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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paper:paper_08926638_v7_n8_p622_Wolosiuk2023-06-08T15:47:24Z The reductive pentose phosphate cycle for photosynthetic CO2 assimilation: Enzyme modulation Wolosiuk, Ricardo Alejandro Ballicora, Miguel Angel Hagelin, Karin 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. 1993 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_08926638_v7_n8_p622_Wolosiuk 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, Ricardo Alejandro Ballicora, Miguel Angel Hagelin, Karin 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. |
author |
Wolosiuk, Ricardo Alejandro Ballicora, Miguel Angel Hagelin, Karin |
author_facet |
Wolosiuk, Ricardo Alejandro Ballicora, Miguel Angel Hagelin, Karin |
author_sort |
Wolosiuk, Ricardo Alejandro |
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 |
publishDate |
1993 |
url |
https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_08926638_v7_n8_p622_Wolosiuk http://hdl.handle.net/20.500.12110/paper_08926638_v7_n8_p622_Wolosiuk |
work_keys_str_mv |
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