Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:4.1.2.13 (aldolase)
 3,461 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Crenate broomrape (Orobanche crenata) is a parasitic plant that threatens legume production in Mediterranean areas. Pea (Pisum sativum) is severely affected, and only moderate levels of genetic resistance have so far been identified. In the present work we selected the most resistant accession available (Ps 624) and compared it with a susceptible (Messire) cultivar. Experiments were performed by using pot and Petri dish bioassays, showing little differences in the percentage of broomrape seed germination induced by both genotypes, but a significant hamper in the number of successfully installed tubercles and their developmental stage in the Ps 624 compared to Messire. The protein profile of healthy and infected P. sativum root tissue were analysed by two-dimensional electrophoresis. Approximately 500 individual protein spots could be detected on silver stained gels. At least 22 different protein spots differentiated control, non-infected, Messire and Ps 624 accessions. Some of them were identified by MALDI-TOF mass spectrometry and database searching as cysteine proteinase, beta-1,3-glucanase, endochitinase, profucosidase, and ABA-responsive protein. Both qualitative and quantitative differences have been found among infected and non-infected root extracts. Thus, in the infected susceptible Messire genotype 34 spots were decreased, one increased and three newly detected, while in Ps 624, 15 spots were increased, three decreased and one newly detected. In response to the inoculation, proteins that correspond to enzymes of the carbohydrate metabolism (fructokinase, fructose-bisphosphate aldolase), nitrogen metabolism (ferredoxin-NADP reductase) and mitochondrial electronic chain transport (alternative oxidase 2) decreased in the susceptible check, while proteins that correspond to enzymes of the nitrogen assimilation pathway (glutamine synthetase) or typical pathogen defence, PR proteins, including beta-1,3-glucanase and peroxidases, increased in Ps 624. Results are discussed in terms of changes in the carbohydrate and nitrogen metabolism an induction of defence proteins in response to broomrape parasitism.
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PMID:A proteomic approach to studying plant response to crenate broomrape (Orobanche crenata) in pea (Pisum sativum). 1527 40

Cells of Picrophilus torridus, grown on glucose, contained all enzyme activities of a non-phosphorylative Entner-Doudoroff pathway, including glucose dehydrogenase, gluconate dehydratase, 2-keto-3-deoxygluconate aldolase, glyceraldehyde dehydrogenase (GADH), glycerate kinase (2-phosphoglycerate forming), enolase and pyruvate kinase. GADH was purified to homogeneity. The 115-kDa homodimeric protein catalyzed the oxidation of glyceraldehyde with NADP+ at highest catalytic efficiency. NAD+ was not used. By MALDI-TOF analysis, open reading frame (ORF) Pto0332 was identified in the genome of P. torridus as the encoding gene, designated gadh, and the recombinant GADH was characterized. In Thermoplasma acidophilum ORF Ta0809 represents a gadh homolog with highest sequence identity; the gene was expressed and the recombinant protein was characterized as functional GADH with properties very similar to the P. torridus enzyme. Sequence comparison and phylogenetic analysis define both GADHs as members of novel enzyme family within the aldehyde dehydrogenase superfamily.
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PMID:Glyceraldehyde dehydrogenases from the thermoacidophilic euryarchaeota Picrophilus torridus and Thermoplasma acidophilum, key enzymes of the non-phosphorylative Entner-Doudoroff pathway, constitute a novel enzyme family within the aldehyde dehydrogenase superfamily. 1645 4

Photosynthetic and respiratory activities have been measured in leaves of Hordeum vulgare L. var. Manchuria (barley) after infection with Erysiphe graminis var. hordei (powdery mildew). Two isogenic lines, one resistant to infection and the other highly susceptible, were examined.These isogenic lines showed very different physiological responses following infection. Photosynthesis and the chlorophyll content of resistant leaves was unaffected by infection. Respiration increased slightly and this was accompanied by small increases in activities of enzymes of glycolysis, the pentose-P pathway and the tricarboxylic acid cycle.The infection of susceptible leaves resulted in a slight increase in photosynthesis 48 hours after inoculation, but subsequently there was a progressive decrease in the photosynthesis of these leaves compared with that of noninfected leaves. The capacity of infected leaves for partial reactions of photosynthesis such as the Hill reaction and the photoreduction of nicotinamide adenine dinucleotide phosphate (NADP(1)) decreased during the later stages of infection. The levels of chlorophyll, NADPH-diaphorase and aldolase also declined. There was no detectable difference in the respiration of infected and noninfected leaves until 48 hours after inoculation. After this time, the infected leaves showed a higher respiration, the maximum difference occurring about 144 hours after inoculation. The respiratory increase was not accompanied by significant changes in the levels of enzymes of glycolysis and the tricarboxylic acid cycle with the exception of malate dehydrogenase which was lower in infected leaves. In contrast, the activities of glucose-6-P dehydrogenase and 6-P-gluconate dehydrogenase showed changes similar to that observed for respiration.The respiration and the activities of glucose-6-P dehydrogenase and 6-P-gluconate dehydrogenase did not increase in infected leaves of etiolated plants, even when excellent growth of the fungus was established by growing the plants in White's basal medium supplemented with sucrose. The respiration of a susceptible mutant barley (the yellow-green virescent mutant of the variety Himalaya) when grown in the light at 11 degrees was not changed by infection although the characteristic respiratory rise occurred in plants grown at 15 degrees . At the lower temperature chloroplasts fail to develop in this mutant, although development is normal at 15 degrees .It is suggested that the pathogen is not directly responsible for the increase in respiration in green leaves, rather that this is a response in the host cells to a loss of photosynthetic capacity.
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PMID:Metabolic regulation in diseased leaves. I. The respiratory rise in barley leaves infected with powdery mildew. 1665 53

The changes in level of activity during the germination of wheat seedling (Triticum durum) in the dark have been investigated with 4 enzymes of glycolysis, 2 enzymes of the pentose phosphate shunt, 2 of the tricarboxylic acid cycle, 2 of amino acid metabolism and acid phosphatase. For some enzymes, which function in photosynthesis (fructose diphosphate aldolase, glyceraldehyde phosphate dehydrogenase NADP dependent), the level of activity was influenced by the presence of light.
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PMID:Changes in Enzyme Levels During Germination of Seeds of Triticum durum. 1665 61

The inhibition of photosynthetic CO(2) fixation by O(2), commonly referred to as the Warburg effect, was examined in isolated intact spinach (Spinacia oleracea) chloroplasts. The major characteristics of this effect in isolated chloroplasts are rapid reversibility when O(2) is replaced by N(2), an increased inhibition by O(2) at low concentrations of CO(2) and a decreased effect of O(2) with increased concentrations of CO(2).Both the DPN- and TPN-linked glyceraldehyde 3-phosphate dehydrogenases but not aldolase were inhibited by O(2). The photoreduction of TPN measured in fragmented chloroplast preparations was similar in N(2) and O(2) down to a concentration of 5 micromolar TPN. The effect of 100% O(2) on (14)CO(2) assimilation was overcome completely by fructose 1,6-diphosphate and by ribose 5-phosphate but not by ascorbate, cysteine, dithiothreitol and reduced lipoate. Glycolate became the major photosynthetic product at high partial pressures of O(2) or at low CO(2) concentrations. It is concluded that O(2) depresses photosynthesis primarily by causing a shift of a major portion of the total carbon into glycolate and impairing the functioning of the photosynthetic carbon reduction cycle. The mechanism whereby O(2) alters the flow of carbon into glycolate remains unknown.
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PMID:Inhibition of photosynthesis by oxygen in isolated spinach chloroplasts. 1665 76

The mutation of a nuclear gene in peanut (Arachis hypogaea L.) plants results in a reduced light-dependent development of chloroplast fine structure, soluble protein, ribulose-1, 5-diP carboxylase, NADP-glyceraldehyde-3-P dehydrogenase, fructose-1, 6-diP aldolase, glycerate-3-P kinase, phosphoenolpyruvate carboxylase, malate dehydrogenase, and dark respiration during the 72-hour lag period of chlorophyll synthesis in dark-grown leaves exposed to continuous light. The mutation has pleiotropic affects. Kinetic analysis shows there is also a 72-hour lag period in the light-dependent development of NADP-glyceraldehyde-3-P dehydrogenase and fructose-1, 6-diP aldolase in the mutant leaves, whereas there is no lag in the development of NAD-malate dehydrogenase and dark respiration. There is minimal development of the chloroplast during the 72-hour mutationally induced lag period, but there is pronounced cytoplasmic and mitochondrial activity during this phase. There is a 24-hour lag period in the light-dependent enlargement of the mutant leaves. At the completion of leaf enlargement, chloroplast differentiation is initiated. The mutation does not result in any chloroplast deletions, it only affects the timing of the synthesis of these components.Elimination of the lag period in leaf enlargement and chloroplast development (potentiation) requires a preliminary 72- to 96-hour dark period before exposing the dark-grown leaves to continuous light. There is extensive development of the etioplasts during this dark period. These results establish that the nuclear gene mutation affects the early stages of plastid development and not the light-dependent synthesis of plastid components. The nuclear gene may code for the regulation of the synthesis of a component (nutrient) in the dark (or during the lag phase in the light) which is essential for the development of mesophyll cells and plastids. Although, the chloroplast is a semi-autonomous organelle, nuclear gene control of chloroplast differentiation may not be independent of cellular growth.
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PMID:Elimination of the lag period in chloroplast development in a chlorophyll mutant of peanuts. 1665 82

The activity of several photosynthetic enzymes was unaltered by exposure of sorghum or maize to low temperatures (10 C) and light (170 w m(-2)). Two light-activated C(4)-pathway enzymes, NADP-malate dehydrogenase and pyruvate Pi dikinase, were reduced in activity, and this was largely attributable to a loss of enzyme rather than to incomplete enzyme activation. Loss of NADP-malate dehydrogenase was more marked in sorghum than in maize, and in both species no loss occurred at 10 C when light levels were reduced from 170 to 50 w m(-2). A light-dependent, low temperature-induced loss of catalase activity was also observed in maize leaves.The rate of in vivo activation of pyruvate Pi dikinase following illumination was reduced at 10 C compared with that at 25 C, but no immediate effect of low temperature on the in vivo activation of NADP-malate dehydrogenease could be measured. A similar differential effect of temperature on the rates of activation of these two enzymes was found in vitro. Arrhenius type plots of pyruvate Pi dikinase from sorghum and maize demonstrated a further sensitivity to low temperature. A sharp increase in the activation energy of this enzyme was observed below 12 C, both in the presence and absence of Triton X-100. No change in the activation energy of maize leaf malic enzyme, NADP-malate dehydrogenase, fructose-1, 6-diphosphate aldolase, or NADP-glyceraldehyde 3-P dehydrogenase occurred over a temperature range of 6 to 30 C.The postillumination time course of pyruvate Pi dikinase activation, net photosynthesis and stomatal opening was followed. Reduction in the rate of response that occurred with decreasing temperature was similar in all cases, and at any one temperature, pyruvate Pi dikinase activation slightly preceded increasing photosynthesis rates. Causal relationships could not, however, be proved.
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PMID:Plants under Climatic Stress: VI. Chilling and Light Effects on Photosynthetic Enzymes of Sorghum and Maize. 1665 54

A mutant strain, Y(9), of Euglena gracilis strain Z that is unable to produce protochlorophyll or chlorophyll has been isolated following treatment of wild type cells with nalidixic acid. Dark-grown cells of the mutant contain proplastids that show only limited ultrastructural development when placed in the light. Treatment of Y(9) cells with ultraviolet light brings about permanent cell bleaching with a target number similar to wild type Euglena, and with a slightly greater sensitivity to ultraviolet. Three enzymes of the reductive pentose phosphate cycle, fructose-1,6-diphosphate aldolase (class I), NADP-dependent glyceraldehyde-3-phosphate dehydrogenase, and 3-phosphoglycerate kinase, are detectable in dark-grown Y(9) cells at the low concentrations characteristic of dark-grown wild type cells, and increase substantially when these cells are exposed to light. The activity of ribulose-1,5-diphosphate carboxylase increases in the light to a lesser extent. Cytochrome 552, a carrier in the photosynthetic electron transport chain, is not present in light-grown cells of Y(9). The significance of this mutant for an understanding of the role of light in Euglena chloroplast development is discussed.
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PMID:Light-induced Enzyme Formation in a Chlorophyll-less Mutant of Euglena gracilis. 1666 May 82

Organelles were isolated from dark-grown Euglena gracilis Klebs by sucrose density gradient centrifugation. Plastids, identified by triosephosphate isomerase and NADP glyoxylate reductase were present at an equilibrium density of 1.24 grams per cubic centimeter clearly separated from mitochondria at an equilibrium density of 1.22 grams per cubic centimeter. Assay for choline phosphotransferase and glucose-6-phosphatase showed that endoplasmic reticulum membranes were present at a density of 1.12 grams per cubic centimeter. The plastid fraction contained phosphofructokinase, pyruvate kinase, triosephosphate isomerase and aldolase indicating the operation of a glycolytic pathway. During regreening pyruvate kinase and phosphofructokinase in the developing proplastid decreased, neither enzyme being present in the mature chloroplast. However, plastids were present in the photosynthetic cell as shown by a peak of glycolysis enzymes at an equilibrium density of 1.24 grams per cubic centimeter.The integrity of isolated plastids was demonstrated by their capacity for protein synthesis. Plastids isolated from dark-grown cells rapidly incorporated [(35)S]methionine into protein with an absolute dependence on added ATP. The large subunit of ribulose diphosphate carboxylase was the major polypeptide synthesized by these isolated plastids.
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PMID:Isolation and enzymic characterization of euglena proplastids. 1666 Jul 49

Tissue distribution and activity of enzymes involved in sucrose and hexose metabolism were examined in kernels of two inbreds of maize (Zea mays L.) at progressive stages of development. Levels of sugars and starch were also quantitated throughout development. Enzyme activities studied were: ATP-linked fructokinase, UTP-linked fructokinase, ATP-linked glucokinase, sucrose synthase, UDP-Glc pyrophosphorylase, UDP-Glc dehydrogenase, PPi-linked phosphofructokinase, ATP-linked phosphofructokinase, NAD-dependent sorbitol dehydrogenase, NADP-dependent 6-P-gluconate dehydrogenase, NADP-dependent Glc-6-P dehydrogenase, aldolase, phosphoglucoisomerase, and phosphoglucomutase. Distribution of invertase activity was examined histochemically. Hexokinase and ATP-linked phosphofructokinase activities were the lowest among these enzymes and it is likely that these enzymes may regulate the utilization of sucrose in developing maize kernels. Most of the hexokinase activity was found in the endosperm, but the embryo had high activity on a dry weight basis. The endosperm, which stores primarily starch, contained high PPi-linked phosphofructokinase and low ATP-linked phosphofructokinase activities, whereas the embryo, which stores primarily lipids, had much higher ATP-linked phosphofructokinase activity than did the endosperm. It is suggested that PPi required by UDP-Glc pyrophosphorylase and PPi-linked phosphofructokinase in the endosperm may be supplied by starch synthesis. Sorbitol dehydrogenase activity was largely restricted to the endosperm, whereas 6-P-gluconate and Glc-6-P dehydrogenase activities were highest in the base and pericarp. A possible metabolic pathway by which sucrose is converted into starch is proposed.
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PMID:Enzymes of sucrose and hexose metabolism in developing kernels of two inbreds of maize. 1666 24


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