Relevant bibliographies by topics / Glutamate and malate dehydrogenases

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Academic literature on the topic 'Glutamate and malate dehydrogenases'

Author: Grafiati
Published: 3 June 2025
Last updated: 23 June 2025

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Journal articles on the topic "Glutamate and malate dehydrogenases"

1

Czosnowski, J. "Metabolism of excised embryos of Lupinus luteus L. VI. An electrophoretic analysis of some dehydrogenases in cultured embryos as compared with the normal seedling axes." Acta Societatis Botanicorum Poloniae 43, no. 1 (2015): 117–27. http://dx.doi.org/10.5586/asbp.1974.011.

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The electrophoretic patterns (disc electrophoresis) of the studied dehydrogenases: glucose-6-phosphate - (A), malate - (B), glutamate - (C), alcohol - (D) and lactate dehydrogenase (E), in the axial organs of isolated <i>Lupinus luteus</i> embryos and seedlings cultivated over 12 days are characterized by great similarities. With time, after the third day of cultivation the patterns begin to become less deyeloped. Analyses performed during the first 10 hours of imbibition of seed parts indicate that the maximal development of isozyme patterns occurs during the third hour after which the patterns become poorer. The most uniform type of pattern. and the lowest number of isozymes was shown by glutamate dehydrogenase, the richest pattern was shown by malate dehydrogenase. No band common for a 11 the 27 experimental elements was found.
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2

Thome, Trace, Zachary R. Salyers, Ravi A. Kumar, et al. "Uremic metabolites impair skeletal muscle mitochondrial energetics through disruption of the electron transport system and matrix dehydrogenase activity." American Journal of Physiology-Cell Physiology 317, no. 4 (2019): C701—C713. http://dx.doi.org/10.1152/ajpcell.00098.2019.

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Chronic kidney disease (CKD) leads to increased skeletal muscle fatigue, weakness, and atrophy. Previous work has implicated mitochondria within the skeletal muscle as a mediator of muscle dysfunction in CKD; however, the mechanisms underlying mitochondrial dysfunction in CKD are not entirely known. The purpose of this study was to define the impact of uremic metabolites on mitochondrial energetics. Skeletal muscle mitochondria were isolated from C57BL/6N mice and exposed to vehicle (DMSO) or varying concentrations of uremic metabolites: indoxyl sulfate, indole-3-acetic-acid, l-kynurenine, and kynurenic acid. A comprehensive mitochondrial phenotyping platform that included assessments of mitochondrial oxidative phosphorylation (OXPHOS) conductance and respiratory capacity, hydrogen peroxide production ( JH2O2), matrix dehydrogenase activity, electron transport system enzyme activity, and ATP synthase activity was employed. Uremic metabolite exposure resulted in a ~25–40% decrease in OXPHOS conductance across multiple substrate conditions ( P < 0.05, n = 5–6/condition), as well as decreased ADP-stimulated and uncoupled respiratory capacity. ATP synthase activity was not impacted by uremic metabolites; however, a screen of matrix dehydrogenases indicated that malate and glutamate dehydrogenases were impaired by some, but not all, uremic metabolites. Assessments of electron transport system enzymes indicated that uremic metabolites significantly impair complex III and IV. Uremic metabolites resulted in increased JH2O2 under glutamate/malate, pyruvate/malate, and succinate conditions across multiple levels of energy demand (all P < 0.05, n = 4/group). Disruption of mitochondrial OXPHOS was confirmed by decreased respiratory capacity and elevated superoxide production in cultured myotubes. These findings provide direct evidence that uremic metabolites negatively impact skeletal muscle mitochondrial energetics, resulting in decreased energy transfer, impaired complex III and IV enzyme activity, and elevated oxidant production.
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3

Lietz, T., K. Winiarska, and J. Bryła. "Ketone bodies activate gluconeogenesis in isolated rabbit renal cortical tubules incubated in the presence of amino acids and glycerol." Acta Biochimica Polonica 44, no. 2 (1997): 323–31. http://dx.doi.org/10.18388/abp.1997_4428.

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In isolated rabbit renal kidney-cortex tubules 2 mM glycerol, which is a poor gluconeogenic substrate, does not induce glucose formation in the presence of alanine, while it activates gluconeogenesis on substitution of alanine by aspartate, glutamate or proline. The addition of either 5 mM 3-hydroxybutyrate or 5 mM acetoacetate to renal tubules incubated with alanine + glycerol causes a marked induction of glucose production associated with inhibition of glutamine synthesis. In contrast, the rate of the latter process is not altered by ketones in the presence of glycerol and either aspartate, glutamine or proline despite the stimulation of glucose formation. Acceleration of gluconeogenesis by ketone bodies in the presence of amino acids and glycerol is probably due to (i) stimulation of pyruvate carboxylase activity, (ii) activation of malate-aspartate shuttle as concluded from elevated intracellular levels of malate, aspartate and glutamate, as well as (iii) diminished supply of ammonium for glutamine synthesis from alanine resulting from a decrease in glutamate dehydrogenase activity.
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4

Bryce, JH, and JT Wiskich. "Effect of NAD and Rotenone on the Partitioning of Malate Oxidation Between Malate Dehydrogenase and Malic Enzyme in Isolated Plant Mitochondria." Functional Plant Biology 12, no. 3 (1985): 229. http://dx.doi.org/10.1071/pp9850229.

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Our aim was to determine whether there is a specific link between NAD-malic enzyme and the rotenone- insensitive bypass of electron transport. Mitochondria were isolated from fresh beetroot tissue, aged beetroot slices, and turnips. Oxygen uptake and pyruvate production were measured in reactions where these mitochondria were metabolizing malate at pH 6.8 in the presence of glutamate, to facilitate the removal of oxaloacetate, and in its absence. In the absence of glutamate there was substantial activity of malic enzyme. NAD+ (577 �M) prevented a fall in oxygen uptake by stimulating malic enzyme. Rotenone (19 �M) reduced oxygen uptake. This inhibited rate was stimulated by NAD+ due, in particular, to a stimulation of malic enzyme. We conclude that the stimulation of malate metabolism by NAD+ is accounted for by malic enzyme due to the unfavourable equilibrium of malate dehydrogenase for malate oxidation and the resultant accumulation of oxaloacetate, and not to any specific link between malic enzyme and the rotenone-insensitive bypass. In the presence of glutamate, malate dehydrogenase was the predominant malate metabolizing enzyme. Oxygen uptake and malic enzyme were stimulated and inhibited by NAD+ and rotenone, respectively. In the presence of rotenone, NAD+ stimulated oxygen uptake and increased the percentage due to malic enzyme. This stimulation is accounted for by the higher Kin of the rotenone-insensitive dehydrogenase for NADH and the unfavourable equilibrium position of malate dehydrogenase resulting in activation of malic enzyme only. We conclude that malic enzyme is not specifically linked to the rotenone-insensitive pathway of electron transport. This has important implications for the regulation of energy metabolism in plants.
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5

Scaduto, R. C., and A. C. Schoolwerth. "Effect of bicarbonate on glutamine and glutamate metabolism by rat kidney cortex mitochondria." American Journal of Physiology-Renal Physiology 249, no. 4 (1985): F573—F581. http://dx.doi.org/10.1152/ajprenal.1985.249.4.f573.

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Isolated rat kidney cortex mitochondria were incubated at pH 7.4 in the presence or absence of a CO2/bicarbonate buffer (28 mM) to investigate the pH-independent role of bicarbonate on glutamine and glutamate metabolism. Changes in the concentration of key intermediates and products during the incubations were used to calculate metabolite flux rates through specific mitochondrial enzymes. With 1 mM glutamine and 2 mM glutamate as substrates, bicarbonate caused an inhibition of glutamate oxalacetate transaminase flux and a stimulation of glutamate deamination. The same effects were also produced with addition of either aminooxyacetate or malonate. These effects of bicarbonate were prevented when 0.2 mM malate was included as an additional substrate. Bicarbonate ion was identified as a potent competitive inhibitor of rat kidney cortex succinate dehydrogenase. These results indicate that aminooxyacetate, malonate, and bicarbonate all act to stimulate glutamate deamination through a suppression of glutamate transamination, and that the control by transamination of glutamate deamination is due to alterations in alpha-ketoglutarate metabolism. In contrast, in mitochondria incubated with glutamine in the absence of glutamate, bicarbonate was found to inhibit glutamate dehydrogenase flux. This effect was found to be due in part to the lower intramitochondrial pH observed in incubations with bicarbonate. These findings indicate that bicarbonate ion, independent of pH, may have an important regulatory role in renal glutamine and glutamate metabolism.
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6

Starritt, Emma C., Damien Angus, and Mark Hargreaves. "Effect of short-term training on mitochondrial ATP production rate in human skeletal muscle." Journal of Applied Physiology 86, no. 2 (1999): 450–54. http://dx.doi.org/10.1152/jappl.1999.86.2.450.

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Seven untrained volunteers [3 men, 4 women, 20.1 ± 2.0 (SD) yr, 66.0 ± 11.0 kg, 171 ± 13 cm] participated in a 10-day cycle exercise training program. Resting muscle samples were obtained from vastus lateralis before and after 5 and 10 days of training. Mitochondrial ATP production rate (MAPR) was assayed in isolated mitochondria by using a bioluminescence technique and referenced to the activity of glutamate dehydrogenase in the muscle sample. MAPR increased 136 and 161% after 10 days of training for the mitochondrial substrate combinations pyruvate + palmitoyl-l-carnitine + α-ketoglutarate + malate and palmitoyl-l-carnitine + malate, respectively. Total muscle glutamate dehydrogenase and citrate synthase activity increased 53 and 16%, respectively, after 5 days but did not significantly increase further after 10 days. The results from the present study indicate that MAPR, measured by using the substrate combinations pyruvate + palmitoyl-l-carnitine + α-ketoglutarate + malate and palmitoyl-l-carnitine + malate, can rapidly increase in response to endurance training.
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7

Mezhenska, O. A., V. A. Aleshin, T. Kaehne, A. V. Artiukhov, and V. I. Bunik. "Regulation of Malate Dehydrogenases and Glutamate Dehydrogenase of Mammalian Brain by Thiamine in vitro and in vivo." Biochemistry (Moscow) 85, no. 1 (2020): 27–39. http://dx.doi.org/10.1134/s0006297920010034.

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8

Katyare, S. S., C. S. Bangur, and J. L. Howland. "Is respiratory activity in the brain mitochondria responsive to thyroid hormone action?: a critical re-evaluation." Biochemical Journal 302, no. 3 (1994): 857–60. http://dx.doi.org/10.1042/bj3020857.

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The effects of in vivo treatment with graded doses (0.5-1.5 micrograms/g body weight) of thyroid hormones, tri-iodothyronine (T3) and thyroxine (T4), for 4 consecutive days to euthyroid rats on the respiratory activity of isolated brain mitochondria were examined. T4 stimulated coupled State-3 respiration with glutamate, pyruvate + malate, ascorbate + tetramethyl-p-phenylenediamine and succinate, in a dose-dependent manner; T3 was effective only at the highest (1.5 micrograms) dose employed. T4 was more effective than T3 in stimulating respiratory activity. State-4 respiratory rates were in general not influenced except in the case of the ascorbate + tetramethyl-p-phenylenediamine system. Primary dehydrogenase activities, i.e. glutamate dehydrogenase, malate dehydrogenase and succinate dehydrogenase, were stimulated about 2-fold; interestingly mitochondrial but not cytosolic malate dehydrogenase activity was influenced under these conditions. The hormone treatments did not greatly influence the mitochondrial cytochrome content. The results therefore suggest that thyroid hormone treatment not only stimulates primary dehydrogenase activities but may also directly influence the process of mitochondrial electron transfer.
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9

Artiukhov, Artem V., Anastasia V. Graf, Alexey V. Kazantsev, et al. "Increasing Inhibition of the Rat Brain 2-Oxoglutarate Dehydrogenase Decreases Glutathione Redox State, Elevating Anxiety and Perturbing Stress Adaptation." Pharmaceuticals 15, no. 2 (2022): 182. http://dx.doi.org/10.3390/ph15020182.

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Specific inhibitors of mitochondrial 2-oxoglutarate dehydrogenase (OGDH) are administered to animals to model the downregulation of the enzyme as observed in neurodegenerative diseases. Comparison of the effects of succinyl phosphonate (SP, 0.02 mmol/kg) and its uncharged precursor, triethyl succinyl phosphonate (TESP, 0.02 and 0.1 mmol/kg) reveals a biphasic response of the rat brain metabolism and physiology to increasing perturbation of OGDH function. At the low (TE)SP dose, glutamate, NAD+, and the activities of dehydrogenases of 2-oxoglutarate and malate increase, followed by their decreases at the high TESP dose. The complementary changes, i.e., an initial decrease followed by growth, are demonstrated by activities of pyruvate dehydrogenase and glutamine synthetase, and levels of oxidized glutathione and citrulline. While most of these indicators return to control levels at the high TESP dose, OGDH activity decreases and oxidized glutathione increases, compared to their control values. The first phase of metabolic perturbations does not cause significant physiological changes, but in the second phase, the ECG parameters and behavior reveal decreased adaptability and increased anxiety. Thus, lower levels of OGDH inhibition are compensated by the rearranged metabolic network, while the increased levels induce a metabolic switch to a lower redox state of the brain, associated with elevated stress of the animals.
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10

Hung, Hui-Chih, Meng-Wei Kuo, Gu-Gang Chang, and Guang-Yaw Liu. "Characterization of the functional role of allosteric site residue Asp102 in the regulatory mechanism of human mitochondrial NAD(P)+-dependent malate dehydrogenase (malic enzyme)." Biochemical Journal 392, no. 1 (2005): 39–45. http://dx.doi.org/10.1042/bj20050641.

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Human mitochondrial NAD(P)+-dependent malate dehydrogenase (decarboxylating) (malic enzyme) can be specifically and allosterically activated by fumarate. X-ray crystal structures have revealed conformational changes in the enzyme in the absence and in the presence of fumarate. Previous studies have indicated that fumarate is bound to the allosteric pocket via Arg67 and Arg91. Mutation of these residues almost abolishes the activating effect of fumarate. However, these amino acid residues are conserved in some enzymes that are not activated by fumarate, suggesting that there may be additional factors controlling the activation mechanism. In the present study, we tried to delineate the detailed molecular mechanism of activation of the enzyme by fumarate. Site-directed mutagenesis was used to replace Asp102, which is one of the charged amino acids in the fumarate binding pocket and is not conserved in other decarboxylating malate dehydrogenases. In order to explore the charge effect of this residue, Asp102 was replaced by alanine, glutamate or lysine. Our experimental data clearly indicate the importance of Asp102 for activation by fumarate. Mutation of Asp102 to Ala or Lys significantly attenuated the activating effect of fumarate on the enzyme. Kinetic parameters indicate that the effect of fumarate was mainly to decrease the Km values for malate, Mg2+ and NAD+, but it did not notably elevate kcat. The apparent substrate Km values were reduced by increasing concentrations of fumarate. Furthermore, the greatest effect of fumarate activation was apparent at low malate, Mg2+ or NAD+ concentrations. The Kact values were reduced with increasing concentrations of malate, Mg2+ and NAD+. The Asp102 mutants, however, are much less sensitive to regulation by fumarate. Mutation of Asp102 leads to the desensitization of the co-operative effect between fumarate and substrates of the enzyme.
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Dissertations / Theses on the topic "Glutamate and malate dehydrogenases"

1

Jackson, Richard Michael. "A theoretical investigation into the properties of lactate and malate dehydrogenases." Thesis, University of Bristol, 1992. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.282473.

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Morgan, Megan Jayne. "Identification of molecular-genetic determinants of quality traits of tomato fruit." Thesis, University of Oxford, 2011. http://ora.ox.ac.uk/objects/uuid:662d8b1e-70cf-44fb-9ed3-46dcacc39bad.

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Tomato is an important food crop and a model for fleshy fruit development. The process of fruit ripening involves changes in chemical composition and in particular the accumulation of sugars, organic, amino acids and carotenes. The research described in this thesis aimed to identify key regulatory aspects associated with the accumulation of the major acids in tomato fruit by analysis of introgression lines resulting from a cross between a cultivated variety, Solanum lycopersicum, and a wild progenitor species, Solanum pennellii. Line 2-5 showed increases in citrate, malate, aspartate and glutamate in fruit grown under greenhouse conditions. The genetic differences between line 2-5, its overlapping lines, sub-introgression lines and the recurrent parent were used to link the metabolite phenotypes to smaller chromosomal regions. This analysis suggested multiple epistatic loci control fruit metabolite accumulation. Investigation of the biochemical differences between line 2-5 and the recurrent parent revealed that organic and amino acid accumulation did not dependent upon increased TCA cycle capacity. Regulation at the metabolic level was identified for citrate accumulation with changes in cytosolic aconitase in line 2-5. As these metabolites accumulate in the vacuole, tonoplast transport was investigated. Correlation of ATPase-dependent malate influx with altered malate content suggested malate tonoplast transport plays a role in malate accumulation and highlights the importance of vacuolar storage and transport in the regulation of organic and amino acid accumulation.
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Mai, Sha Li, and 麥莎麗. "Thermal adaptation of cytoplasmic malate dehydrogenases on grass carp, ctenopharyngodon idella." Thesis, 1994. http://ndltd.ncl.edu.tw/handle/27265213160074794531.

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Books on the topic "Glutamate and malate dehydrogenases"

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Wynne, S. A. Malate dehydrogenases from the thermophilic organisms bacillusisraeli and pyrobaculum icelandicum. UMIST, 1994.

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2

Storts, Douglas Ray. Purification and properties of a-Aminoadipate semialdehyde dehydrogenase and saccharopine dehydrogenase (glutamate-forming): From Saccharomyces cerevisiae and identification of the structural genes encoding a-Aminoadipate semialdehyde dehydrogenase. 1985.

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Book chapters on the topic "Glutamate and malate dehydrogenases"

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Steen, Ida Helene, Hilde Hvoslef, Torleiv Lien, and Nils-Kåre Birkeland. "[2] Isocitrate dehydrogenase, malate dehydrogenase, and glutamate dehydrogenase from Archaeoglobus fulgidus." In Hyperthermophilic enzymes Part B. Elsevier, 2001. http://dx.doi.org/10.1016/s0076-6879(01)31043-1.

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Santero, Eduardo, Ana B., Ines Canosa, and Fernando Govantes. "Glutamate Dehydrogenases: Enzymology, Physiological Role and Biotechnological Relevance." In Dehydrogenases. InTech, 2012. http://dx.doi.org/10.5772/47767.

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3

Friday, Ellen, Robert Oliver, Francesco Turturro, and Tomas Welbourne. "Role of Glutamate Dehydrogenase in Cancer Growth and Homeostasis." In Dehydrogenases. InTech, 2012. http://dx.doi.org/10.5772/48606.

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Robb, Frank T., Dennis L. Maeder, Jocelyne Diruggiero, Kim M. Borges, and Niccola Tolliday. "[3] Glutamate dehydrogenases from hyperthermophiles." In Hyperthermophilic enzymes Part B. Elsevier, 2001. http://dx.doi.org/10.1016/s0076-6879(01)31044-3.

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5

Frey, Perry A., and Adrian D. Hegeman. "Oxidoreductases." In Enzymatic Reaction Mechanisms. Oxford University Press, 2007. http://dx.doi.org/10.1093/oso/9780195122589.003.0020.

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Oxidoreductases constitute a very large class of enzymes. They are dehydrogenases and reductases that catalyze the removal or addition of the elements of molecular hydrogen to or from substrates. Enzymatic dehydrogenation is sometimes linked to auxiliary functions such as decarboxylation, deamination, or dehydration of the substrate, as in the actions of isocitrate dehydrogenase (decarboxylation), glutamate dehydrogenase (deamination), and ribonucleotide reductase (deoxygenation). The best known oxidoreductases are the NAD-dependent dehydrogenases, and a thorough discussion of the actions of these enzymes could easily fill a volume the size of this book. For this reason, this discussion must focus on the salient aspects of reaction mechanisms that represent the major classes of oxidoreductases. Authoritative reviews on the kinetics and structures of the main dehydrogenases are available (Banaszak et al., 1975; Brändén et al., 1975; Dalziel, 1975; Harris and Waters, 1976; Holbrook et al., 1975; Rossman et al., 1975; Smith et al., 1975; Williams, 1976). In this chapter, we emphasize the diverse oxidoreduction mechanisms and place less emphasis on auxiliary functions such as decarboxylation, the mechanisms of which are similar to the actions of enzymes discussed in earlier chapters of this book. Discussions of several dehydrogenases not included in this chapter can be found in other chapters. These include methanol, glucose, and methylamine dehydrogenases in chapter 3, dimethylsulfoxide reductase in chapter 4, and dihydrofolate reductase and β-hydroxymethylglutaryl CoA reductase in chapter 5. Pyruvate and α-ketoglutarate dehydrogenases are discussed in chapter 18. Enzymatic addition or removal of the elements of hydrogen to or from an organic molecule generally requires the action of a coenzyme. In principle, the process may proceed by any of several mechanisms, including the formal transfer of a hydride and a proton; or the transfer of two electrons and two protons; or the transfer of a hydrogen atom, an electron, and a proton; or any of several other sequences. Proteins alone do not efficiently catalyze these processes; coenzymes and cofactors generally provide the essential chemistry for catalysis by oxidoreductases. Many enzymes catalyze the dehydrogenation of an alcoholic group to a ketone or aldehyde coupled with the reduction of NAD+ to NADH.
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