Properties and Function of Enzymes in the Metabolic Regulation of Oxidative and Reductive Processes

A special issue of Cells (ISSN 2073-4409). This special issue belongs to the section "Cell Microenvironment".

Deadline for manuscript submissions: closed (31 March 2024) | Viewed by 4403

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Biochemistry Unit, Department of Biology, University of Pisa, Via S. Zeno, 51, 56123 Pisa, Italy
Interests: allosteric and covalent regulation of enzymes; kinetic and regulatory properties of enzymes; oxidative stress; protein S-thiolation; purine salvage enzymes; chaperon-like activity of α-crystallin; polyol pathway enzymes; cytotoxic aldehyde metabolism; aldose reductase inhibition
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Special Issue Information

Dear Colleagues,

The transfer of electrons between atoms is the simplest way to mobilize chemical energy between molecules. Indeed, oxidative and reductive processes represent the cell’s unavoidable path for recruiting and managing metabolic energy. Hence, the catabolic pathways through which metabolic energy is made available for biosynthetic purposes or more generally for allowing the variety of cellular functions are closely related to redox processes. Thus, molecular oxygen and/or a number of intracellular redox systems allow the replenishment of high-energy molecules on which cellular life relies. On the other hand, anabolism often proceeds via reductive steps, which are also essential to counteract the conditions of oxidative stress deriving from the oxidative environment in which cellular life normally takes place. In this regard, the redox homeostasis of cellular systems represents a goal pursued in all living organisms. Such a large network of molecular events requires rigorous metabolic control via oxidoreductases activities, in charge of catalyzing the single competing events. Oxidoreductases represent the largest and most articulated enzyme class with over 1400 entries. This is due both to the variety of redox reactions used in different organisms to meet metabolic needs and to the specificity of the enzymes involved. Thus, many different dehydrogenases targeting specific substrates and cofactors, oxidases, and peroxidases are recruited to drive metabolic reactions, to control transmembrane trafficking, and to perform an antioxidant/detoxifying action.

The aim of this Special Issue is to offer a common platform where the action of different oxidoreductases, acting on reversible or irreversible reactions, can be dissected in terms of structural determinants, catalytic properties, regulatory features, and metabolic function.

Prof. Dr. Umberto Mura
Guest Editor

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Keywords

  • oxidoreductases
  • dehydrogenases
  • pyridine redox cofactors
  • flavine redox cofactors
  • oxygenases
  • hydroxylases
  • peroxidases
  • oxidative stress
  • antioxidant enzymes
  • glutathione
  • metallothionein

Published Papers (3 papers)

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Research

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20 pages, 2962 KiB  
Article
NTRC and TRX-f Coordinately Affect the Levels of Enzymes of Chlorophyll Biosynthesis in a Light-Dependent Manner
by Daniel Wittmann, Peter Geigenberger and Bernhard Grimm
Cells 2023, 12(12), 1670; https://doi.org/10.3390/cells12121670 - 20 Jun 2023
Cited by 1 | Viewed by 1285
Abstract
Redox regulation of plastid gene expression and different metabolic pathways promotes many activities of redox-sensitive proteins. We address the question of how the plastid redox state and the contributing reducing enzymes control the enzymes of tetrapyrrole biosynthesis (TBS). In higher plants, this metabolic [...] Read more.
Redox regulation of plastid gene expression and different metabolic pathways promotes many activities of redox-sensitive proteins. We address the question of how the plastid redox state and the contributing reducing enzymes control the enzymes of tetrapyrrole biosynthesis (TBS). In higher plants, this metabolic pathway serves to produce chlorophyll and heme, among other essential end products. Because of the strictly light-dependent synthesis of chlorophyll, tight control of TBS requires a diurnal balanced supply of the precursor 5-aminolevulinic acid (ALA) to prevent the accumulation of photoreactive metabolic intermediates in darkness. We report on some TBS enzymes that accumulate in a light intensity-dependent manner, and their contents decrease under oxidizing conditions of darkness, low light conditions, or in the absence of NADPH-dependent thioredoxin reductase (NTRC) and thioredoxin f1 (TRX-f1). Analysis of single and double trxf1 and ntrc mutants revealed a decreased content of the early TBS enzymes glutamyl-tRNA reductase (GluTR) and 5-aminolevulinic acid dehydratase (ALAD) instead of an exclusive decrease in enzyme activity. This effect was dependent on light conditions and strongly attenuated after transfer to high light intensities. Thus, it is suggested that a deficiency of plastid-localized thiol-redox transmitters leads to enhanced degradation of TBS enzymes rather than being directly caused by lower catalytic activity. The effects of the proteolytic activity of the Clp protease on TBS enzymes were studied by using Clp subunit-deficient mutants. The simultaneous lack of TRX and Clp activities in double mutants confirms the Clp-induced degradation of some TBS proteins in the absence of reductive activity of TRXs. In addition, we verified previous observations that decreased chlorophyll and heme levels in ntrc could be reverted to WT levels in the ntrc/Δ2cp triple mutant. The decreased synthesis of 5-aminolevulinic acid and porphobilinogen in ntrc was completely restored in ntrc/Δ2cp and correlated with WT-like levels of GluTR, ALAD, and other TBS proteins. Full article
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Review

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17 pages, 3221 KiB  
Review
CAH3 from Chlamydomonas reinhardtii: Unique Carbonic Anhydrase of the Thylakoid Lumen
by Vasily V. Terentyev and Anna K. Shukshina
Cells 2024, 13(2), 109; https://doi.org/10.3390/cells13020109 - 05 Jan 2024
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Abstract
CAH3 is the only carbonic anhydrase (CA) present in the thylakoid lumen of the green algae Chlamydomonas reinhardtii. The monomer of the enzyme has a molecular weight of ~29.5 kDa with high CA activity. Through its dehydration activity, CAH3 can be involved [...] Read more.
CAH3 is the only carbonic anhydrase (CA) present in the thylakoid lumen of the green algae Chlamydomonas reinhardtii. The monomer of the enzyme has a molecular weight of ~29.5 kDa with high CA activity. Through its dehydration activity, CAH3 can be involved either in the carbon-concentrating mechanism supplying CO2 for RuBisCO in the pyrenoid or in supporting the maximal photosynthetic activity of photosystem II (PSII) by accelerating the removal of protons from the active center of the water-oxidizing complex. Both proposed roles are considered in this review, together with a description of the enzymatic parameters of native and recombinant CAH3, the crystal structure of the protein, and the possible use of lumenal CA as a tool for increasing biomass production in higher plants. The identified involvement of lumenal CAH3 in the function of PSII is still unique among green algae and higher plants and can be used to understand the mechanism(s) of the functional interconnection between PSII and the proposed CA(s) of the thylakoid lumen in other organisms. Full article
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31 pages, 2569 KiB  
Review
Fungal Alcohol Dehydrogenases: Physiological Function, Molecular Properties, Regulation of Their Production, and Biotechnological Potential
by J. Félix Gutiérrez-Corona, Gloria Angélica González-Hernández, Israel Enrique Padilla-Guerrero, Vianey Olmedo-Monfil, Ana Lilia Martínez-Rocha, J. Alberto Patiño-Medina, Víctor Meza-Carmen and Juan Carlos Torres-Guzmán
Cells 2023, 12(18), 2239; https://doi.org/10.3390/cells12182239 - 08 Sep 2023
Cited by 2 | Viewed by 1515
Abstract
Fungal alcohol dehydrogenases (ADHs) participate in growth under aerobic or anaerobic conditions, morphogenetic processes, and pathogenesis of diverse fungal genera. These processes are associated with metabolic operation routes related to alcohol, aldehyde, and acid production. The number of ADH enzymes, their metabolic roles, [...] Read more.
Fungal alcohol dehydrogenases (ADHs) participate in growth under aerobic or anaerobic conditions, morphogenetic processes, and pathogenesis of diverse fungal genera. These processes are associated with metabolic operation routes related to alcohol, aldehyde, and acid production. The number of ADH enzymes, their metabolic roles, and their functions vary within fungal species. The most studied ADHs are associated with ethanol metabolism, either as fermentative enzymes involved in the production of this alcohol or as oxidative enzymes necessary for the use of ethanol as a carbon source; other enzymes participate in survival under microaerobic conditions. The fast generation of data using genome sequencing provides an excellent opportunity to determine a correlation between the number of ADHs and fungal lifestyle. Therefore, this review aims to summarize the latest knowledge about the importance of ADH enzymes in the physiology and metabolism of fungal cells, as well as their structure, regulation, evolutionary relationships, and biotechnological potential. Full article
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