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Functions of Enzymes Related to Plant Dicarboxylic Acid Metabolism
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Functions of Enzymes Related to Plant Dicarboxylic Acid Metabolism

A special issue of Plants (ISSN 2223-7747). This special issue belongs to the section "Plant Molecular Biology".

Deadline for manuscript submissions: closed (31 October 2023) | Viewed by 11267

Special Issue Editors

Dr. Naoki Yamamoto

E-Mail Website
Guest Editor
1. Rice Research Institute, Sichuan Agricultural University, Chengdu 611130, China
2. Laboratory of Genetic Engineering, Graduate School of Life and Environmental Sciences, Kyoto Prefectural University, Kyoto 6068522, Japan
Interests: Phosphoenolpyruvate carboxylase, seed development and metabolism, seed storage compounds, plant responses to biotic and abiotic stress, plant and fungal genomics, computational biology
Dr. Toshio Sugimoto

E-Mail Website
Guest Editor
Research Center for Food and Agriculture, Wakayama University, Wakayama 6408510, Japan
Interests: Environmental and genetical factors affecting on accumulation of storage compounds, protein and oil, in crop seeds

Special Issue Information

Dear Colleagues,

Plant dicarboxylic acids include primary substances, such as oxaloacetate, malalte, α-ketoglutaric acid, glutamic acid, and aspartic acid. These chemicals are synthesized via the glycolytic pathway, the TCA cycle, and several specific enzymes in amino acid biosynthesis and organic acid metabolism. These enzymes play critical roles in multiple biological processes, such as bioenergy metabolism and the storage, transportation, and utilization of carbon, nitrogen, and other substances. They involve various important biological enzyme reactions, regulating the balance of amino acids, sugar metabolism, fat metabolism, and cellular energy state in an organism. In a C4-photosynthetic system, a set of enzymes in the C4-dicarboxylic acid pathway (Hatch–Slack pathway) acts on concentrating atmospheric CO2 to achieve high-efficiency photosynthesis under abiotic stress conditions.

This Special Issue will highlight original research papers (research articles and communications), reviews, and concept papers focusing on the molecular, biochemical, and/or physiological functions of enzymes related to plant dicarboxylic acid metabolism. Manuscripts describing not only the new functions of these enzymes but also novel insights into the functionality of plant dicarboxylic acid metabolism are welcome. Studies containing molecular diversity and evolutionary analyses will be considered if the manuscripts represent clear ideas and evidence linked to enzymes involved in plant dicarboxylic acid metabolism.

Dr. Naoki Yamamoto
Dr. Toshio Sugimoto
Guest Editors

Manuscript Submission Information

Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. All submissions that pass pre-check are peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.

Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a single-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. Plants is an international peer-reviewed open access semimonthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. The Article Processing Charge (APC) for publication in this open access journal is 2700 CHF (Swiss Francs). Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.

Keywords

  • malate
  • fumalate
  • succinic acid
  • TCA cycle

Published Papers (4 papers)

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Research

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12 pages, 3026 KiB  
Communication
Prokaryotic Expression of Phosphoenolpyruvate Carboxylase Fragments from Peanut and Analysis of Osmotic Stress Tolerance of Recombinant Strains
by Jiaqi Tu, Lanlan Feng, Yanbin Hong, Qiuyun Liu, Xia Huang and Yin Li
Plants 2021, 10(2), 365; https://doi.org/10.3390/plants10020365 - 14 Feb 2021
Cited by 4 | Viewed by 2079
Abstract
Phosphoenolpyruvate carboxylase (PEPC) is a ubiquitous cytosolic enzyme that catalyzes the irreversible β-carboxylation of phosphoenolpyruvate (PEP) in presence of HCO3− to produce oxaloacetate (OAA) during carbon fixation and photosynthesis. It is well accepted that PEPC genes are [...] Read more.
Phosphoenolpyruvate carboxylase (PEPC) is a ubiquitous cytosolic enzyme that catalyzes the irreversible β-carboxylation of phosphoenolpyruvate (PEP) in presence of HCO3− to produce oxaloacetate (OAA) during carbon fixation and photosynthesis. It is well accepted that PEPC genes are expressed in plants upon stress. PEPC also supports the biosynthesis of biocompatible osmolytes in many plant species under osmotic stress. There are five isoforms of PEPC found in peanut (Arachis hypogaea L.), namely, AhPEPC1, AhPEPC2, AhPEPC3, AhPEPC4, and AhPEPC5. Quantitative real-time polymerase chain reaction (qRT-PCR) analysis revealed that the gene expression patterns of these AhPEPC genes were different in mature seeds, stems, roots, flowers, and leaves. The expression of all the plant type PEPC (PTPCs) (AhPEPC1, AhPEPC2, AhPEPC3, and AhPEPC4) was relatively high in roots, while the bacterial type PEPC (BTPC) (AhPEPC5) showed a remarkable expression level in flowers. Principal component analysis (PCA) result showed that AhPEPC3 and AhPEPC4 are correlated with each other, indicating comparatively associations with roots, and AhPEPC5 have a very close relationship with flowers. In order to investigate the function of these AhPEPCs, the fragments of these five AhPEPC cDNA were cloned and expressed in Escherichia coli (E. coli). The recombinant proteins contained a conserved domain with a histidine site, which is important for enzyme catalysis. Results showed that protein fragments of AhPEPC1, AhPEPC2, and AhPEPC5 had remarkable expression levels in E. coli. These three recombinant strains were more sensitive at pH 9.0, and recombinant strains carrying AhPEPC2 and AhPEPC5 fragments exhibited more growth than the control strain with the presence of PEG6000. Our findings showed that the expression of the AhPEPC fragments may enhance the resistance of transformed E. coli to osmotic stress. Full article
(This article belongs to the Special Issue Functions of Enzymes Related to Plant Dicarboxylic Acid Metabolism)
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17 pages, 3737 KiB  
Article
Genetic and Pharmacological Inhibition of Autophagy Increases the Monoubiquitination of Non-Photosynthetic Phosphoenolpyruvate Carboxylase
by Guillermo Baena, Ana B. Feria, Luis Hernández-Huertas, Jacinto Gandullo, Cristina Echevarría, José A. Monreal and Sofía García-Mauriño
Plants 2021, 10(1), 12; https://doi.org/10.3390/plants10010012 - 23 Dec 2020
Cited by 4 | Viewed by 2464
Abstract
Phosphoenolpyruvate carboxylase (PEPC) is an enzyme with key roles in carbon and nitrogen metabolisms. The mechanisms that control enzyme stability and turnover are not well known. This paper investigates the degradation of PEPC via selective autophagy, including the role of the [...] Read more.
Phosphoenolpyruvate carboxylase (PEPC) is an enzyme with key roles in carbon and nitrogen metabolisms. The mechanisms that control enzyme stability and turnover are not well known. This paper investigates the degradation of PEPC via selective autophagy, including the role of the monoubiquitination of the enzyme in this process. In Arabidopsis, the genetic inhibition of autophagy increases the amount of monoubiquitinated PEPC in the atg2, atg5, and atg18a lines. The same is observed in nbr1, which is deficient in a protein that recruits monoubiquitinated substrates for selective autophagy. In cultured tobacco cells, the chemical inhibition of the degradation of autophagic substrates increases the quantity of PEPC proteins. When the formation of the autophagosome is blocked with 3-methyladenine (3-MA), monoubiquitinated PEPC accumulates as a result. Finally, pull-down experiments with a truncated version of NBR1 demonstrate the recovery of intact and/or fragmented PEPC in Arabidopsis leaves and roots, as well as cultured tobacco cells. Taken together, the results show that a fraction of PEPC is cleaved via selective autophagy and that the monoubiquitination of the enzyme has a role in its recruitment towards this pathway. Although autophagy seems to be a minor pathway, the results presented here increase the knowledge about the role of monoubiquitination and the regulation of PEPC degradation. Full article
(This article belongs to the Special Issue Functions of Enzymes Related to Plant Dicarboxylic Acid Metabolism)
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12 pages, 1024 KiB  
Article
Molecular Cloning of Novel-Type Phosphoenolpyruvate Carboxylase Isoforms in Pitaya (Hylocereus undatus)
by Keiichi Nomura, Yuho Sakurai and Mayu Dozono
Plants 2020, 9(9), 1241; https://doi.org/10.3390/plants9091241 - 21 Sep 2020
Cited by 2 | Viewed by 2378
Abstract
Phosphoenolpyruvate carboxylase (PEPC) is an important enzyme involved in the initial CO2 fixation of crassulacean acid metabolism (CAM) photosynthesis. To understand the cultivation characteristics of a CAM plant pitaya, it is necessary to clarify the characteristics of PEPC in this [...] Read more.
Phosphoenolpyruvate carboxylase (PEPC) is an important enzyme involved in the initial CO2 fixation of crassulacean acid metabolism (CAM) photosynthesis. To understand the cultivation characteristics of a CAM plant pitaya, it is necessary to clarify the characteristics of PEPC in this species. Here, we cloned three PEPC cDNAs in pitaya, HuPPC1, HuPPC2, and HuPPC3, which encode 942, 934, and 966 amino acid residues, respectively. Phylogenetic analysis indicated that these PEPC belonged to plant-type PEPC (PTPC), although HuPPC1 and HuPPC2 have no Ser-phosphorylation motif in N-terminal region, which is a crucial regulation site in PTPC and contributes to CAM periodicity. HuPPC1 and HuPPC2 phylogenetically unique to the Cactaceae family, whereas HuPPC3 was included in a CAM clade. Two isoforms were partially purified at the protein level and were assigned as HuPPC2 and HuPPC3 using MASCOT analysis. The most distinct difference in enzymatic properties between the two was sensitivity to malate and aspartate, both of which are allosteric inhibitors of PEPC. With 2 mM malate, HuPPC3 was inhibited to 10% of the initial activity, whereas HuPPC2 activity was maintained at 70%. Aspartate inhibited HuPPC3 activity by approximately 50% at 5 mM; however, such inhibition was not observed for HuPPC2 at 10 mM. These results suggest that HuPPC3 corresponds to a general CAM-related PEPC, whereas HuPPC1 and HuPPC2 are related to carbon and/or nitrogen metabolism, with a characteristic regulation mechanism similar to those of Cactaceae plants. Full article
(This article belongs to the Special Issue Functions of Enzymes Related to Plant Dicarboxylic Acid Metabolism)
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Review

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14 pages, 1256 KiB  
Review
Differential Expression, Tissue-Specific Distribution, and Posttranslational Controls of Phosphoenolpyruvate Carboxylase
by Lorrenne Caburatan and Joonho Park
Plants 2021, 10(9), 1887; https://doi.org/10.3390/plants10091887 - 13 Sep 2021
Cited by 4 | Viewed by 2662
Abstract
Phosphoenolpyruvate carboxylase (PEPC) is a ubiquitous cytosolic enzyme, which is crucial for plant carbon metabolism. PEPC participates in photosynthesis by catalyzing the initial fixation of atmospheric CO2 and is abundant in both C4 and crassulacean acid metabolism leaves. PEPC is differentially [...] Read more.
Phosphoenolpyruvate carboxylase (PEPC) is a ubiquitous cytosolic enzyme, which is crucial for plant carbon metabolism. PEPC participates in photosynthesis by catalyzing the initial fixation of atmospheric CO2 and is abundant in both C4 and crassulacean acid metabolism leaves. PEPC is differentially expressed at different stages of plant development, mostly in leaves, but also in developing seeds. PEPC is known to show tissue-specific distribution in leaves and in other plant organs, such as roots, stems, and flowers. Plant PEPC undergoes reversible phosphorylation and monoubiquitination, which are posttranslational modifications playing important roles in regulatory processes and in protein localization. Phosphorylation activates the PEPC enzyme, making it more sensitive to glucose-6-phosphate and less sensitive to malate or aspartate. PEPC phosphorylation is known to be diurnally regulated and delicately changed in response to various environmental stimuli, in addition to light. PEPCs belong to a small gene family encoding several plant-type and distantly related bacterial-type PEPCs. This paper provides a minireview of the general information on PEPCs in both C4 and C3 plants. Full article
(This article belongs to the Special Issue Functions of Enzymes Related to Plant Dicarboxylic Acid Metabolism)
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