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:2.7.1.1 (hexokinase)
5,274 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The specific activity of hexokinase, phosphofructokinase, aldolase, enolase, pyruvate kinase and glucose-6-phosphate dehydrogenase was measured in 41 smooth muscle cell tumors: 20 leiomyomas and 21 cases of leiomyosarcoma. Statistical analysis revealed no significant differences in specific activity between normal smooth muscle tissue and the benign and malignant tumors originating from it. Quantification of the isozyme composition of pyruvate kinase showed a significant shift in isozyme pattern towards K-type subunits in leiomyosarcomas as compared to leiomyomas.
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PMID:Activity of glycolytic enzymes and glucose-6-phosphate dehydrogenase in smooth muscle proliferation. 237 98

Effect of three antiandrogens: cyproterone acetate (5 mg/day, sc), flutamide (5 mg/day, sc) and STS-557 (5 mg/day, po) and an estrogen, estradiol dipropionate (5 micrograms/day, sc) on some key enzymes of carbohydrate metabolism was investigated in adult rat epididymis and ventral prostate. Antiandrogens were administered for 21 days and estrogen for 14 days. All of them caused a significant decrease in the weight of epididymis, seminal vesicles and ventral prostate. A significant decrease in the specific activities of enzymes (hexokinase, phosphofructokinase, aldolase, glyceraldehyde phosphate dehydrogenase, pyruvate kinase, glucose-6-phosphate dehydrogenase and 6-phosphogluconate dehydrogenase) occurred only in the organs of estrogen treated rats; activities of some of the enzymes were lowered also in the prostate of STS-557 treated rats. Flutamide and cyproterone acetate were ineffective in this regard. The possible factors responsible for the ineffectiveness of synthetic antiandrogens in influencing epididymal metabolism are discussed.
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PMID:Effect of antiandrogens on some key enzymes of glycolysis in epididymis and ventral prostate of rat. 253 Jan 66

The toxic nature of the secondary metabolite of Penicillium patulum has been studied in rats. Liver, Kidney and Intestine of the experimental animals showed derangement in carbohydrate metabolism. Changes in the concentration of a few key enzymes in carbohydrate metabolism have also been studied. Glycogen phosphorylase is found to be markedly increased while the glycolytic enzymes like hexokinase and aldolase are significantly lowered. Gluconeogenesis is stimulated and this is evidenced by increased glucose-6-phosphatase and fructose-1,6-diphosphatase activity. Our results revealed that, patulin, the secondary metabolite of Penicillium patulum showed toxicity in all the organs studied.
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PMID:Effect of patulin on some enzymes of carbohydrate metabolism studied in rats. 255 6

Intensity of glycolysis and the pentose phosphate cycle in staphylococci sensitive and resistant to novobiocin was studied. The resistant variants did not practically store lactate and the activity of glycolytic enzymes i.e. hexokinase and aldolase was lowered by 15-20 and 53-59 per cent, respectively. Monoiodoacetate, a glycolysis inhibitor suppressed the glucose oxidation rate by 53.3-66.9 per cent in the sensitive variants and by 16-21.8 per cent in the resistant variants. At the same time it was characteristic of the resistant variants to increase the activity of the pentose phosphate cycle enzymes; glucose-6-phosphate dehydrogenase by 25-38.1 per cent transketolase by 21.5-27.3 per cent and transaldolase by 30-57.1 per cent. No differences in the transhydrogenase reaction kinetics of both the novobiocin sensitive and the novobiocin resistant variants were observed.
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PMID:[Features of glycolysis and pentose phosphate pathway in novobiocin sensitive and novobiocin resistant staphylococci]. 273 Feb 11

Energy metabolism in proliferating cultured rat thymocytes was compared with that of freshly prepared non-proliferating resting cells. Cultured rat thymocytes enter a proliferative cycle after stimulation by concanavalin A and Lymphocult T (interleukin-2), with maximal rates of DNA synthesis at 60 h. Compared with incubated resting thymocytes, glucose metabolism by incubated proliferating thymocytes was 53-fold increased; 90% of the amount of glucose utilized was converted into lactate, whereas resting cells metabolized only 56% to lactate. However, the latter oxidized 27% of glucose to CO2, as opposed to 1.1% by the proliferating cells. Activities of hexokinase, 6-phosphofructokinase, pyruvate kinase and aldolase in proliferating thymocytes were increased 12-, 17-, 30- and 24-fold respectively, whereas the rate of pyruvate oxidation was enhanced only 3-fold. The relatively low capacity of pyruvate degradation in proliferating thymocytes might be the reason for almost complete conversion of glucose into lactate by these cells. Glutamine utilization by rat thymocytes was 8-fold increased during proliferation. The major end products of glutamine metabolism are glutamate, aspartate, CO2 and ammonia. A complete recovery of glutamine carbon and nitrogen in the products was obtained. The amount of glutamate formed by phosphate-dependent glutaminase which entered the citric acid cycle was enhanced 5-fold in the proliferating cells: 76% was converted into 2-oxoglutarate by aspartate aminotransferase, present in high activity, and the remaining 24% by glutamate dehydrogenase. With resting cells the same percentages were obtained (75 and 25). Maximal activities of glutaminase, glutamate dehydrogenase and aspartate aminotransferase were increased 3-, 12- and 6-fold respectively in proliferating cells; 32% of the glutamate metabolized in the citric acid cycle was recovered in CO2 and 61% in aspartate. In resting cells this proportion was 41% and 59% and in mitogen-stimulated cells 39% and 65% respectively. Addition of glucose (4 mM) or malate (2 mM) strongly decreased the rates of glutamine utilization and glutamate conversion into 2-oxoglutarate by proliferating thymocytes and also affected the pathways of further glutamate metabolism. Addition of 2 mM-pyruvate did not alter the rate of glutamine utilization by proliferating thymocytes, but decreased the rate of metabolism beyond the stage of glutamate significantly. Formation of acetyl-CoA in the presence of pyruvate might explain the relatively enhanced oxidation of glutamate to CO2 (56%) by proliferating thymocytes.
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PMID:Glutamine and glucose metabolism during thymocyte proliferation. Pathways of glutamine and glutamate metabolism. 286 9

Past work, including our computer simulation of cardiac energy metabolism, indicates that magnesium is an important coherent controller of glycolysis and the Krebs cycle. Many of the glycolytic enzymes are sensitive to Mg2+. The most important effect is due to MgATP2-being a cofactor for a number of these enzymes while other chelation forms are inactive or inhibitory. The means by which Mg2+ and Mg2+ chelates of adenine nucleotides regulate the most important glycolytic enzymes--hexokinase, phosphofructokinase, aldolase, phosphoglycerate kinase, and pyruvate kinase--are described in detail. Creatine kinase, which is important in energy metabolism and highly sensitive to both metal ions and pH, is also discussed. It is necessary to properly control the composition of assay mixtures (particularly with regard to metal ions) in order to determine what actually regulates the activity of an enzyme.
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PMID:Magnesium regulation of the glycolytic pathway and the enzymes involved. 293 60

We have developed a method for the simultaneous purification of hexokinase, glucosephosphate isomerase, phosphofructokinase, fructose-1,6-bisphosphate aldolase, triosephosphate isomerase, D-glyceraldehyde-phosphate dehydrogenase, phosphoglycerate kinase, glycerol-3-phosphate dehydrogenase and glycerol kinase from Trypanosoma brucei in yields varying over 8-55%. Crude glycosomes were prepared by differential centrifugation of cell homogenates. Subsequent hydrophobic interaction chromatography on phenyl-Sepharose resulted in six pools containing various mixtures of enzymes. These pools were processed via affinity chromatography (immobilized ATP), hydrophobic interaction chromatography (octyl-Sepharose) and ion-exchange chromatography (CM- and DEAE-cellulose) which resulted in the purification of all nine enzymes. The native enzyme and subunit molecular masses, as determined by gel filtration and gel electrophoresis under denaturing conditions, were compared with those of their homologous counterparts from other organisms. Trypanosomal hexokinase is a hexamer and differs in subunit composition from the mammalian enzymes (monomers) as well as in subunit size (51 kDa versus 96-100 kDa, respectively). Phosphofructokinase only differs in subunit size (51 kDa for T. brucei versus 80-90 kDa for mammals) but had identical subunit composition (tetrameric). The others all have the same subunit composition as their mammalian counterparts. Except for triosephosphate isomerase, all Trypanosoma enzymes have subunits which are 1-5 kDa larger in size. Together these nine enzymes contribute 3.3 +/- 1.6% to the total cellular protein of T. brucei and at least 90% to the total glycosomal protein. A comparison of calculated intraglycosomal concentrations of the enzymes with the glycosomal metabolite concentrations shows that in the case of aldolase, glyceraldehyde-phosphate dehydrogenase and phosphoglycerate kinase, the concentration of active sites is of the same order of magnitude as that of their reactants. A common feature of the glycosomal glycolytic enzymes (with the exception of glucosephosphate isomerase) is that they are highly basic proteins with pI values between 8.8 and 10.2, values which are 1-4 higher than in the case of their mammalian cytosolic counterparts and 3-6 higher than in the case of the various unicellular organisms. It is suggested that both the larger subunit size and the basic character of the T. brucei glycolytic proteins are involved in the routing of the enzymes from their site of biogenesis (the cytosol) towards their site of action (the glycosome).
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PMID:Glycolytic enzymes of Trypanosoma brucei. Simultaneous purification, intraglycosomal concentrations and physical properties. 294 90

Isoenzyme patterns of adult Malaysian Schistosoma, S. mekongi and S. japonicum strains were analysed by isoelectric focusing (IEF) in polyacrylamide gel. Enzyme patterns obtained from Malaysian Schistosoma homogenates differed from those of S. mekongi and S. japonicum strains. Malaysian Schistosoma was found to differ from S. japonicum by 8 enzymes, namely phosphoglucomutase, phosphoglucoisomerase, malate dehydrogenase, acid phosphatase, hydroxy-butyrate dehydrogenase, hexokinase and alkaline phosphatase, and from S. mekongi by phosphoglucomutase, malate dehydrogenase, aldolase and alkaline phosphatase. These results and the distinct biology of the parasite suggest that Malaysian Schistosoma is a new species in the S. japonicum complex.
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PMID:Isoenzyme analyses of Malaysian Schistosoma, S. mekongi and S. japonicum by isoelectric focusing in polyacrylamide gel. 294 Jun 88

The transmural distribution of five glucose metabolizing enzymes (hexokinase; glucose-6-phosphate dehydrogenase; phosphofructokinase; aldolase; and lactate dehydrogenase) were explored in the left and in the right ventricle wall of rat, ox and pig hearts. The levels of most of these enzyme activities were different in the different animal species and (within the same species) in the two ventricles. Most of these enzyme activities were found to be non-uniformly distributed across the left (but not across the right) ventricle wall. Differences in the transmural distribution of enzyme activities were detected among the three examined mammalian species.
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PMID:Transmural distribution of glucose metabolizing enzymes across the left and the right ventricle heart walls in three different mammalian species. 294 92

The age-related changes in the activities of five glucose-metabolizing enzymes (hexokinase, HK; glucose-6-phosphate dehydrogenase, G6P-DH; aldolase, ALD; phosphofructokinase, PFK; and lactate dehydrogenase, LDH) were investigated in the walls of left and right ventricles of rats of various age-groups (1-24 months). Age-related changes were found in the activities of all of the enzymes in both ventricles during growth (with significant decreases between 2 and 6 months of age) and in the levels of PFK and LDH in the left ventricle during ageing (with a significant increase between 12 and 24 months of age). The distribution of the enzyme activities across the wall of both ventricles was quite uniform in young, adult and mature rats (the distribution of G6P-DH activity in the left ventricle wall at 2 months of age was the only notable exception) but became non-uniform in the old rats with regard to G6P-DH, PFK, LDH and probably HK in the left ventricle and G6P-DH and HK in the right ventricle. These data support the hypothesis that alterations connected with ageing do not lead to a generalized decline of cardiac metabolic capacity, and that they are also the result of specific adaptive modifications, perhaps related to alteration in the distribution of the work load and/or of nutrition across the ventricular wall.
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PMID:Changes in the transmural distribution of glucose-metabolizing enzymes across the left and right ventricular wall of rat heart during growth and ageing. 296 12


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