Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound

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Query: EC:1.1.1.37 (malate dehydrogenase)
4,591 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The activity of 10 enzymes separated by acrylamide disc gel electrophoresis of leaf and stem extracts from Dianthus grown under summer and winter conditions was studied. While banding was constant and highly reproducible under each environment, differences between the 3 cultivars and between the tissues were evident. No significant differences in the isozyme patterns of glutamate dehydrogenase, 6-phosphogluconate dehydrogenase, glucose-6-phosphate dehydrogenase, malate dehydrogenase, and catalase were observed between the 2 environments. Loss of activity was observed under winter conditions with amylase and lactate dehydrogenase and loss of certain isozymic components was evident with acid phosphatase and esterase. Prominent changes were observed in peroxidase isozymes, the hardy cultivars developing additional isozymic components under winter conditions. Only minor changes in the total protein banding were seen. The enzymes showed considerable stability in those tissues killed by the freezing conditions.
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PMID:Plant Leaf and Stem Proteins. II. Isozymes and Environmental Cabbage. 1665 48

The levels of 18 enzymes were determined in leaves, stems, and roots of 11-day-old pea seedlings grown in a liquid medium or in the same medium containing, in addition, 5 atmospheres of either NaCl, KCl, Na(2)SO(4), or K(2)SO(4). Though the plants grown in saline media were stunted, the specific activities of the enzymes were the same in the given tissues of all plants. Also, the electrophoretic pattern of isozymes of malate dehydrogenase was not altered by growth of the plants in a saline medium. However, the isozyme pattern of peroxidase from roots of salt-grown plants was altered in that two of the five detectable isozymes migrated a little more slowly than those in extracts from nonsaline plant tissues.
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PMID:Enzyme levels in pea seedlings grown on highly salinized media. 1665 88

The activities of three enzymes of phenolic biosynthesis and six of general metabolism were studied at 24-hour intervals between the 3rd and 8th day after planting in barley shoots treated with the chlorosis-inducing herbicide Sandoz 6706 and grown in the dark or under high or low intensity light. The herbicide had no effect on fresh weight or soluble protein (per shoot) in plants grown in the dark or under low intensity light, but slightly decreased these parameters in plants grown for more than 5 days under high intensity light. In dark-grown seedlings the herbicide had no detectable effects on plastid ultrastructure or on the activity of malate dehydrogenase, cytochrome c oxidase, NADP-cytochrome c reductase, triose phosphate isomerase, peroxidase, catalase, shikimate dehydrogenase, phenylalanine ammonia-lyase, or chalcone-flavanone isomerase. Under low intensity light, Sandoz 6706-treated plants developed plastids with single thylakoids extending across the organelle, and the activity of all enzymes examined was increased to varying degrees. When the herbicide-treated plants were grown under high intensity light, plastid lamellar organization was severely disrupted. Activities of shikimate dehydrogenase and chalcone-flavanone isomerase were markedly enhanced, phenylalanine ammonia-lyase activity slightly promoted, and catalase activity severely inhibited. The other enzymes were not appreciably affected by Sandoz 6706 under high intensity light. It is concluded that the changes in plastid ultrastructure and enzyme activities of the herbicide-treated plants are largely secondary photomorphogenetic or photooxidative responses in the carotenoid-free plants in which chlorophylls accumulate in reduced amounts (low intensity light) or are completely absent (high intensity light).
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PMID:Developmental Effects of Sandoz 6706 on Activities of Enzymes of Phenolic and General Metabolism in Barley Shoots Grown in the Dark or under Low or High Intensity Light. 1666 Nov 67

When the protoplasts of peeled oat leaf segments (Avena sativa L.) expand after a brief plasmolysis (osmotic shock), fusicoccin-enhanced H(+) excretion is reduced and protein is released to the rehydration medium. This shock protein seems to arise from the cell surface, not from the interior of leaky cells or from broken cells, because (a) the protein differs quantitatively and qualitatively from protein of cell homogenates as determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis; (b) peroxidase, phosphatase, and malate dehydrogenase activities, which are associated with the cell surface, are detected in the shock fluids; (c) the specific activities of enzymes in shock fluids are different than those of cell homogenates; (d) the amount of protein released is correlated with tissue mass, not number of cut surfaces and is not diminished by pre-washing the tissue.Some of the shock protein may arise from plasmodesmata; this suggestion is based on (a) the cell surface origin of the protein; (b) the presence in the shock fluid of NADPH-cytochrome c reductase activity, usually associated with the endoplasmic reticulum which traverses plasmodesmata; (c) on the release of smaller amounts of protein after plasmolysis with polyethylene glycol 4000, an osmoticum which may tend to preserve plasmodesmata.The amount of protein released by osmotic shock is correlated with the extent of inhibition of fusicoccin-enhanced H(+) excretion. A specific function for the shock protein is implied by the presence of a component which specifically binds fusicoccin.
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PMID:Regulation of H Excretion : ROLE OF PROTEIN RELEASED BY OSMOTIC SHOCK. 1666 24

An intercellular washing solution containing about 1% of the soluble protein, 0.3% or less of the glucose-6-phosphate dehydrogenase activity, but up to 20% of the peroxidase and beta-d-glucosidase activity of barley (Hordeum vulgare L.) or oat (Avena sativa L.) primary leaves was obtained by vacuum infiltrating peeled leaves with pH 6.9 buffered 200 millimolar NaCl. After this wash, segments were homogenized in buffer, centrifuged, and the supernatant was assayed for soluble cytoplasmic enzymes. The pellet was washed and resuspended in 1 molar NaCl to solubilize enzymes strongly ionically bound to the cell wall. The final pellet was assayed for enzyme activity covalently bound in the cell wall. Apoplastic (intercellular washing solution, ionically bound, and covalently bound) fractions contained up to 76% of the beta-d-glucosidase activity, 36% of the peroxidase activity, 11% of the nonspecific arylesterase activity, 4% of the malate dehydrogenase activity, but less than 2% of the glucose-6-phosphate dehydrogenase activity of peeled leaf segments. The partitioning and salt-solubility of the enzymes between the apoplast and symplast differed considerably between these two species. Intercellular washing fluid prepared by centrifuging unpeeled leaves had higher activity for glucose-6-phosphate dehydrogenase, less soluble protein, and less peroxidase activity per leaf than intercellular washing solution obtained by our peeling-infiltration-washing technique. The results are discussed in relation to the roles of these enzymes in phenolic metabolism in the cell wall.
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PMID:Soluble and Bound Apoplastic Activity for Peroxidase, beta-d-Glucosidase, Malate Dehydrogenase, and Nonspecific Arylesterase, in Barley (Hordeum vulgare L.) and Oat (Avena sativa L.) Primary Leaves. 1666 33

Differential resistance to metal pollution in Daphnia longispina populations was reported in previous studies. In this work, we tried to determine if variation in polymorphic enzymes, often referred as being under metal selection, were related with differences in resistance to acute single- and mixed-metal exposure. Allozyme genotype of 20 putatively polymorphic enzymes, 48-h median lethal concentration (LC50) for copper, and median lethal time (LT50) for a 3% dilution of acid mine drainage (AMD) were determined for 24 lineages of D. longispina. The copper LC50s ranged from 29.3 to 226 microg/L, and the AMD LT50s ranged from 48 min to 25 h and 29 min, with a strong correlation between both end points. Five distinct multilocus genotypes were identified based on polymorphisms in glucose-6-phosphate isomerase, lactate dehydrogenase, malate dehydrogenase, nicotinamide adenine dinucleotide phosphate (NADP+), phosphoglucomutase, and peroxidase. No differences were found in average genotype sensitivity for both toxicity end points or in genotype frequencies between the resistant- and sensitive-lineage groups. The results obtained indicate that allozyme genotype is not associated with increased resistance to acute metal stress in D. longispina.
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PMID:Differential resistance to copper and mine drainage in Daphnia longispina: relationship with allozyme genotypes. 1770 44

Addition of chitosan or H2O2 caused destruction of nuclei of epidermal cells (EC) in the epidermis isolated from pea leaves. Phenol, a substrate of the apoplastic peroxidase-oxidase, in concentrations of 10(-10)-10(-6) M prevented the destructive effect of chitosan. Phenolic compounds 2,4-dichlorophenol, catechol, and salicylic acid, phenolic uncouplers of oxidative phosphorylation pentachlorophenol and 2,4-dinitrophenol, and a non-phenolic uncoupler carbonyl cyanide m-chlorophenylhydrazone, but not tyrosine or guaiacol, displayed similar protective effects. A further increase in concentrations of the phenolic compounds abolished their protective effects against chitosan. Malate, a substrate of the apoplastic malate dehydrogenase, replenished the pool of apoplastic NADH that is a substrate of peroxidase-oxidase, prevented the chitosan-induced destruction of the EC nuclei, and removed the deleterious effect of the increased concentration of phenol (0.1 mM). Methylene Blue, benzoquinone, and N,N,N',N'-tetramethyl-p-phenylenediamine (TMPD) capable of supporting the optimal catalytic action of peroxidase-oxidase cancelled the destructive effect of chitosan on the EC nuclei. The NADH-oxidizing combination of TMPD with ferricyanide promoted the chitosan-induced destruction of the nuclei. The data suggest that the apoplastic peroxidase-oxidase is involved in the antioxidant protection of EC against chitosan and H2O2.
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PMID:Programmed cell death in plants: protective effect of phenolic compounds against chitosan and H2O2. 2036 14

By using aeroponics culture system, this paper studied the impacts of root-zone hypoxia (10% O2 and 5% O2) stress on the plant growth, root respiratory metabolism, and antioxidative enzyme activities of muskmelon at its fruit development stage. Root-zone hypoxia stress inhibited the plant growth of muskmelon, resulting in the decrease of plant height, root length, and fresh and dry biomass. Comparing with the control (21% O2), hypoxia stress reduced the root respiration rate and malate dehydrogenase (MDH) activity significantly, and the impact of 5% O2 stress was more serious than that of 10% O2 stress. Under hypoxic conditions, the lactate dehydrogenase (LDH), alcohol dehydrogenase (ADH), pyruvate decarboxylase (PDC), superoxide dismutase (SOD), peroxidase (POD), and catalase (CAT) activities and the malondialdehyde (MDA) content were significantly higher than the control. The increment of antioxidative enzyme activities under 10% O2 stress was significantly higher than that under 5% O2 stress, while the MDA content was higher under 5% O2 stress than under 10% O2 stress, suggesting that when the root-zone oxygen concentration was below 10%, the aerobic respiration of muskmelon at its fruit development stage was obviously inhibited while the anaerobic respiration was accelerated, and the root antioxidative enzymes induced defense reaction. With the increasing duration of hypoxic stress, the lipid peroxidation would be aggravated, resulting in the damages on muskmelon roots, inhibition of plant growth, and decrease of fruit yield and quality.
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PMID:[Impacts of root-zone hypoxia stress on muskmelon growth, its root respiratory metabolism, and antioxidative enzyme activities]. 2087 18

Legumes have the ability to form root nodules that fix atmospheric nitrogen through a symbiotic interaction with nitrogen-fixing bacteria. As a first step in dissecting the molecular process of nodulation, proteome reference maps of soybean roots and nodules were constructed. Time course analysis revealed that the transition from root to nodule was accompanied with downregulation of defense-response related proteins, including Mn-superoxide dismutase, peroxidase (Prx), PR10, and stress-induced protein, leading to the initiation of a symbiotic interaction between the two partners. Following nitrogenase biosynthesis, the host plant cooperated with the rhizobia to fix atmospheric nitrogen under microaerobic conditions via expression of leghemoglobins and antioxidant proteins. Comparative proteome analysis indicated lower expression of malate dehydrogenase (MDH), leghemoglobins and nitrogenase in the nodule development of the supernodulation mutant, SS2-2, as compared to the wild type, indicating that SS2-2 forms functionally immature nodules in higher numbers with the lower activity of nitrogen fixation.
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PMID:Comparative proteomic analysis of soybean nodulation using a supernodulation mutant, SS2-2. 2115 Jan 21

Peroxiredoxins are antioxidative enzymes that catalyze the reduction of alkyl hydroperoxides to alcohols and hydrogen peroxide to water. 1-Cys peroxiredoxins (1-Cys Prxs) perform important roles during late seed development in plants. To characterize their biochemical functions in plants, a 1Cys-Prx gene was cloned from a Chinese cabbage cDNA library and designated as "C1C-Prx". Glutamine synthetase (GS) protection and hydrogen peroxide reduction assays indicated that C1C-Prx was functionally active as a peroxidase. Also C1C-Prx prevented the thermal- or chemical-induced aggregation of malate dehydrogenase and insulin. Hydrogen peroxide treatment changed the mobility of C1C-Prx on a two-dimensional gel, which implies overoxidation of the conserved Cys residue. Furthermore, after overoxidation, the chaperone activity of C1C-Prx increased approximately two-fold, but its peroxidase activity decreased to the basal level of the reaction mixture without enzyme. However, according to the structural analysis using far-UV circular dichroism spectra, intrinsic tryptophan fluorescence spectra, and native-PAGE, overoxidation did not lead to a conformational change in C1C-Prx. Therefore, our results suggest that 1-Cys Prxs function not only to relieve mild oxidative stresses but also as molecular chaperones under severe conditions during seed germination and plant development, and that overoxidation controls the switch in function of 1-Cys-Prxs from peroxidases to molecular chaperones.
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PMID:The 1-Cys peroxiredoxin, a regulator of seed dormancy, functions as a molecular chaperone under oxidative stress conditions. 2168 76


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