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:4.1.2.13 (aldolase)
3,461 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

1. The degradation rates and half-lives of hexokinase, 6-phosphogluconate dehydrogenase, lactate dehydrogenase, pyruvate kinase, glucose 6-phosphate dehydrogenase, phosphoglycerate kinase and aldolase were calculated from measurements of the decline in activities of these enzymes in rat small intestine during starvation. 2. The half-lives of the enzymes are: hexokinase, 5.7h; 6-phosphogluconate dehydrogenase, 7.6h; glucose 6-phosphate dehydrogenase, 6.0h; pyruvate kinase, 8.9h; lactate dehydrogenase, 8.7h; phosphoglycerate kinase, 8.7h; aldolase, 5.1h. 3. The significance of the results is discussed with respect to the regulation of enzyme concentrations in response to changes in diet.
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PMID:Degradation of glucose-metabolizing enzymes in the rat small intestine during starvation. 472 2

Clostridium thermocellum was shown to ferment glucose in a medium containing salts and 0.5% yeast extract. An active glucokinase was obtained with improved conditions for growth, assay, and preparation of cell extracts. Cell extracts appear to contain a glucokinase inhibitor that interferes with the assays at high protein concentrations. Glucokinase activity is stimulated about 60% by pretreatment with dithiothreitol. Little or no fructokinase or mannokinase activity was detected in cell extracts. The absence of glucokinase in mannitol-grown cells, the increase in glucokinase activity upon incubation of cell suspensions with glucose, and the lack of increase in activity when chloramphenical is added are evidence that glucokinase is an inducible enzyme. The following enzymes were detected in cell extracts (the enzyme activities are shown in parentheses are micromoles per minute per milligram or protein at 27 C): glucokinase (0.48), phosphoglucose isomerase (0.73), fructose 6-phosphate kinase (0.24), fructose diphosphate aldolase (0.59), glyceraldehyde 3-phosphate dehydrogenase (0.53), triose phosphate isomerase (0.13), phosphoglycerate kinase (0.20), phosphoglycerate mutase (0.20), enolase (0.28), pyruvic kinase (0.13), and lactic dehydrogenase (0.13). Glucose 6-phosphate dehydrogenase activity was absent or very low (0.0002) and 6-phosphogluconate dehydrogenase activity also was relatively low (0.015). From these data, it is proposed that carbohydrate metabolism in C. thermocellum proceeds by the Embden-Meyerhof pathway.
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PMID:Utilization of glucose by Clostridium thermocellum: presence of glucokinase and other glycolytic enzymes in cell extracts. 554 Oct 8

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

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

A marked reduction of granulocyte chemotactic function accompanies the storage of granulocyte concentrates. Since chemotaxis is energy dependent, we studied energy metabolism in stored neutrophils. We and others have reported that stored neutrophils have a defect in their energy metabolism. We found that defective adenosine triphosphate maintenance in stored neutrophils was occult in resting cells, but was unmasked by an energy-intensive stimulus, phagocytosis. In studies reported here, we sought to determine if defective adenosine triphosphate maintenance during granulocyte storage was related to altered glycolytic enzyme activity. We studied the activity of glycolytic enzymes in fresh and stored, resting and stimulated (opsonized zymosan) neutrophils. The following enzyme activities showed no major changes during storage, in resting or stimulated neutrophils: hexokinase, phosphofructokinase, aldolase, glucose phosphate isomerase, triose phosphate isomerase, glyceraldehyde phosphate dehydrogenase, phosphoglycerate kinase, phosphoglyceromutase, enolase, lactate dehydrogenase, glucose-6-phosphate dehydrogenase, glutathione reductase, and glutathione peroxidase. In contrast, pyruvate kinase activity consistently increased during storage. In 6 units, pyruvate kinase activity increased by 75 percent after 24 hours of storage at room temperature and by 198 percent after 48 hours. The storage-associated increase in pyruvate kinase activity was not inhibited by cycloheximide. Stimulation of neutrophils by phagocytosis of opsonized zymosan also produced striking increases in the pyruvate kinase activity of both fresh and stored cells. Additional studies indicated that the increases in pyruvate kinase activity observed during storage and after phagocytosis were associated with an increase in the availability of pyruvate kinase activity in the supernatant fraction of neutrophil sonicates. Total pyruvate kinase activity in sonicates of neutrophils was unchanged by storage or particle ingestion.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Glycolytic enzymes of stored granulocytes. 632 24

Evidence is presented for the occurrence of glycosomes (organelles resembling peroxisomes) in four major species of Leishmania (viz. L. major, L.m. mexicana, L. b. braziliensis and L. donovani), based on latency as well as differential and isopycnic centrifugation studies. The enzymes involved in glycolysis; (hexokinase, phosphoglucose isomerase, phosphofructokinase, fructose-1,6-bisphosphate aldolase, triosephosphate isomerase, glyceraldehyde-phosphate dehydrogenase and phosphoglycerate kinase); glycerol metabolism (sn-glycerol-3-phosphate dehydrogenase and glycerol kinase); carbon dioxide fixation (phosphoenolpyruvate carboxykinase and possibly malate dehydrogenase); together with an enzyme involved in the beta-oxidation of fatty acids (3-beta-hydroxybutyryl coenzyme A dehydrogenase); a key enzyme in the synthesis of ether lipids (dihydroxyacetone phosphate acyltransferase) as well as the ADP utilising enzyme adenylate kinase, were all found associated, at least in part, with a subcellular organelle which had a buoyant density in sucrose gradients of 1.21 to 1.24 g cm-3. Little variance in enzyme composition was found between the different species of Leishmania or in comparison with other members of the Trypanosomatidae, supporting the unifying principle that glycosomes are a unique characteristic of this family. The occurrence of important catabolic, anabolic and anaplerotic pathways in the glycosomes of Leishmania renders them prime targets for chemotherapy.
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PMID:The occurrence of glycosomes (microbodies) in the promastigote stage of four major Leishmania species. 644 18

The activities of red cell enzymes enolase (ENO), phosphoglycerate kinase (PGK), phosphofructokinase (PFK), glucose-6-phosphate dehydrogenase (G-6-PD), hexokinase (HK), aldolase (ALD), and pyruvate kinase (PK) were followed sequentially in term infants from birth to one year of age. At birth, red cell PGK and ENO activities were disproportionately elevated when compared to both red cells with a similar mean cell age and those with a younger mean cell age; red cell PFK was significantly decreased. There was a progressive full in PGK and ENO activities and rise in PFK levels toward normal values in the first year of life. The most significant changes in PGK, ENO, and PFK appeared to begin at 8 to 9 wk of age. ENO and PFK activities stabilized at approximately 5 to 6 months of age at values compatible with mean cell age; mean PGK levels remained mildly elevated at 11 to 12 months. The age-dependent enzymes G-6-PD, PK, ALD, and HK were all elevated in term newborns. G-6-PD and ALD progressively decreased in activity during the first year of life. PK and HK decreased in activity until 8 to 9 wk when there was a secondary rise in mean activity. Mean red cell G-6-PD, PK, ALD, and HK levels remained mildly to moderately elevated at 11 to 12 months of life, suggesting the persistence of a relatively young red cell population throughout the first year of life.
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PMID:Red cell metabolic alterations in postnatal life in term infants: glycolytic enzymes and glucose-6-phosphate dehydrogenase. 645 61

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

A method is presented for the simultaneous purification of hexokinase, fructose-bisphosphate aldolase, triosephosphate isomerase and phosphoglycerate kinase, and the partial purification of glycerol-3-phosphate dehydrogenase (NAD+), 6-phosphofructokinase, glucosephosphate isomerase, and glycerol kinase from Trypanosoma brucei. As a first step, the glycosomes, microbody-like organelles of Trypanosomatidae, containing almost exclusively enzymes involved in glucose and glycerol metabolism [Opperdoes, F. R. and Borst, P. (1977) FEBS Lett. 80, 360-364], were purified eightfold from homogenates with an average yield of 38%. Subsequently, the glycosomal content was subjected to hydrophobic interaction chromatography on phenyl-Sepharose. This step results in pure hexokinase (15% final yield) and almost pure triosephosphate isomerase, while the other glycosomal enzymes elute as mixtures of two or three enzymes. Triosephosphate isomerase was further purified to homogeneity on CM-cellulose (33% final yield), while phosphoglycerate kinase and fructose-bisphosphate aldolase were separated from each other and purified to homogeneity by affinity chromatography using ATP-Sepharose (25% and 30% final yields, respectively). Fructose-bisphosphate aldolase was further characterized as a typical class I enzyme.
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PMID:Simultaneous purification of hexokinase, class-I fructose-bisphosphate aldolase, triosephosphate isomerase and phosphoglycerate kinase from Trypanosoma brucei. 648 38

Highly purified glycosomes were isolated from Trypanosoma brucei bloodstream forms and cultured procyclic trypomastigotes. A comparison of the specific activities of glycosomal enzymes revealed that glycosomes from insect stages had decreased levels of hexokinase, phosphoglucose isomerase, phospho-fructokinase, fructose-bisphosphate aldolase, glyceraldehyde-phosphate dehydrogenase and phosphoglycerate kinase, but contained increased levels of adenylate kinase, malate dehydrogenase and phosphoenolpyruvate carboxykinase. Glycosomes from bloodstream forms were almost totally devoid of the latter two activities. Comparison of the two types of glycosomes by sodium dodecylsulphate-polyacrylamide gel electrophoresis revealed that bloodstream form glycosomes contained 3 prominent polypeptides (64, 46 and 40 kDa) which were hardly detectable in insect stage glycosomes, whereas the latter contained 3 insect stage specific bands with molecular weight of 34 000, 61 000 and 77 000 and 4 additional bands with molecular weights between 94 000 and 110 000. Both types of glycosome contained the phospholipids phosphatidylcholine and phosphatidylethanolamine. Insect stage glycosomes contained in addition also phosphatidylinositol and some phosphatidylserine.
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PMID:A comparison of the glycosomes (microbodies) isolated from Trypanosoma brucei bloodstream form and cultured procyclic trypomastigotes. 674 87


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