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:4.1.1.32 (phosphoenolpyruvate carboxykinase)
4,204 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Exposure of ribose-grown Hydrogenomonas facilis to (14)CO(2) for 6 to 12 sec during ribose oxidation resulted in labeling of a number of compounds, three of which were glutamate, phosphoglycerate, and pyruvate. Phosphoglycerate and pyruvate were labeled almost exclusively in C(1), suggesting operation of the reductive pentose phosphate cycle. Glutamate was labeled initially to the extent of 90% in C(1) and 10% in C(5), and this was followed by a concentration of radioisotope in C(5). All of the enzymes of the tricarboxylic acid cycle were detectable in ribose-grown cells, and, in general, specific activities were similar to those found in yeast extract-grown cells. Reduced nicotinamide adenine dinucleotide oxidase, aconitase, and the dehydrogenases for pyruvate, alpha-ketoglutarate, and succinate appeared to be of particulate origin. In addition to enzymes of the tricarboxylic acid cycle, an acetyl coenzyme A-stimulated phosphoenolpyruvate carboxylase was found, as was isocitrate lyase. Possible participation of these catalysts in glutamate synthesis is discussed.
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PMID:CO(2) Fixation, Glutamate Labeling, and the Krebs Cycle in Ribose-grown Hydrogenomonas facilis. 1656 53

After a 5-second exposure of illuminated bermudagrass (Cynodon dactylon L. var. ;Coastal') leaves to (14)CO(2), 84% of the incorporated (14)C was recovered as aspartate and malate. After transfer from (14)CO(2)-air to (12)CO(2)-air under continuous illumination, total radioactivity decreased in aspartate, increased in 3-phosphoglyceric acid and alanine, and remained relatively constant in malate. Carbon atom 1 of alanine was labeled predominantly, which was interpreted to indicate that alanine was derived from 3-phosphoglyceric acid. The activity of phosphoenolpyruvate carboxylase, alkaline pyrophosphatase, adenylate kinase, pyruvate-phosphate dikinase, and malic enzyme in bermudagrass leaf extracts was distinctly higher than those in fescue (Festuca arundinacea Schreb.), a reductive pentose phosphate cycle plant. Assays of malic enzyme activity indicated that the decarboxylation of malate was favored. Both malic enzyme and NADP(+)-specific malic dehydrogenase activity were low in bermudagrass compared to sugarcane (Saccharum officinarum L.). The activities of NAD(+)-specific malic dehydrogenase and acidic pyrophosphatase in leaf extracts were similar among the plant species examined, irrespective of the predominant cycle of photosynthesis. Ribulose-1, 5-diphosphate carboxylase in C(4)-dicarboxylic acid cycle plant leaf extracts was about 60%, on a chlorophyll basis, of that in reductive pentose phosphate cycle plants.We conclude from the enzyme and (14)C-labeling studies that bermudagrass contains the C(4)-dicarboxylic acid cycle and that pyruvate-phosphate dikinase does not exist exclusively in C(4)-dicarboxylic acid cycle plants, and we propose that in C(4)-dicarboxylic acid cycle plants the transfer of carbon from a dicarboxylic acid to 3-phosphoglyceric acid involves a decarboxylation reaction and then a refixation of carbon dioxide by ribulose-1, 5-diphosphate carboxylase.
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PMID:Photosynthetic CO(2) Fixation Products and Activities of Enzymes Related to Photosynthesis in Bermudagrass and Other Plants. 1665 95

Chlorophyll synthesis induced by continuous illumination of dark-grown seedlings has been followed in wild-type and virescent peanut leaves. Compared to the wild-type leaves, chlorophyll synthesis in the virescent leaves shows a 72-hour lag period before the onset of a phase of rapid chlorophyll accumulation. The development of chloroplast grana and the activity of many enzymes of the reductive pentose phosphate cycle, phosphoenolpyruvate carboxylase, and malate dehydrogenase are reduced in the virescent leaves during the lag phase of chlorophyll accumulation. Although nucleic acid synthesis in the virescent leaves in normal, there is a distinctly lower rate of protein synthesis. The low level of protein synthesis during the lag period might limit the synthesis of a factor(s) essential for the development of both cell and chloroplast constituents.
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PMID:Nuclear gene affecting greening in virescent peanut leaves. 1665 94

The activities of certain enzymes related to the carbon assimilation pathway in whole leaves, mesophyll cell extracts, and bundle sheath extracts of the C(4) plant Panicum miliaceum have been measured and compared on a chlorophyll basis. Enzymes of the C(4) dicarboxylic acid pathway-phosphoenolpyruvate carboxylase and NADP-malic dehydrogenase-were localized in mesophyll cells. Carbonic anhydrase was also localized in mesophyll cell extracts. Ribose 5-phosphate isomerase, ribulose 5-phosphate kinase, and ribulose diphosphate carboxylase-enzymes of the reductive pentose phosphate pathway-were predominantly localized in bundle sheath extracts. High activities of aspartate and alanine transaminases and glyceraldehyde-3-P dehydrogenase were found about equally distributed between the photosynthetic cell types. P. miliaceum had low malic enzyme activity in both mesophyll and bundle sheath extracts.Isolated bundle sheath cells were capable of converting aspartate to oxalacetate at rates approaching the aspartate transaminase activity of bundle sheath extracts. The bundle sheath cells had a light induced CO(2) fixation of 23 mumoles of CO(2)/mg chl.hr in the absence of exogenous substrates.The photorespiratory enzymes, hydroxypyruvate reductase and glycolic oxidase, were about 3 fold higher in bundle sheath extracts than in mesophyll extracts when compared on a chlorophyll basis.
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PMID:Metabolic Activities in Extracts of Mesophyll and Bundle Sheath Cells of Panicum miliaceum (L.) in Relation to the C(4) Dicarboxylic Acid Pathway of Photosynthesis. 1665 52

Phosphoenolpyruvate carboxykinase has been found in significant activities in a number of plants exhibiting Crassulacean acid metabolism. Thirty-five species were surveyed for phosphoenolpyruvate carboxykinase, phosphoenolpyruvate carboxylase, ribulose diphosphate carboxylase, malic enzyme, and malate dehydrogenase (NAD). Plants which showed high activities of malic enzyme contained no detectable phosphoenolpyruvate carboxykinase, while plants with high activities of the latter enzyme contained little malic enzyme. It is proposed that phosphoenolpyruvate carboxykinase acts as a decarboxylase during the light period, furnishing CO(2) for the pentose cycle and phosphoenolpyruvate for gluconeogenesis.Some properties of phosphoenolpyruvate carboxykinase in crude extracts of pineapple leaves were investigated. The enzyme required Mn(2+), Mg(2+), and ATP for maximum activity. About 60% of the activity could be pelleted, along with chloroplasts and mitochondria, in extracts from leaves kept in the dark overnight.
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PMID:Phosphoenolpyruvate carboxykinase in plants exhibiting crassulacean Acid metabolism. 1665 62

Labeling studies using detached lupin (Lupinus angustifolius) nodules showed that over times of less than 3 minutes, label from [3,4-(14)C]glucose was incorporated into amino acids, predominantly aspartic acid, to a much greater extent than into organic acids. Only a slight preferential incorporation was observed with [1-(14)C]- and [6-(14)C]glucose, while with [U-(14)C]-glucose more label was incorporated into organic acids than into amino acids at all labeling times. These results are consistent with a scheme whereby the "carbon skeletons" for amino acid synthesis are provided by the phosphoenolpyruvate carboxylase reaction.A comparison of (14)CO(2) release from nodules supplied with [1-(14)C]- and [6-(14)C]glucose indicated that the oxidative pentose phosphate pathway accounted for less than 6% of glucose metabolism. Several enzymes of the oxidative pentose phosphate and glycolytic pathways were assayed in vitro using the 12,000g supernatant fraction from nodule homogenates. In all cases, the specific activities were adequate to account for the calculated in vivo fluxes.Three out of four diverse treatments that inhibited nodule nitrogen fixation also inhibited nodule CO(2) fixation, and in the case of the fourth treatment, replacement of N(2) with He, it was shown that the normal entry of label from exogenous (14)CO(2) into the nodule amino acid pool was strongly inhibited.
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PMID:Carbon Dioxide Fixation by Lupin Root Nodules: II. Studies with C-labeled Glucose, the Pathway of Glucose Catabolism, and the Effects of Some Treatments That Inhibit Nitrogen Fixation. 1666 Jul 46

Short-term changes in pyridine nucleotides and other key metabolites were measured during the onset of NO(3) (-) or NH(4) (+) assimilation in the dark by the N-limited green alga Selenastrum minutum. When NH(4) (+) was added to N-limited cells, the NADH/NAD ratio rose immediately and the NADPH/NADP ratio followed more slowly. An immediate decrease in glutamate and 2-oxoglutarate indicates an increased flux through the glutamine synthase/glutamate oxoglutarate aminotransferase. Pyruvate kinase and phosphoenolpyruvate carboxylase are rapidly activated to supply carbon skeletons to the tricarboxylic acid cycle for amino acid synthesis. In contrast, NO(3) (-) addition caused an immediate decrease in the NADPH/NADP ratio that was accompanied by an increase in 6-phosphogluconate and decrease in the glucose-6-phosphate/6-phosphogluconate ratio. These changes show increased glucose-6-phosphate dehydrogenase activity, indicating that the oxidative pentose phosphate pathway supplies some reductant for NO(3) (-) assimilation in the dark. A lag of 30 to 60 seconds in the increase of the NADH/NAD ratio during NO(3) (-) assimilation correlates with a slow activation of pyruvate kinase and phosphoenolpyruvate carboxylase. Together, these results indicate that during NH(4) (+) assimilation, the demand for ATP and carbon skeletons to synthesize amino acid signals activation of respiratory carbon flow. In contrast, during NO(3) (-) assimilation, the initial demand on carbon respiration is for reductant and there is a lag before tricarboxylic acid cycle carbon flow is activated in response to the carbon demands of amino acid synthesis.
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PMID:Activation of Respiration to Support Dark NO(3) and NH(4) Assimilation in the Green Alga Selenastrum minutum. 1666 13

Glucose metabolism plays an essential role in the physiology and development of almost all living organisms. In the present study we investigated glucose metabolism during the embryogenesis of the hard tick Boophilus microplus. An increase in glucose and glycogen content during the embryonic development of B. microplus was detected and shown to be due to the high enzyme activity of both gluconeogenesis and glycolytic pathways. Glucose 6-phosphate (G-6P), formed by hexokinase, is driven mainly to pentose-phosphate pathway, producing fundamental substrates for cellular biosynthesis. We detected an increase in glucose 6-phosphate dehydrogenase and pyruvate kinase activities after embryo cellularization. Accumulation of key metabolites such as glycogen and glucose was monitored and revealed that glycogen content decreases from day 1 up to day 6, as the early events of embryogenesis take place, and increases after the formation of embryo cellular blastoderm on day 6. Glucose and guanine (a sub-product of amino acids degradation in arachnids) accumulate almost concomitantly. The activity of phosphoenolpyruvate carboxykinase was increased after embryo cellularization. Taken together these data indicate that glycogen and glucose, formed during B. microplus embryogenesis after blastoderm formation, are produced by intense gluconeogenesis.
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PMID:Glucose metabolism during embryogenesis of the hard tick Boophilus microplus. 1690 22

The transcriptional regulator CcpN of Bacillus subtilis has been recently characterized as a repressor of two gluconeogenic genes, gapB and pckA, and of a small noncoding regulatory RNA, sr1, involved in arginine catabolism. Deletion of ccpN impairs growth on glucose and strongly alters the distribution of intracellular fluxes, rerouting the main glucose catabolism from glycolysis to the pentose phosphate (PP) pathway. Using transcriptome analysis, we show that during growth on glucose, gapB and pckA are the only protein-coding genes directly repressed by CcpN. By quantifying intracellular fluxes in deletion mutants, we demonstrate that derepression of pckA under glycolytic condition causes the growth defect observed in the ccpN mutant due to extensive futile cycling through the pyruvate carboxylase, phosphoenolpyruvate carboxykinase, and pyruvate kinase. Beyond ATP dissipation via this cycle, PckA activity causes a drain on tricarboxylic acid cycle intermediates, which we show to be the main reason for the reduced growth of a ccpN mutant. The high flux through the PP pathway in the ccpN mutant is modulated by the flux through the alternative glyceraldehyde-3-phosphate dehydrogenases, GapA and GapB. Strongly increased concentrations of intermediates in upper glycolysis indicate that GapB overexpression causes a metabolic jamming of this pathway and, consequently, increases the relative flux through the PP pathway. In contrast, derepression of sr1, the third known target of CcpN, plays only a marginal role in ccpN mutant phenotypes.
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PMID:CcpN controls central carbon fluxes in Bacillus subtilis. 1858 36

The two main contributions of this are the solidification of Corynebacterium glutamicum biochemistry guided by bioreaction network analysis, and the determination of bansal metabolic flux distributions during growth and lysine synthesis. Employed methodology makes use of stoichiometrically based mass balances to determine flux distributions in the C. glutamicum metabolic network. Presented are a brief description of the methodology, a through literature review of glutamic acid bacteria biochemistry, and specific results obtained through a combination of fermentation studies and analysis-directed intracellular assays. The latter include the findings of the lack of activity of glyoxylate shunt, and that phosphoenolpyruvate carboxylase (PPC) is the only anaplerotic reaction expressed in C. glutamicum cultivated on glucose minimal media. Network simplifications afforded by the above findings facilitated the determination of metabolic flux distributions under a variety of culture conditions and led to the following conclusions. Both the pentose phosphate pathway and PPC support fluxes during growth and lysine overproduction branch point does not appear to limit lysine synthesis.
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PMID:Metabolic flux distributions in Corynebacterium glutamicum during growth and lysine overproduction. 1860 99


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