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Query: EC:4.1.1.49 (phosphoenolpyruvate carboxykinase)
4,654 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Four enzymes, namely, the maize C(4)-specific phosphoenolpyruvate carboxylase (PEPC), the maize C(4)-specific pyruvate, orthophosphate dikinase (PPDK), the sorghum NADP-malate dehydrogenase (MDH), and the rice C(3)-specific NADP-malic enzyme (ME), were overproduced in the mesophyll cells of rice plants independently or in combination. Overproduction individually of PPDK, MDH or ME did not affect the rate of photosynthetic CO(2) assimilation, while in the case of PEPC it was slightly reduced. The reduction in CO(2) assimilation in PEPC overproduction lines remained unaffected by overproduction of PPDK, ME or a combination of both, however it was significantly restored by the combined overproduction of PPDK, ME, and MDH to reach levels comparable to or slightly higher than that of non-transgenic rice. The extent of the restoration of CO(2) assimilation, however, was more marked at higher CO(2) concentrations, an indication that overproduction of the four enzymes in combination did not act to concentrate CO(2) inside the chloroplast. Transgenic rice plants overproducing the four enzymes showed slight stunting. Comparison of transformants overproducing different combinations of enzymes indicated that overproduction of PEPC together with ME was responsible for stunting, and that overproduction of MDH had some mitigating effects. Possible mechanisms underlying these phenotypic effects, as well as possibilities and limitations of introducing the C(4)-like photosynthetic pathway into C(3) plants, are discussed.
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PMID:Overproduction of C4 photosynthetic enzymes in transgenic rice plants: an approach to introduce the C4-like photosynthetic pathway into rice. 1831 17

Sugarcane (Saccharum officinarum L. cv. CP72-2086) was grown in sunlit greenhouses at daytime [CO(2)] of 360 (ambient) and 720 (elevated)mumolmol(-1). Drought stress was imposed for 13d when plants were 4 months old, and various photosynthetic parameters and levels of nonstructural carbohydrates were determined for uppermost fully expanded leaves of well-watered (control) and drought stress plants. Control plants at elevated [CO(2)] were 34% and 25% lower in leaf stomatal conductance (g(s)) and transpiration rate (E) and 35% greater in leaf water-use efficiency (WUE) than their counterparts at ambient [CO(2)]. Leaf CO(2) exchange rate (CER) and activities of Rubisco, NADP-malate dehydrogenase, NADP-malic enzyme and pyruvate P(i) dikinase were marginally affected by elevated [CO(2)], but were reduced by drought, whereas activity of PEP carboxylase was reduced by elevated [CO(2)], but not by drought. At severe drought developed at day 12, leaf g(s) and WUE of ambient-[CO(2)] stress plants declined to 5% and 7%, while elevated-[CO(2)] stress plants still maintained g(s) and WUE at 20% and 74% of their controls. In control plants, elevated [CO(2)] did not enhance the midday levels of starch, sucrose, or reducing sugars. For both ambient- and elevated-[CO(2)] stress plants, severe drought did not affect the midday level of sucrose but substantially reduced that of starch. Nighttime starch decomposition in control plants was 55% for ambient [CO(2)] and 59% for elevated [CO(2)], but was negligible for stress plants of both [CO(2)] treatments. For both ambient-[CO(2)] control and stress plants, midday sucrose level at day 12 was similar to the predawn value at day 13. In contrast, sucrose levels of elevated-[CO(2)] control and stress plants at predawn of day 13 were 61-65% of the midday values of day 12. Levels of reducing sugars were much greater for both ambient- and elevated-[CO(2)] stress plants, implying an adaptation to drought stress. Sugarcane grown at elevated [CO(2)] had lower leaf g(s) and E and greater leaf WUE, which helped to delay the adverse effects of drought and, thus, allowed the stress plants to continue photosynthesis for at least an extra day during episodic drought cycles.
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PMID:Growth at elevated CO(2) delays the adverse effects of drought stress on leaf photosynthesis of the C(4) sugarcane. 1846 32

The physiology and central carbon metabolism of Corynebacterium glutamicum was investigated through the study of specific disruption mutants. Mutants deficient in phosphoenolpyruvate carboxylase (PPC) and/or pyruvate kinase (PK) activity were constructed by disrupting the corresponding gene(s) via transconjugation. Standard batch fermentations were carried out with these mutants and results were evaluated in the context of intracellular flux analysis. The following were determined. (a) There is a significant reduction in the glycolytic pathway flux in the pyruvate kinase deficient mutants during growth on glucose, also evidenced by secretion of dihydroxyacetone and glyceraldehyde. The resulting metabolic overflow is accommodated by the pentose phosphate pathway (PPP) acting as mechanism for dissimilating, in the form of CO(2), large amounts of accumulated intermediates. (b) The high activity through the PPP causes an overproduction of reducing power in the form of NADPH. The overproduction of biosynthetic reducing power, as well as the shortage of NADPH produced via the tricarboxylic acid cycle (as evidenced by a reduced citrate synthase flux), are compensated by an increased activity of the transhydrogenase (THD) enzyme catalyzing the reaction NADPH + NAD(+)<-->NADP(+) + NADH. The presence of active THD was also confirmed directly by enzymatic assays. (c) Specific glucose uptake rates declined during the course of fermentation and this decline was more pronounced in the case of a double mutant strain deficient in both PPC and PK. Specific ATP consumption rates similarly declined during the course of the batch. However, they were approximately the same for all strains, indicating that energetic requirements for biosynthesis and maintenance are independent of the specific genetic background of a strain. The above results underline the importance of intracellular flux analysis, not only for producing a static set of intracellular flux estimates, but also for uncovering changes occurring in the course of a batch fermentation or as result of specific genetic modifications.
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PMID:Metabolic and physiological studies of Corynebacterium glutamicum mutants. 1863 97

The effects of Fe deficiency on different metabolic processes were characterized in roots, xylem sap and leaves of tomato. The total organic acid pool increased significantly with Fe deficiency in xylem sap and leaves of tomato plants, whereas it did not change in roots. However, the composition of the pool changed with Fe deficiency, with major increases in citrate concentrations in roots (20-fold), leaves (2-fold) and xylem sap (17-fold). The activity of phosphoenolpyruvate carboxylase, an enzyme leading to anaplerotic C fixation, increased 10-fold in root tip extracts with Fe deficiency, whereas no change was observed in leaf extracts. The activities of the organic acid synthesis-related enzymes malate dehydrogenase, citrate synthase, isocitrate dehydrogenase, fumarase and aconitase, as well as those of the enzymes lactate dehydrogenase and pyruvate carboxylase, increased with Fe deficiency in root extracts, whereas only citrate synthase increased significantly with Fe deficiency in leaf extracts. These results suggest that the enhanced C fixation capacity in Fe-deficient tomato roots may result in producing citrate that could be used for Fe xylem transport. Total pyridine nucleotide pools did not change significantly with Fe deficiency in roots or leaves, although NAD(P)H/NAD(P) ratios were lower in Fe-deficient roots than in controls. Rates of O(2) consumption were similar in Fe-deficient and Fe-sufficient roots, but the capacity of the alternative oxidase pathway was decreased by Fe deficiency. Also, increases in Fe reductase activity with Fe deficiency were only 2-fold higher when measured in tomato root tips. These values are significantly lower than those found in other plant species, where Fe deficiency leads to larger increases in organic acid synthesis-related enzyme activities and flavin accumulation. These data support the hypothesis that the extent of activation of different metabolic pathways, including carbon fixation via PEPC, organic acid synthesis-related enzymes and oxygen consumption is different among species, and this could modulate the different levels of efficiency in Strategy I plants.
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PMID:Metabolic responses in iron deficient tomato plants. 1876 May

Oxidation of ethanol, acetaldehyde, and acetate in Rhodococcus erythropolis EK-1, producer of surface-active substances (SAS), is catalyzed by N,N-dimethyl-4-nitrosoaniline (DMNA)-dependent alcohol dehydrogenase, NAD+/NADP(+)-dependent dehydrogenases (optimum pH 9.5), and acetate kinase/acetyl-CoA-synthetase, respectively. The glyoxylate cycle and complete tricarboxylic acid cycle function in the cells of R. erythropolis EK-1 growing on ethanol; the synthesis of phosphoenolpyruvate (PEP) is provided by the two key enzymes of gluconeogenesis, PEP carboxykinase and PEP synthetase. Introduction of citrate (0.1%) and fumarate (0.2%) into the cultivation medium of R. erythropolis EK-1 containing 2% ethanol resulted in the 1.5- and 5.3-fold increase in the activities of isocitrate lyase and PEP synthetase (the key enzymes of the glyoxylate cycle and gluconeogenesis branch of metabolism, respectively) and of lipid synthesis, as evidenced by the 1.5-fold decrease of isocitrate dehydrogenase activity. In the presence of fumarate and citrate, the indices of SAS synthesis by strain R. erythropolis EK-1 grown on ethanol increased by 40-100%.
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PMID:[C2 metabolism and intensification of the synthesis of surface-active substances in Rhodococcus erythropolis EK-1 grown on ethanol]. 1913 13

The enzyme activities of isocitrate dehydrogenase (ICDH, NADP-specific), lactate dehydrogenase (LDH), malate dehydrogenase (MDH), phosphoenolpyruvate carboxykinase (PEPCK), phosphofructokinase (PFK), pyruvate kinase (PK), and fructose-l,6-bisphosphatase (FBPase) were studied in the third-stage juveniles of Steinernema carpocapsae. Reaction requirements, pH optima, substrate and cofactor kinetic constants were similar to those reported previously from other parasitic helminths with the exception of LDH, which was unstable and could not be characterized for specific activity and kinetic constants. The respective pH optima were 7.5 for ICDH, 8.8 for MDH, 6.5 for PEPCK, 7.3 for PFK, 7.2 for PK, and 7.5 for FBPase. The specific activities for ICDH, MDH, PEPCK, PFK, PK, and FBPase at pH 7.5 were 4.8, 1,300, 22, 25, 35, and 6.8 (nmoles substrate min(1) mg protein(1)), respectively. In summary, the infective juveniles of S. carpocapsae display the metabolism typical of a facultative aerobe.
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PMID:Characterization of Key Glycolytic and Oxidative Enzymes in Steinernema carpocapsae. 1927 61

Seedlings of sour pummelo (Citrus grandis) were irrigated daily for 18 weeks with nutrient solution containing four phosphorus (P) levels (50, 100, 250 and 500 microM KH2PO4) and two aluminum (Al) levels [0 (-Al) and 1.2 mM AlCl3 x 6H2O (+Al)]. Both malate and citrate concentrations in +Al leaves decreased with increasing P supply, but their concentrations in -Al leaves did not change in response to P supply. The concentrations of malate under 50 microM P and of citrate under 50 and 100 microM P were higher in +Al leaves than in -Al ones, but malate concentration was lower in +Al leaves than in -Al ones under 500 microM P. There was no difference in root malate and citrate concentrations among different P and Al combinations except for an increase in malate and citrate under 50 microM P+0 mM Al and a slight decrease in malate under 50 microM P+1.2 mM Al. The activities of acid-metabolizing enzymes (citrate synthase, aconitase, phosphoenolpyruvate carboxylase, NADP-isocitrate dehydrogenase, phosphoenolpyruvate phosphatase, NAD-malate dehydrogenase, NADP-malic enzyme and pyruvate kinase) in most cases were less affected by P and Al interactions in roots compared to the leaves. Our results support the hypothesis that changes in organic acid metabolism differ between roots and leaves of C. grandis in response to P and Al interactions.
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PMID:Changes in organic acid metabolism differ between roots and leaves of Citrus grandis in response to phosphorus and aluminum interactions. 1959 84

Cells associated with veins of petioles of C(3) tobacco possess high activities of the decarboxylase enzymes required in C(4) photosynthesis. It is not clear whether this is the case in other C(3) species, nor whether these enzymes provide precursors for specific biosynthetic pathways. Here, we investigate the activity of C(4) acid decarboxylases in the mid-vein of Arabidopsis, identify regulatory regions sufficient for this activity, and determine the impact of removing individual isoforms of each protein on mid-vein metabolite profiles. This showed that radiolabelled malate and bicarbonate fed to the xylem stream were incorporated into soluble and insoluble material in the mid-vein of Arabidopsis leaves. Compared with the leaf lamina, mid-veins possessed high activities of NADP-dependent malic enzyme (NADP-ME), NAD-dependent malic enzyme (NAD-ME) and phosphoenolpyruvate carboxykinase (PEPCK). Transcripts derived from both NAD-ME, one PCK and two of the four NADP-ME genes were detectable in these veinal cells. The promoters of each decarboxylase gene were sufficient for expression in mid-veins. Analysis of insertional mutants revealed that cytosolic NADP-ME2 is responsible for 80% of NADP-ME activity in mid-veins. Removing individual decarboxylases affected the abundance of amino acids derived from pyruvate and phosphoenolpyruvate. Reducing cytosolic NADP-ME activity preferentially affected the sugar content, whereas abolishing NAD-ME affected both the amino acid and the glucosamine content of mid-veins.
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PMID:C acid decarboxylases required for C photosynthesis are active in the mid-vein of the C species Arabidopsis thaliana, and are important in sugar and amino acid metabolism. 1980 80

Response of two wheat cultivars (Triticum aestivum cv. YM 158 and NM 9) to the herbicide chlorotoluron and the effect of two forms of dissolved organic matter on the chlorotoluron toxicity to the plants were characterized. Treatment with chlorotoluron at 10-50 microg/ml inhibited the seed germination and a dose-response was observed. The inhibition of seed germination was correlated to the depression of alpha-amylase activities. To identify whether chlorotoluron induced oxidative damage to wheat plants, the malondlaldehyde (MDA) content and electrolyte leakage were measured. Results showed that both MDA content and electrolyte leakage in the chlorotoluron-treated roots significantly increased. Activities of several key enzymes were measured that operate in citric acid cycle and carbohydrate metabolic pathway. Inhibited activities of citrate synthase and NADP-isocitrate dehydrogenase were observed in the chlorotoluron-treated roots as compared to control plants. We also examined malate dehydrogenase and phosphoenolpyruvate carboxylase in wheat roots exposed to 30 gg/ml chlorotoluron. However, none of the enzymes showed significant changes in activities. Application of 160 microg/ml dissolved organic matter (DOM) extracted from non-treated sludge (NTS) and heat-expanded sludge (HES) in the medium with 30 microg/ml chlorotoluron induced an additive inhibition of seed germination and plant growth. The inhibition of growth due to the DOM treatment was associated with the depression of activities of alpha-amylase, citrate synthase and NADP-isocitrate dehydrogenase, as well as the increase in malondlaldehyde content and electrolyte leakage. These results suggested that the presence of DOM might enhance the uptake and accumulation of chlorotoluron, and thus resulted in greater toxicity in wheat plants. The two forms of DOM exhibited differences in regulation of chlorotoluron toxicity to the wheat plants. Treatments with DOM-NTS induced greater toxicity to plants as compared to those with DOM-HES. In addition to DOM affecting chlorotoluron-induced toxicity to wheat plants, the cultivars could have also contributed to differences. Generally, NM-9 showed a higher sensitivity to chlorotoluron than YM 158 either in the absence or in the presence of DOM.
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PMID:Effect of dissolved organic matter on the toxicity of chlorotoluron to Triticum aestivum. 2005 May 56

Two common bean (Phaseolus vulgaris L.) genotypes differing in aluminum (Al) resistance, Quimbaya (Al-resistant) and VAX-1 (Al-sensitive) were grown in hydroponics for up to 25 h with or without Al, and several parameters related to the exudation of organic acids anions from the root apex were investigated. Al treatment enhanced the exudation of citrate from the root tips of both genotypes. However, its dynamic offers the most consistent relationship between Al-induced inhibition of root elongation and Al accumulation in and exclusion from the root apices. Initially, in both genotypes the short-term (4 h) Al-injury period was characterized by the absence of citrate efflux independent of the citrate content of the root apices, and reduction of cytosolic turnover of citrate conferred by a reduced Nicotinamide adenine dinucleotide phosphate-isocitrate dehydrogenase (EC 1.1.1.42) activity. Transient recovery from initial Al stress (4-12 h) was found to be dependent mainly on the capacity to utilize internal citrate pools (Al-resistant genotype Quimbaya) or enhanced citrate synthesis [increased activities of NAD-malate dehydrogenase (EC 1.1.1.37) and ATP-phosphofructokinase (EC 2.7.1.11) in Al-sensitive VAX-1]. Sustained recovery from Al stress through citrate exudation in genotype Quimbaya after 24 h Al treatment relied on restoring the internal citrate pool and the constitutive high activity of citrate synthase (CS) (EC 4.1.3.7) fuelled by high phosphoenolpyruvate carboxylase (EC 4.1.1.31) activity. In the Al-sensitive genotype VAX-1 the citrate exudation and thus Al exclusion and root elongation could not be maintained coinciding with an exhaustion of the internal citrate pool and decreased CS activity.
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PMID:Aluminum resistance in common bean (Phaseolus vulgaris) involves induction and maintenance of citrate exudation from root apices. 2005 83


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