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)

Enzyme abnormalities are frequently found in the red cells of patients with various acquired blood disorders. In leukaemias, preleukaemic states and bone marrow insufficiencies with or without sideroblastosis, changes in enzyme activity are usually characterized by the coexistence of deficiency of some enzymes and an increased activity of others. The most frequently decreased activities are those of pyruvate kinase, phosphofructokinase,2,3-diphosphoglycerate mutase and adenylate kinase; the most frequently increased activities are those of hexokinase, aldolase, enolase, 6-phosphogluconate dehydrogenase and glucose-6-phosphate dehydrogenase. In primary myelofibrosis and in polycythaemia rubra vera, enzyme deficiencies are infrequent and differ from those observed in leukaemias and related disorders. Phosphohexose isomerase and phosphoglucomutase deficiencies seem relatively specific for polycythaemia rubra vera. Explanations for the acquired enzymopathies are still at the stage of hypothesis. The theory of multiple genetic damage may explain some findings but has not yet been proved right. The possibility of post-translational molecular modification is suggested as a working hypothesis.
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PMID:Acquired erythroenzymopathies in blood disorders: study of 200 cases. 107 44

The erythrocytes of 350 pigtailed macaques (Macaca nemestrina) were examined for electrophoretic variation of hemoglobin and 26 enzymes. Seven enzymes showed variation in more than 1% of individuals: phosphoglucose isomerase, phosphoglucomutase-1, soluble NADP-dependent isocitric dehydrogenase, peptidase A, peptidase C, 2,3-diphosphoglycerate mutase, and acid phosphatase. Variation with lesser frequency was found in soluble glutamic-oxalacetic transaminase, phosphoglycerate kinase, lactic dehydrogenase, and hemoglobin. Only eight samples were tested for esterase D, and one of these had a variant phenotype. Enzymes with no clear variation were adenylate kinase, adenosine deaminase, phosphofructokinase, hexokinase, pyruvate kinase, glyceraldehyde 3-phosphate dehydrogenase, aldolase, phosphoglycerate mutase, phosphopyruvate hydratase (enolase), phosphoglucomutase-3, and superoxide dismutase. There was father-to-son transmission of PGI, PGM-1, peptidase C, 6PGD, 2,3-DPGAM, NADP-ICD, and acid phosphatase variants, suggesting that these loci are autosomal as in man.
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PMID:Intraspecific red cell enzyme variation in the pigtailed macaque (Macaca nemestrina). 114 87

The age changes of 2,3-DPG concentration, 2,3-diphosphoglycerate mutase, hexokinase and pyruvate kinase activities in pigs erythroid cells during the first 10 days after birth have been investigated for study of the mechanism of blood oxygen-transport function regulation at the early stages of postnatal adaptation. It was established, that there are age peculiarities in young, mature and old erythrocytes metabolism in piglets during the transition to postnatal development. It was shown that the rise of 2,3-DPG, the allosteric effector of hemoglobin oxygen affinity level, is due to the increased activities of 2,3-diphosphoglycerate mutase and hexokinase after birth, that is particularly characteristic of the young pigs erythrocytes.
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PMID:[Activity of enzymes of glycolysis in pig erythrocytes in the neonatal period]. 774 43

The age dynamics of activities of enzymes which catalysis several stages of metabolism (hexokinase, phosphofructokinase, pyruvate kinase, lactate dehydrogenase, 2,3-diphosphoglycerate mutase, glucose-6-phosphate dehydrogenase, isocitrate dehydrogenase and cytochrome oxidase) and antioxidant system (superoxide dismutase, glutathione peroxidase and glutathione reductase) was studied in the bone marrow erythroid cells of pig during the 10-day period after birth as well as in the cells of 30 days old animals. It was established that in the neonatal period of development the reorganization of energy metabolism in pig bone marrow erythrokaryocytes took place. It consisted in the intensification of oxidative processes and in a great measure was directed on the activation of 2,3-diphosphoglycerate mutase formation in the nature red cells. During the early period after birth the activation of antioxidant system in erythroid cells of pig bone marrow was observed.
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PMID:[Changes in various links of metabolism and the antioxidant system in the bone marrow erythroid cells of the pig during the neonatal period]. 1044 74

The kinetic parameters of the 10 glycolytic enzymes and glycolytic fluxes were determined for the first time in Ustilago maydis. Enzyme activities in yeast grown in minimal medium and harvested in the stationary stage were twofold higher than those from yeast grown in rich medium. In contrast, in yeast harvested in the exponential stage, the enzyme activities were higher in cells grown in rich medium. Phosphofructokinase activity was the lowest in the four culture conditions analyzed, suggesting that this enzyme is a flux-controlling step in U. maydis glycolysis. The V(max) and K(m) values of hexokinase and pyruvate kinase were similar under all conditions. The results revealed that U. maydis aldolase belongs to the class II type of metalo-aldolases. 3-Phosphoglycerate mutase (PGAM) activity was 2,3-bisphosphoglycerate cofactor independent, which contrasted with the cofactor dependency predicted by the amino acid sequence alignment analysis. Pyruvate was secreted by U. maydis yeast in the presence and absence of external glucose. The glycolytic enzyme activities in the U. maydis mycelial form were similar to those found in yeast, except for one order of magnitude higher phosphofructokinase and PGAM activities, thus suggesting differences in the glycolysis regulatory mechanisms between the two cellular forms.
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PMID:Glycolysis in Ustilago maydis. 1880 52