Photosynthesis Support, Non-U.S. Gov't Thioredoxin
Acceso en línea:	http://hdl.handle.net/20.500.12110/paper_08926638_v7_n8_p622_Wolosiuk
Aporte de:	Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires

id	todo:paper_08926638_v7_n8_p622_Wolosiuk
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spelling	todo:paper_08926638_v7_n8_p622_Wolosiuk2023-10-03T15:41:38Z The reductive pentose phosphate cycle for photosynthetic CO2 assimilation: Enzyme modulation Wolosiuk, R.A. Ballicora, M.A. Hagelin, K. Benson-Calvin cycle Chloroplasts Enzyme modulation Ferredoxin-thioredoxin system carbon dioxide ferredoxin fructose bisphosphatase glyceraldehyde 3 phosphate dehydrogenase thioredoxin transketolase amino acid sequence carbon dioxide measurement chloroplast enzyme modification enzyme regulation pentose phosphate cycle photosynthesis plant priority journal review Amino Acid Sequence Carbon Dioxide Chloroplasts Molecular Sequence Data Pentosephosphate Pathway Photosynthesis Support, Non-U.S. Gov't Thioredoxin The reductive pentose phosphate cycle (Benson-Calvin cycle) is the main biochemical pathway for the conversion of atmospheric CO2 to organic compounds. Two unique systems that link light-triggered events in thylakoid membranes with enzyme regulation are located in the soluble portion of chloroplasts (stroma): the ferredoxin-thioredoxin system and ribulose 1,5-bisphosphate carboxylase/oxygenase-Activase (Rubisco-Activase). The ferredoxin-thioredoxin system (ferredoxin, ferredoxin-thioredoxin reductase, and thioredoxin) transforms native (inactive) glyceraldehyde-3-P dehydrogenase, fructose-1,6-bisphosphatase, sedoheptulose-1,7-bisphosphatase, and phosphoribulokinase to catalytically competent forms. However, the comparison of enzymes reveals the absence of common amino acid sequences for the action of reduced thioredoxin. Thiol/disulfide exchanges appear as the underlying mechanism, but chloroplast metabolites and target domains make the activation process peculiar for each enzyme. On the other hand, Rubisco-Activase facilitates the combination of CO2 with a specific ∈-amino group of ribulose 1,5-bisphosphate carboxylase/oxygenase and the subsequent stabilization of the carbamylated enzyme by Mg2+, in a reaction that depends on ATP and ribulose 1,5-bisphosphate. Most of these studies were carried out in homogenous solutions; nevertheless, a growing body of evidence indicates that several enzymes of the cycle associate either with thylakoid membranes or with other proteins yielding supramolecular complexes in the chloroplast. Fil:Wolosiuk, R.A. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Ballicora, M.A. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Hagelin, K. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar http://hdl.handle.net/20.500.12110/paper_08926638_v7_n8_p622_Wolosiuk
institution	Universidad de Buenos Aires
institution_str	I-28
repository_str	R-134
collection	Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA)
topic	Benson-Calvin cycle Chloroplasts Enzyme modulation Ferredoxin-thioredoxin system carbon dioxide ferredoxin fructose bisphosphatase glyceraldehyde 3 phosphate dehydrogenase thioredoxin transketolase amino acid sequence carbon dioxide measurement chloroplast enzyme modification enzyme regulation pentose phosphate cycle photosynthesis plant priority journal review Amino Acid Sequence Carbon Dioxide Chloroplasts Molecular Sequence Data Pentosephosphate Pathway Photosynthesis Support, Non-U.S. Gov't Thioredoxin
spellingShingle	Benson-Calvin cycle Chloroplasts Enzyme modulation Ferredoxin-thioredoxin system carbon dioxide ferredoxin fructose bisphosphatase glyceraldehyde 3 phosphate dehydrogenase thioredoxin transketolase amino acid sequence carbon dioxide measurement chloroplast enzyme modification enzyme regulation pentose phosphate cycle photosynthesis plant priority journal review Amino Acid Sequence Carbon Dioxide Chloroplasts Molecular Sequence Data Pentosephosphate Pathway Photosynthesis Support, Non-U.S. Gov't Thioredoxin Wolosiuk, R.A. Ballicora, M.A. Hagelin, K. The reductive pentose phosphate cycle for photosynthetic CO2 assimilation: Enzyme modulation
topic_facet	Benson-Calvin cycle Chloroplasts Enzyme modulation Ferredoxin-thioredoxin system carbon dioxide ferredoxin fructose bisphosphatase glyceraldehyde 3 phosphate dehydrogenase thioredoxin transketolase amino acid sequence carbon dioxide measurement chloroplast enzyme modification enzyme regulation pentose phosphate cycle photosynthesis plant priority journal review Amino Acid Sequence Carbon Dioxide Chloroplasts Molecular Sequence Data Pentosephosphate Pathway Photosynthesis Support, Non-U.S. Gov't Thioredoxin
description	The reductive pentose phosphate cycle (Benson-Calvin cycle) is the main biochemical pathway for the conversion of atmospheric CO2 to organic compounds. Two unique systems that link light-triggered events in thylakoid membranes with enzyme regulation are located in the soluble portion of chloroplasts (stroma): the ferredoxin-thioredoxin system and ribulose 1,5-bisphosphate carboxylase/oxygenase-Activase (Rubisco-Activase). The ferredoxin-thioredoxin system (ferredoxin, ferredoxin-thioredoxin reductase, and thioredoxin) transforms native (inactive) glyceraldehyde-3-P dehydrogenase, fructose-1,6-bisphosphatase, sedoheptulose-1,7-bisphosphatase, and phosphoribulokinase to catalytically competent forms. However, the comparison of enzymes reveals the absence of common amino acid sequences for the action of reduced thioredoxin. Thiol/disulfide exchanges appear as the underlying mechanism, but chloroplast metabolites and target domains make the activation process peculiar for each enzyme. On the other hand, Rubisco-Activase facilitates the combination of CO2 with a specific ∈-amino group of ribulose 1,5-bisphosphate carboxylase/oxygenase and the subsequent stabilization of the carbamylated enzyme by Mg2+, in a reaction that depends on ATP and ribulose 1,5-bisphosphate. Most of these studies were carried out in homogenous solutions; nevertheless, a growing body of evidence indicates that several enzymes of the cycle associate either with thylakoid membranes or with other proteins yielding supramolecular complexes in the chloroplast.
format	JOUR
author	Wolosiuk, R.A. Ballicora, M.A. Hagelin, K.
author_facet	Wolosiuk, R.A. Ballicora, M.A. Hagelin, K.
author_sort	Wolosiuk, R.A.
title	The reductive pentose phosphate cycle for photosynthetic CO2 assimilation: Enzyme modulation
title_short	The reductive pentose phosphate cycle for photosynthetic CO2 assimilation: Enzyme modulation
title_full	The reductive pentose phosphate cycle for photosynthetic CO2 assimilation: Enzyme modulation
title_fullStr	The reductive pentose phosphate cycle for photosynthetic CO2 assimilation: Enzyme modulation
title_full_unstemmed	The reductive pentose phosphate cycle for photosynthetic CO2 assimilation: Enzyme modulation
title_sort	reductive pentose phosphate cycle for photosynthetic co2 assimilation: enzyme modulation
url	http://hdl.handle.net/20.500.12110/paper_08926638_v7_n8_p622_Wolosiuk
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The reductive pentose phosphate cycle for photosynthetic CO2 assimilation: Enzyme modulation

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