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spelling 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
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