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:1.2.1.13 (glyceraldehyde-3-phosphate dehydrogenase)
6,511 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Crude extracts of both vegetative cells and glycerol-induced microcysts of Myxococcus xanthus contained the following enzyme activities: phosphofructokinase, phosphoglucoisomerase, fructose-1,6-diphosphatase, fructosediphosphate aldolase, glyceraldehyde-3-phosphate dehydrogenase, phosphopyruvate carboxylase, citrate synthase, isocitrate dehydrogenase, alpha-ketoglutarate dehydrogenase, succinate dehydrogenase, malate dehydrogenase, glucose-6-phosphate dehydrogenase, 6-phosphogluconate dehydrogenase, phosphoglucomutase, and uridine diphosphate glucose pyrophosphorylase. With the exception of isocitrate dehydrogenase, which was present at a fivefold higher concentration in microcysts, all activities in extracts from both types of cells were essentially equal. Hexokinase and pyruvate kinase could not be detected in extracts from either type of cell. Microcysts metabolized acetate at a lower rate than did vegetative cells. Most of this decrease was reflected in a substantial decrease in ability of microcysts to oxidize acetate to CO(2). In addition, microcysts and vegetative cells showed a different distribution of (14)C-label from incorporated acetate.
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PMID:Comparative intermediary metabolism of vegetative cells and microcysts of Myxococcus xanthus. 430 96

Purified preparations of Coxiella burnetii were examined for enzymes of the glycolytic pathway. Glucose-phosphate isomerase, fructose-1,6-diphosphatase, aldolase, glyceraldehyde-3-phosphate dehydrogenase, and pyruvate kinase were shown to be present in C. burnetii extracts. Heat-killed C. burnetii purified with normal yolk sacs demonstrated no activity after disruption. Aldolase was shown to be of the class II type by complete inhibition of activity in the presence of 8 x 10(-3)m ethylenediaminetetraacetic acid. The host enzyme activity (normal and infected yolk sacs) was not affected by the same treatment. When cellulose acetate electrophoresis was performed on the extracts, aldolase from both normal and infected yolk sacs exhibited five isozyme bands, whereas aldolase from the C. burnetii extract appeared as a single band.
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PMID:Biochemistry of Coxiella burnetii: Embden-Meyerhof pathway. 432 56

Some highly purified glycolytic enzymes have been subjected to isoelectric focusing and found to contain a number of enzymatically active species. Crystalline aldolase A and glyceraldehyde-3-phosphate dehydrogenase from rabbit muscle were resolved into five components, crystalline aldolase from yeast was resolved into three components, pyruvate kinase from rabbit muscle yielded four components, and yeast enolase was resolved into two components. Rabbit muscle lactate dehydrogenase (M(4)) gave one major peak of protein and enzymatic activity. The profiles of aldolase, glyceraldehyde-3-phosphate dehydrogenase, and yeast aldolases suggest random combinations of two closely related subunits into tetramers and dimers, respectively. The molecular heterogeneity of the other enzymes is not so easily related to subunit structure.
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PMID:Heterogeneity of presumably homogeneous protein preparations. 580 37

Red cell enzymes, 2,3-diphosphoglycerate (2,3-DPG) and adenosine triphosphate (ATP), were evaluated in a 23-mo-old boy with juvenile chronic myelocytic leukemia (JCML) at the onset of his illness and 6 mo later during the accelerated phase. The activities of the age-dependent red cell enzymes, hexokinase, aldolase, pyruvate kinase, and glucose-6-phosphate dehydrogenase, were elevated, as were the concentrations of red cell 2,3-DPG and ATP, consistent with a young red cell population metabolizing at an increased glycolytic rate. The activities of the non-age-dependent enzymes, glyceraldehyde-3-phosphate dehydrogenase (G3PD), phosphoglycerate kinase, and enolase, were also increased to levels similar to or greater than those observed in term infants. As the illness progressed, the activity of red cell G3PD increased further, and phosphoglucose isomerase activity increased markedly. These results are consistent with the prior suggestion that JCML represents a reversion to "fetal" erythropoiesis.
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PMID:Fetal erythropoiesis in juvenile chronic myelocytic leukemia. 622 20

Damage to the plasma membrane of rabbit epididymal spermatozoa during spontaneous lipid peroxidation was examined by means of trypan blue uptake and expression of activity of the intracellular enzymes, lactate dehydrogenase and pyruvate kinase. Both the dye uptake and the expression of enzyme activity probe cell damage from lipid peroxidation as loss of integrity of the plasma membrane. A linear correlation was obtained between trypan blue staining of the cells and malondialdehyde production, a quantifiable measure of the extent of lipid peroxidation. At the point of trypan blue staining of all cells, 0.5 nmol malondialdehyde/10(8) cells was produced. This is the same amount produced at the point of complete loss of motility and superoxide dismutase activity. We have defined this as the "lipoperoxidative lethal end point." Expression of lactate dehydrogenase and pyruvate kinase activities increased with time of aerobic incubation. In the high Na+ medium, NTP, in which lipid peroxidation is slow, there is a linear correlation between increase in expressed enzyme activities and malondialdehyde production. But in the high K+ medium, KTP, in which lipid peroxidation is rapid, there is an initial rapid rise in expressed enzyme activity over 3 h, followed by a slower increase. Activities of rabbit sperm lactate dehydrogenase, pyruvate kinase, and flagellar ATPase were unaffected by aerobic incubations for up to 48 h, double the incubation period used for the assay of enzymatic activities for the first two. The activity of glyceraldehyde-3-phosphate dehydrogenase decreased during aerobic incubation, the time course matching the loss of motility. The subcellular distribution of lactate dehydrogenase in rabbit spermatozoa was determined: 4% in the mitochondrial matrix, 10% in the plasma membrane and 85% in the cytosolic compartment.
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PMID:Assessment of cell damage caused by spontaneous lipid peroxidation in rabbit spermatozoa. 623 Oct 58

Activities of ten main metabolic pathway enzymes and seven lysosomal enzymes were determined in specimens from human normal palmar fascia and Dupuytren's contracture. The activities of the enzymes tested are 2-3 times higher in fresh specimens of Dupuytren's contracture. There are no differences in the activity distribution patterns of both these specimens, or in the absolute activities calculated in relation of the glyceraldehyde-3-phosphate dehydrogenase activities. With the exception of adenylate kinase and pyruvate kinase, the activities of main metabolic pathway enzymes based on the DNA content showed significantly lower activities in Dupuytren's contracture tissue than in palmar fascia. Lysosomal enzymes exhibit no significant differences of activity in the respective specimens. However, the lysosomal enzyme activities of cultured fibroblasts are lower than the corresponding activities from tissue specimens. The enzyme activities per DNA content in cultured fibroblasts are 10-50 times higher than in tissue specimens. The enzyme activities in cultured fibroblasts decrease with age or density of the cells in culture. The increased metabolic activity of the diseased tissues in Dupuytren's contracture is due to the higher cell content of the afflicted portions of the tissue, but individual enzymes show no qualitative changes in activity and there are no increases of enzyme activity per cell (DNA).
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PMID:A comparative study of the activity of lysosomal and main metabolic pathway enzymes in tissue biopsies and cultured fibroblasts from Dupuytren's disease and palmar fascia. On the pathobiochemistry of connective tissue proliferation, I. 627 Feb 31

In order to evaluate properly red cell metabolic data obtained in newborns with congenital hemolytic disorders, the unique metabolic characteristics and normal developmental changes that occur prenatally and postnatally are presented. The age-dependent red cell glycolytic enzymes (hexokinase, aldolase, pyruvate kinase) and glucose-6-phosphate dehydrogenase and most glycolytic intermediates are elevated at birth and at 11 to 12 months of age, consistent with the presence of a young red cell population the entire first year of life. However, certain red cell enzymes are elevated out of proportion to the age of the red cell population [phosphoglucose isomerase. glyceraldehyde-3-phosphate dehydrogenase, phosphoglycerate kinase (PGK), and enolase (ENO)] whereas others are decreased [phosphofructokinase (PFK), glutathione peroxidase, carbonic anhydrase, and others]. These metabolic characteristics are felt to be unique and representative of "fetal erythropoiesis." Activities of PGK and ENO decrease the PFK increases toward normal adult values beginning at eight to nine weeks of age. The concentration of glucose-6-phosphate steadily increases after birth and peaks at three to four weeks of age, at a time when PFK activity remains relatively unchanged, suggesting a relative block in glycolysis at the PFK step secondary to an enzyme with both decreased activity and altered kinetic properties (a "fetal" isozyme). Thus, evaluation of red cell enzyme and glycolytic intermediate data obtained in the first year of life should be related to the knowledge that a young red cell population is present and the characteristic unique metabolic red cell alterations described in cord blood persist beyond the immediate neonatal period.
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PMID:Red cell enzymopathies in the newborn. I. Evaluation of red cell metabolism. 628 May 78

Rat liver enzymes were used to study the relationship between their in vivo half-lives and their apparent hydrophobicity or their resistance to inactivation by mechanical shaking. The apparent hydrophobicity of these enzymes, measured as the percent of the protein recovered from an octyl-Sepharose column, is correlated with their known half-lives (r = 0.75, P less than 0.01). The presence of specific ligands which are known to increase compactness by impeding unfolding of proteins decreased the apparent hydrophobicity of fructose-1,6-bisphosphatase, glucose-6-phosphate dehydrogenase, glyceraldehyde-3-phosphate dehydrogenase, and pyruvate kinase. Resistance of enzymes to inactivation by mechanical shaking correlated well with their in vivo half-lives (r = 0.90, P less than 0.01). When the shaking experiments were done in the presence of substrates, fructose-1,6-bisphosphatase, glucose-6-phosphate dehydrogenase, glyceraldehyde-3-phosphate dehydrogenase and lactate dehydrogenase were protected from inactivation.
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PMID:Protein hydrophobicity and stability support the thermodynamic theory of protein degradation. 633 12

We present an analysis of glycolysis based on experimental findings and an interpretation based on concepts of efficiency, resonance response, and control features available in highly nonlinear reaction kinetics. We begin with a model for the glycolytic mechanism that is comprehensive, includes a large number of known activations and inhibitions of enzymes by metabolites, and couples the phosphofructokinase (PFKase) and the pyruvate kinase (PKase) reactions. The PFKase and PKase reactions and the coupling between them are modeled according to experimental information, but we do not attempt to model the glyceraldehyde-3-phosphate dehydrogenase-3-phosphoglycerate kinase reaction. We use experimental data to obtain the best estimates for the kinetic parameters and test the model by calculating the concentration variations of the intermediate metabolites. We confirm oscillatory behavior and calculate the ATP/ADP ratio and the free-energy dissipation for an extended range of the kinetic parameters as a function of the driving force for the glycolytic pathway, a measure of which is the total adenine nucleotide concentration. We find agreement of the calculated results with experimental findings except for the insufficiently represented reactions. Our model shows that the average ATP/ADP ratio is increased and the average free-energy dissipation is decreased in an oscillatory compared with a steady state mode of operation. The average values of the ATP/ADP ratio and of the free energy dissipation change abruptly past the onset of sustained oscillations.
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PMID:Oscillations and control features in glycolysis: numerical analysis of a comprehensive model. 645 92

Assay of maximal activities of 11 glycolytic enzymes in cell-free buffalo sperm extracts showed that hexokinase, phosphofructokinase and glyceraldehyde-3-phosphate dehydrogenase had the lowest activities, suggesting regulation of fructolysis at steps catalysed by these enzymes. The ratios of glyceraldehyde-3-phosphate dehydrogenase/phosphofructokinase (0.67) and phosphoglycerate kinase/phosphofructokinase (4.60) are typical of cells exhibiting high Pasteur effect (50% for ejaculated buffalo spermatozoa). The regulatory nature of phosphofructokinase was shown through its modulation by ATP, AMP and inorganic phosphate. The determination of fructolytic intermediates and cofactors and calculation of mass action ratios for each enzymic step revealed that hexokinase, phosphofructokinase, fructose-biphosphate aldolase, glyceraldehyde-3-phosphate dehydrogenase and pyruvate kinase catalysed reactions far removed from the equilibrium. A regulatory role by glyceraldehyde-3-phosphate dehydrogenase appeared to be most likely because triosephosphates and inorganic phosphate accumulated more under anaerobic than under aerobic conditions.
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PMID:REgulation of glycolysis/fructolysis in buffalo spermatozoa. 645 53


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