Expression and properties of the mitochondrial and cytosolic forms of aconitase in maize scutellum

Епринцев, А. Т.; Федорин, Д. Н.; Nikitina, Marina V.; Igamberdiev, Abir U.

doi:10.1016/j.jplph.2015.03.012

Cited by 30 publications

(19 citation statements)

References 38 publications

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“…It is likely that citrate is exported from mitochondria preferentially as compared to isocitrate and 2-oxoglutarate. The aconitase equilibrium is strongly displaced toward citrate, and the mitochondrial aconitase, as compared to the cytosolic form, has a lower affinity to citrate and a higher affinity to isocitrate that favors citrate accumulation ( Eprintsev et al, 2015a ). Citrate export is more than ten times as fast as the export of 2-oxoglutarate in isolated pea leaf mitochondria and twice as fast in spinach leaf mitochondria ( Hanning and Heldt, 1993 ).…”

Section: Incomplete Tricarboxylic Acid Cycle and The Operation Of Malmentioning

confidence: 99%

“…13 C nuclear magnetic resonance studies confirmed that in intact leaves in the light citrate is a major mitochondrial product ( Gout et al, 1993 ). Isocitrate and 2-oxoglutarate are then formed from the exported citrate in the cytosol via the cytosolic aconitase and NADP-isocitrate dehydrogenase which activities are high and usually exceed the activities of the mitochondrial isoforms of these enzymes ( Eprintsev et al, 2015a ).…”

Section: Incomplete Tricarboxylic Acid Cycle and The Operation Of Malmentioning

confidence: 99%

“…The universality of malate as a redox transport compound determines localization of different isoforms of NAD-malate dehydrogenase in mitochondria, cytosol, peroxisomes, plastids and apoplast ( Gietl, 1992 ) as well as the presence of light-activated NADP-malate dehydrogenase in chloroplasts, NAD-malic enzyme in mitochondria and NADP-malic enzyme in plastids and cytosol ( Drincovich et al, 2001 ). Aconitase is present in mitochondria, cytosol and likely absent from peroxisomes ( Eprintsev et al, 2015a ). While NAD-dependent isocitrate dehydrogenase is located in mitochondria, NADP-dependent isocitrate dehydrogenase is found in mitochondria, cytosol, peroxisomes and plastids ( Randall, 1981 ; Corpas et al, 1999 ).…”

Section: Incomplete Tricarboxylic Acid Cycle and The Operation Of Malmentioning

confidence: 99%

“…The aconitase reaction establishes an equilibrium that includes three organic acids: citrate, cis -aconitate and isocitrate. The aconitase equilibrium is shifted toward citrate; however, the ratio between its intermediates depends on the concentration of magnesium, affinity of aconitase to its substrates and other factors ( Blair, 1969 ; Eprintsev et al, 2015a ). In the TCA cycle cis -aconitate appears as a low-concentration intermediate, however, it can be accumulated in plants as the more stable isomer, trans -aconitate ( Stout et al, 1967 ).…”

Section: Trans-aconitate – a Stored Tricarboxylic Acid Poolmentioning

confidence: 99%

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Organic Acids: The Pools of Fixed Carbon Involved in Redox Regulation and Energy Balance in Higher Plants

2016

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Organic acids are synthesized in plants as a result of the incomplete oxidation of photosynthetic products and represent the stored pools of fixed carbon accumulated due to different transient times of conversion of carbon compounds in metabolic pathways. When redox level in the cell increases, e.g., in conditions of active photosynthesis, the tricarboxylic acid (TCA) cycle in mitochondria is transformed to a partial cycle supplying citrate for the synthesis of 2-oxoglutarate and glutamate (citrate valve), while malate is accumulated and participates in the redox balance in different cell compartments (via malate valve). This results in malate and citrate frequently being the most accumulated acids in plants. However, the intensity of reactions linked to the conversion of these compounds can cause preferential accumulation of other organic acids, e.g., fumarate or isocitrate, in higher concentrations than malate and citrate. The secondary reactions, associated with the central metabolic pathways, in particularly with the TCA cycle, result in accumulation of other organic acids that are derived from the intermediates of the cycle. They form the additional pools of fixed carbon and stabilize the TCA cycle. Trans-aconitate is formed from citrate or cis-aconitate, accumulation of hydroxycitrate can be linked to metabolism of 2-oxoglutarate, while 4-hydroxy-2-oxoglutarate can be formed from pyruvate and glyoxylate. Glyoxylate, a product of either glycolate oxidase or isocitrate lyase, can be converted to oxalate. Malonate is accumulated at high concentrations in legume plants. Organic acids play a role in plants in providing redox equilibrium, supporting ionic gradients on membranes, and acidification of the extracellular medium.

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Section: Incomplete Tricarboxylic Acid Cycle and The Operation Of Malmentioning

confidence: 99%

Section: Incomplete Tricarboxylic Acid Cycle and The Operation Of Malmentioning

confidence: 99%

Section: Incomplete Tricarboxylic Acid Cycle and The Operation Of Malmentioning

confidence: 99%

Section: Trans-aconitate – a Stored Tricarboxylic Acid Poolmentioning

confidence: 99%

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Organic Acids: The Pools of Fixed Carbon Involved in Redox Regulation and Energy Balance in Higher Plants

2016

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“…Mitochondrial aconitases are a fundamental part of the Krebs cycle (Sadka et al 2000;Schnarrenberger and Martin 2002;Moeder et al 2007;Terol et al 2010). Although cytosolic aconitases are under-researched as compared with mitochondrial aconitases, they are thought to be involved in numerous processes such as cytosolic citrate metabolism and the glyoxylate cycle (Hayashi et al 1995;Eprintsev et al 2015). Mitochondrial and cytosolic aconitases in plants have similar kinetic properties and are believed to be encoded by the same genes (Carrari et al 2003;Moeder et al 2007).…”

Section: Introductionmentioning

confidence: 99%

Isolation and characterization of Aconitate hydratase 4 (Aco4) from soybean

et al. 2017

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Aconitase catalyzes the reversible isomerization of two tricarboxylic acids, citrate and isocitrate, during the Krebs cycle. Five aconitase genes, namely, Aco1, Aco2, Aco3, Aco4, and Aco5, have been identified in soybean. Previously, Aco4 was mapped on chromosome 11. The purpose of this investigation was to isolate and sequence the candidate gene for Aco4. We mapped the Aco4 gene to a 148 kb region on chromosome 11 that contained 19 predicted genes. One of these, Glyma.11G080600, codes for aconitate hydratase. Sequencing of two isozyme variants (A-line and B-line) for Glyma.11G080600 revealed three synonymous and two non-synonymous substitutions. Perhaps, the two non-synonymous substitutions resulted in a variable isozyme pattern between the variants. Glyma.11G080600 contains a catalytic domain and a swivel domain that are known to catalyze isomerization of citrate to isocitrate and swiveling conformational change in the enzyme mechanism, respectively. Conservation of both the domains implies the role of Glyma.11G080600 in the interconversion of citrate and isocitrate. Glyma.11G080600 is expressed in most tissues, with maximum expression in leaves. Phylogenetic analysis of 25 genes from different species displayed three major clusters. Glyma.11G080600 (Aco4) and Glyma.01G162800, which are conserved in Glycine max (L.) Merr. and Glycine soja Siebold. & Zucc., may have common ancestry before G. max and G. soja split.

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An in‐silico investigation of fluoride ions impact on pancreatic lipase

Yadav

Basha²,

Pindi

2022

J of Cellular Biochemistry

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Fluorine is a halogen beneficial to teeth and bones at a lower concentration. But in excess, it is a toxin and causes adverse effects. Fluoride is toxic to enzymes generally when it inhibits the enzyme activity involved in metabolic pathways. Here we study invitro and invivo findings on the interaction of fluoride on the enzymes Aconitase, Adenylyl cyclase, Arginase, Cytochrome‐c‐oxidase, Glucose‐6‐phosphatase, Protein phosphatase, Succinate dehydrogenase from liver and lipase from pancreas by using molecular docking and simulations to gain insights into the mechanism by which fluoride modifies the activity of pancreatic lipase. our molecular modeling and docking studies identified that lipase is the most strongly inhibited enzyme compared to other enzymes mentioned above with −0.42 Kcal/mol binding energy and 495.78 milli molar of predicted IC50 value with interaction with Phe227 residue. To further validate this, we have taken the lipase enzyme in presence of fluoride ions for molecular dynamic simulations of 100 ns. To analyze the impact of fluoride ions on the lipase dynamics, two different simulations of 100 ns each were performed. In one simulation, we have simulated lipase in its apo form in the aqueous environment without any fluoride ions and in another simulation lipase in its apo form was kept in the presence of randomly placed fluoride ions countered with sodium ions to maintain the pH as neutral. The simulation analysis revealed that major fluctuations in lipase was observed between 230 and 300 residues in presence of fluoride ions. Interestingly, this is the exact location of the “lid” like acting loop of residues responsible for the inward/outward movement of the substrate to lipase catalytically active site containing catalytic triad of residues Leu153, His263, and Pro177. His263 residue random flip is believed to be the critical incident that causes the substrate's inward/outward movement at the catalytically active site coordinated by “lid” opening, providing enough space for the substrate.

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Expression and properties of the mitochondrial and cytosolic forms of aconitase in maize scutellum

Cited by 30 publications

References 38 publications

Organic Acids: The Pools of Fixed Carbon Involved in Redox Regulation and Energy Balance in Higher Plants

Organic Acids: The Pools of Fixed Carbon Involved in Redox Regulation and Energy Balance in Higher Plants

Isolation and characterization of Aconitate hydratase 4 (Aco4) from soybean

An in‐silico investigation of fluoride ions impact on pancreatic lipase

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