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)

A protease from Tetrahymena pyriformis inactivated eight of nine commercially available enzymes tested, including lactate deyhdrogenase, isocitrate dehydrogenase (TPN-specific), glucose-6 phosphate dehydrogenase, D-amino acid oxidase, fumarase, pyruvate kinase, hexokinase, and citrate synthase. Urate oxidase was not inactivated. Inactivation occurred at neutral pH, was prevented by inhibitors of the protease, and followed first order kinetics. In those cases tested, inactivation was enhanced by mercaptoethanol. Most of the enzyme-inactivating activity was due to a protease of molecular weight 25,000 that eluted from DEAE-Sephadex at 0.3 M KCl. A second protease of this molecular weight, which was not retained by the gel, inactivated only isocitrate dehydrogenase and D-amino acid oxidase. These two proteases could also be distinguished by temperature and inhibitor sensitivity. Two other protease peaks obtained by DEAE-Sephadex chromatography had little or no no enzyme inactivating activity, while another attacked only D-amino acid oxidase. At least six of the enzymes could be protected from proteolytic inactivation by various ligands. Isocitrates dehydrogenase was protected by isocitrate, TPN, or TPNH, glucose-6-dehydrogenase by glucose-6-P or TPN, pyruvate kinase by phosphoenolypyruvate or ADP, hexokinase by glucose, and fumarase by a mixture of fumarate and malate. Lactate dehdrogenase was not protected by either of its substrates of coenzymes. Citrate synthase was probably protected by oxalacetate. Our data suggest that the protease or proteases discussed here may participate in the inactivation or degradation of a least some enzymes in Tetrahymena. Since the inactivation occurs at neutral pH, this process could be regulated by variations in the cellular levels of substrates, coenzymes, or allosteric regulators resulting form changes in growth conditions or growth state. Such a mechanism would permit the selective retention of enzymes of metabolically active pathways.
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PMID:Enzyme inactivation by a cellular neutral protease: enzyme specificity, effects of ligands on inactivation, and implications for the regulation of enzyme degradation. 1 68

Clinical and hematological studies were performed on ten homozygous and seven heterozytous individuals with pyruvate kinase deficiency, aged between 2 and 71 years. Five of the homozygotes were splenectomized. With the exception of a decreased enzyme activity between 41 and 55 per cent and minor changes in their red cell metabolism the heterozygotes showed no abnormal results. In the homozygotes the following results could be demonstrated: 1. Pyruvate kinase activity was decreased to 11 to 35 per cent of normal enzyme activity. 2. There is no relation between the severity of hemolysis and the degree of the enzyme defect. 3. The reticulocyte counts correlated inversely with the hemoglobin concentrations. 4. There is a close correlation between the activities of hexokinase, phosphofructokinase, glucose-6-phosphate dehydrogenase and glutamate oxalacetate transaminase on the one side and reticulocyte counts on the other. 5. Adenosine triphosphate or adenosine reduced the increased autohemolysis in all cases. 6. Following splenectomy, anemia was less pronounced than before. Splenectomized patients did not need further transfusions, though hemolysis persisted.
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PMID:[Pyruvate kinase deficiency. I. Clinical and hematological observations (author's transl)]. 12 93

Strains of Giardia lamblia were isolated from symptomatic cases of giardiasis and axenized in the laboratory. Electrophoretic mobility patterns of four enzymes, viz., EC 5.3.1.9 glucose phosphate isomerase (GPI); EC 1.1.1,4.0.L-malate; NADP+ Oxidoreductase (Oxaloacetate decarboxylating) (ME); EC 2.7.5.1 phosphoglucomutase (PGM); and EC 2.7.1.1 hexokinase (HK) of the lysates prepared from these isolates were studied using starch-gel. Based on differences in mobility patterns of PGM and HK, the four strains studied could be grouped into three different isoenzyme types (Zymodemes). ME mobility was identical in all the four strains. Some relative difference was seen in the mobility of GPI, though the pattern of mobility was similar in all the strains.
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PMID:Isoenzyme studies of Giardia lamblia isolated from symptomatic cases. 294 57

Stocks of intestinal amoebae isolated from hospital patients in Mexico City and grown in monoxenic culture were compared among themselves and with those already described (SARGEAUNT & WILLIAMS, 1979), using the electrophoretic patterns of four enzymes: glucose phosphate isomerase (GPI), phosphoglucomutase (PGM), L-malate:NADP+ oxido-reductase (oxalacetate-decarboxylating) (ME) and hexokinase (HK). New isoenzyme groups (SARGEAUNT & WILLIAMS, 1979) of all the amoebae, including Entamoeba histolytica have been demonstrated. Amongst these have been found seven more groups of E. histolytica, two new groups of E. hartmanni, one new group of Dientamoeba fragilis and one new group of E. coli. Of the seven new groups of E. histolytica three are known to originate from patients with clinical amoebiasis whilst the remainder are from asymptomatic subjects. Only 11.2% of the 125 isolations were associated with clinical amoebiasis, and these are clearly distinguished from the isolations from asymptomatic patients by their electrophoretic isoenzyme pattern.
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PMID:The epidemiology of Entamoeba histolytica in Mexico City. A pilot survey I. 625 79

Stocks of intestinal amoebae grown in monoxenic culture, were compared against each other and against those previously reported from Mexico City. These were isolated from subjects in San Cristobal de las Casas, Chiapas (rural area) and hospital patients in Merida, Yucatan (urban area). Electrophoretic patterns of the four enzymes: glucose phosphate isomerase (GPI), phosphoglucomutase (PGM), L-malate: NADP+ oxido-reductase (oxalacetate-decarboxylating) (ME) and hexokinase (HK) demonstrated the presence of five groups (zymodemes) of Entamoeba histolytica already described from Mexico City, together with two new zymodemes, one of which gave a recognizable pathogenic pattern, whilst the other gave a contradictory pattern. Zymodemes of Entamoeba coli, Entamoeba hartmanni, Iodamoeba buetschlii and Dientamoeba fragilis, previously described were also isolated. One new zymodeme of D. fragilis was demonstrated.
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PMID:The epidemiology of Entamoeba histolytica in a rural and an urban area of Mexico. A pilot survey II. 628 56

Using a biphasic culture medium, stocks of intestinal amoebae were isolated from a group of children attending school in Durban, South Africa. These were compared with stocks collected in other areas of the world already characterized using the electrophoretic patterns of four enzymes: glucose phosphate isomerase (GPI), phosphoglucomutase (PGM) L-malate: NADP+ oxido-reductase (oxalacetate-decarboxylating) (ME) and hexokinase (HK). 33% of 94 samples grew Entamoeba histolytica, only one of which gave a pattern indicative of a pathogenic stock. Entamoeba hartmanni, Dientamoeba fragilis and Entamoeba coli were also grown from some samples, increasing the total positive samples for all species isolated to 40%.
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PMID:A zymodeme study of Entamoeba histolytica in a group of South African schoolchildren. 628 86

Steady state sensitivity analysis of a model of carbohydrate metabolism and anaplerotic synthesis of oxalacetate were, in Aspergillus niger under conditions of citric acid accumulation, carried out. The flux and metabolite concentration control structure of the system obtained shows that the hexokinase/substrate transport step is the main controlling step of the pathway. The quantitative contribution of the other enzyme catalyzed or transport steps are also discussed. These results allow the design of a proper strategy of biotechnological manipulation aimed at improvement of the process.
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PMID:Modeling approach to control of carbohydrate metabolism during citric acid accumulation by Aspergillus niger: II. Sensitivity analysis. 1861 53

1. Electron microscopic studies of the sieve tube sap obtained from the secondary phloem of Robinia pseudoacacia by the method of Hartig (1860) showed the presence of well developed mitochondria in addition to membrane fragments. 2. In this sieve tube sap the following enzymes could be detected qualitatively: UTP-glucose-1-phosphate-uridyl transferase, UDPG-fructose glucosyl transferase, glucose-6-phosphate dehydrogenase, hexokinase (for glucose and fructose), phosphohexose isomerase, phosphofructokinase, and UDPG-pyrophosphatase. 3. The following enzymes were determined quantitatively: phosphorylase, amylase, aldolase, triosephosphate isomerase, NAD(+)-dependent glyceraldehyde-3-phosphate dehydrogenase, phosphoglyceromutase, enolase, pyruvate kinase, pyruvate decarboxylase, alcohol dehydrogenase, isocitrate dehydrogenase, fumarase, malate dehydrogenase, glutamate-pyruvate transaminase, glutamate dehydrogenase, glutamate-oxalacetate transaminase, and anorganic pyrophosphatase. 4. The following enzymes could not be detected: UDGP dehydrogenase, UDPG-fructose-6-phosphate-glucosyltransferase, invertase, phosphoglucomutase, lactate dehydrogenase, and citrate synthase. 5. The enzyme pattern in the sieve tube saps of Tilia platyphyllos, Carpinus betulus, Fraxinus americana, Quercus borealis maxima, and Salix viminalis is qualitatively similar to that of Robinia, but shows quantitative differences (as far as analyzed). 6. The meaning of the results for the metabolism and function of the sieve tubes in situ is discussed.
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PMID:[Enzyme activities in the sieve tube sap of Robinia pseudoacacia L. and of other tree species]. 2449 58