Ribulose-1,5-bisphosphate regeneration in the Calvin-Benson-Bassham cycle: Focus on the last three enzymatic steps that allow the formation of Rubisco substrate.

carbon fixation catalysis epimerase isomerase kinase structure

Journal

Frontiers in plant science
ISSN: 1664-462X
Titre abrégé: Front Plant Sci
Pays: Switzerland
ID NLM: 101568200

Informations de publication

Date de publication:
2023
Historique:
received: 23 12 2022
accepted: 27 01 2023
entrez: 6 3 2023
pubmed: 7 3 2023
medline: 7 3 2023
Statut: epublish

Résumé

The Calvin-Benson-Bassham (CBB) cycle comprises the metabolic phase of photosynthesis and is responsible for carbon fixation and the production of sugar phosphates. The first step of the cycle involves the enzyme ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) which catalyzes the incorporation of inorganic carbon into 3-phosphoglyceric acid (3PGA). The following steps include ten enzymes that catalyze the regeneration of ribulose-1,5-bisphosphate (RuBP), the substrate of Rubisco. While it is well established that Rubisco activity acts as a limiting step of the cycle, recent modeling studies and experimental evidence have shown that the efficiency of the pathway is also impacted by the regeneration of the Rubisco substrate itself. In this work, we review the current understanding of the structural and catalytic features of the photosynthetic enzymes that catalyze the last three steps of the regeneration phase, namely ribose-5-phosphate isomerase (RPI), ribulose-5-phosphate epimerase (RPE), and phosphoribulokinase (PRK). In addition, the redox- and metabolic-based regulatory mechanisms targeting the three enzymes are also discussed. Overall, this review highlights the importance of understudied steps in the CBB cycle and provides direction for future research aimed at improving plant productivity.

Identifiants

pubmed: 36875598
doi: 10.3389/fpls.2023.1130430
pmc: PMC9978339
doi:

Types de publication

Journal Article Review

Langues

eng

Pagination

1130430

Informations de copyright

Copyright © 2023 Meloni, Gurrieri, Fermani, Velie, Sparla, Crozet, Henri and Zaffagnini.

Déclaration de conflit d'intérêts

The authors declare that the research was conducted in the absence of any commercial or financial relationships that could be construed as a potential conflict of interest.

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Auteurs

Maria Meloni (M)

Department of Pharmacy and Biotechnologies, University of Bologna, Bologna, Italy.

Libero Gurrieri (L)

Department of Pharmacy and Biotechnologies, University of Bologna, Bologna, Italy.

Simona Fermani (S)

Department of Chemistry "G. Ciamician", University of Bologna, Bologna, Italy.
Interdepartmental Centre for Industrial Research Health Sciences & Technologies, University of Bologna, Bologna, Italy.

Lauren Velie (L)

Department of Biochemistry and Molecular Biology, University of Massachusetts Amherst, Amherst, MA, United States.

Francesca Sparla (F)

Department of Pharmacy and Biotechnologies, University of Bologna, Bologna, Italy.

Pierre Crozet (P)

Laboratory of Computational and Quantitative Biology, Sorbonne Université, CNRS, Institut de Biologie Paris-Seine, Paris, France.

Julien Henri (J)

Laboratory of Computational and Quantitative Biology, Sorbonne Université, CNRS, Institut de Biologie Paris-Seine, Paris, France.

Mirko Zaffagnini (M)

Department of Pharmacy and Biotechnologies, University of Bologna, Bologna, Italy.

Classifications MeSH