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phosphofructokinase/картоф
Линкът е запазен в клипборда
Страница 1 от 33 резултата
Effect of low temperature on the activity of phosphofructokinase from potato tubers.
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The aim of this work was to compare the coldlability of phosphofructokinase (EC 2.7.1.11) from tubers of potato cultivars (cvs.) known to differ in their propensity to accumulate sugars at low temperature. When stored at 4°C for six weeks, the sugar content of tubers ofSolanum tuberosum L. cv.
Metabolic Control Analysis of glycolysis in tuber tissue of potato (Solanum tuberosum): explanation for the low control coefficient of phosphofructokinase over respiratory flux.
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We have applied Metabolic Control Analysis (MCA) in an attempt to determine the distribution of glycolytic flux control between the steps of glycolysis in aged disks of potato tuber under aerobic conditions, using concentrations of glycolytic metabolites in tuber tissue from a range of transgenic
Starch synthesis in transgenic potato tubers with increased 3-phosphoglyceric acid content as a consequence of increased 6-phosphofructokinase activity.
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The aim of this work was to test the hypothesis that changes in cytosolic 3-phosphoglyceric acid (3-PGA) content can regulate the rate of starch synthesis in potato (Solanum tuberosum L.) tubers. The amount of 3-PGA was increased by expressing bacterial phosphofructokinase (PFK; EC 2.7.1.11) in
Molecular characterization of four forms of phosphofructokinase purified from potato tuber.
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Four forms of phosphofructokinase (PFK) have been purified to apparent homogeneity from tubers of potato (Solanum tuberosum cv. Record). Each had a final specific activity of about 200 mumol.min-1.mg-1 protein. Similar forms of PFK were found in partially purified extracts from tubers and leaves of
Inorganic pyrophosphate: fructose-6-phosphate 1-phosphotransferase of the potato tuber is related to the major ATP-dependent phosphofructokinase of E. coli.
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A procedure was developed for the purification of inorganic pyrophosphate: fructose-6-phosphate 1-phospho-transferase (PPi-PFK) from potato tubers. The enzyme has the structure alpha 4 beta 4 with a subunit of 68 kDa and a beta subunit of 60 kDa. The structural relationship of this enzyme to other
Fluorescence study of ligand binding to potato tuber pyrophosphate-dependent phosphofructokinase: evidence for competitive binding between fructose-1,6-bisphosphate and fructose-2,6-bisphosphate.
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The intrinsic fluorescence of potato tuber pyrophosphate:fructose-6-phosphate 1-phosphotransferase (PFP) was used as an indicator of conformational changes due to ligand binding. Binding of the substrates and the allosteric activator fructose-2,6-bisphosphate was quantitatively compared to their
Potato tuber pyrophosphate-dependent phosphofructokinase: effect of thiols and polyalcohols on its intrinsic fluorescence, oligomeric structure, and activity in dilute solutions.
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The effect of dilution of homogeneous potato tuber pyrophosphate:fructose-6-phosphate 1-phosphotransferase (EC 2.7.1.90; PFP) on the enzyme's intrinsic fluorescence, activity, and oligomeric structure has been examined. A rapid decrease in PFP's intrinsic fluorescence occurred in response to
Finite change analysis of glycolytic intermediates in tuber tissue of lines of transgenic potato (Solanum tuberosum) overexpressing phosphofructokinase.
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Genetically engineered organisms overexpressing phosphofructokinase (PFK), a supposed 'regulatory' step of glycolysis, often show little or no measurable change in glycolytic or respiratory flux, although the concentrations of glycolytic intermediates may change. We have used the finite change
Effect of chloride ions on the kinetic parameters of the potato tuber and mung bean pyrophosphate-dependent phosphofructokinase.
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The affinity constant Ka of PPi-PFK for Fru 2,6-P2 is equal to 1.56 nM for the potato enzyme and to 6.67 nM for that of the mung bean in the absence of chloride ions. These results are notably lower than the currently reported 5.5 nM and 30, 50 nM respectively. It is shown that the chloride ion is a
Low levels of pyrophosphate in transgenic potato plants expressing E. coli pyrophosphatase lead to decreased vitality under oxygen deficiency.
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OBJECTIVE
The aim of this study was to investigate the importance of pyrophosphate (PPi) for plant metabolism and survival under low oxygen stress. Responses of roots of wild-type potato plants were compared with roots of transgenic plants containing decreased amounts of PPi as a result of the
Effect of sink isolation on sugar uptake and starch synthesis by potato-tuber storage parenchyma.
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Import into potato (Solarium tuberosum L. cv. Record) tubers was terminated by removing the sink at its connection with the stolon. The ability of discs of storage tissue from the excised tubers to take up exogenous sugars and convert them to starch was compared with that of discs from untreated
Cloning, sequencing, and expression of pyrophosphate-dependent phosphofructokinase from Propionibacterium freudenreichii.
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Pyrophosphate-dependent 6-phosphofructo-1-kinase (PPi-PFK) from Propionibacterium freudenreichii is a non-allosteric enzyme with properties dissimilar to those of other described phosphofructokinases. The enzyme was cloned into pBluescript, sequenced, and expressed in Escherichia coli at levels 15
Molecular, Kinetic, and Immunological Properties of the 6-Phosphofructokinase from the Green Alga Selenastrum minutum: Activation during Biosynthetic Carbon Flow.
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The ATP:d-fructose-6-phosphate 1-phosphotransferase (PFK) from Selenastrum minutum was purified to homogeneity. The purified plastid enzyme had a specific activity of 180 micromoles per milligram of protein per minute. It is a homomer with a subunit molecular weight of 70,000. The smallest
[The use of pyrophosphate-dependent phosphofructokinase for the determination of fructose-2,6-bisphosphate concentration in biological material].
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The authors discuss methods for purification of pyrophosphate fructose-6-phosphate phosphotransferase from potato tuber and enzymatic method for measuring fructose-2,6-biphosphate concentration in isolated hepatocytes of normal and diabetic rats and come to a conclusion on a higher sensitivity of
Cloning and sequencing a putative pyrophosphate-dependent phosphofructokinase gene from Entamoeba histolytica.
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Pyrophosphate-dependent phosphofructokinase (PPi-PFK) gene from Entamoeba histolytica was cloned from its genomic library and sequenced. The open reading frame has 1149 bp and codes for a protein of 41.5 kDa. The deduced amino acid sequence of E. histolytica PPi-PFK has 25 to 28% identity to the
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