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 metabolic activity of the red cell glycolytic pathway hexose monophosphate shunt (HMP) with dependent glutathione system was studied in patients with hyperthyroidism (n = 10), hyperlipoproteinemia (n = 16), hypoglycemia (n = 25) and hyperglycemia (n = 23). In uncontrolled diabetics and patients with hyperthyroidism the mean value of glucose phosphate isomerase (GPI), glucose-6-phosphate dehydrogenase (G-6-PD), glutathione reductase (GR) was increased, whereas these enzyme activities were reduced in patients with hypoglycemia. Apart from a few values of hexokinase (HK) which were lower than normal the results in hyperlipoproteinemia patients remained essentially unchanged, including the intermediates such as 2,3-diphosphoglycerate (2,3-DPG), adenosine triphosphate (ATP) and reduced glutathione (GSH). While increased rates of 2,3-DPG and ATP in hypoglycemia patients were obtained, these substrates were markedly reduced in diabetics.
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PMID:Adaptation of red cell enzymes and intermediates in metabolic disorders. 12 51

The regularities for changes were established in activity of hexokinase, glucokinase, glucosephosphate-isomerase, phosphofructokinase and glucose-6-phosphate dehydrogenaseduring the early development of loach (Misgurnus fossilis). It was found that a 30-minute incubation of fertilized loach eggs in the lactate or fumarate solutions decreases the glucokinase activity in the embryos of 3, 6, 9, 12, 15, 18 and 24 hours of their development, while the inhibitory effect of glucose on the enzyme activity is pronounced only after 18 and 24 hours of the development. A significant increase in the hexokinase and glucose-6-phosphate dehydrogenase activities under the above-mentioned conditions is observed only under the effect of glucose 9 and 6 and 9 hours, respectively, after fertilization. The glucose phosphate isomerase and phosphofructokinase activites under the effect of used compounds undergo no changes during the primary stages of embryogenesis.
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PMID:[Enzymes of glycolysis and pentosephosphate shunt during early embryogenesis of the loach and the effect of glucose, lactate and fumarate on fertilized oocytes]. 12 65

Administration of 60,000 i.e. of vitamin A into rats within three weeks caused an increase in amount of reticulocytes, in the rate of glucose utilization and in formation of lactic acid by erythrocytes. The activity of glycolytic enzymes was intensified. The activity of hexokinase was increased by 84.6%, activities of aldolase and phosphohexoisomerase were increased by 34%. But in the erythrocytes content of AMP, ADP and ATP was unaltered, probably due to activation of total and Na+, K+-dependent ATPase. The harmful effect of an excess of the vitamin A was manifested in an increased content of Na+ in erythrocytes and also in decreased stability of the cells to acid hemolytics.
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PMID:[Intensity of glycolysis and energy metabolism in erythrocytes in experimental hypervitaminosis A]. 13 57

Adipose tissue and liver from vitamin B6-deficient rats have an increased lipogenic capacity. Whether this phenomenon is accompanied by changes in the activities of certain enzymes involved in the metabolism of carbohydrate and lipid, or by altered transport of glucose into adipocytes, has been studied. Five glycolytic enzymes (hexokinase, phosphoglucose isomerase, phosphofructokinase, aldolase, and pyruvate kinase), two pentose phosphate pathway enzymes (glucose-6-phosphate dehydrogenase and 6-phosphogluconate dehydrogenase), malic enzyme, and ATP citrate lyase were measured in the epididymal adipose tissue, livers and kidneys of vitamin B6-deficient and control rats. Vitamin B6 deficiency did not significantly affect the glycolytic enzyme levels in the tissues studied, or the dehydrogenases measured in adipose tissue and kidneys. Liver glucose-6-phosphate dehydrogenase, and adipose tissue and liver malic enzyme were significantly lowered in deficient rats compared to ad libitum and pair-fed controls. Adipose tissue and liver ATP citrate lyase activities were also significantly decreased by vitamin B6 deficiency. In the presence of insulin, the uptake of glucose and 3-O-methyl glucose, a non-metabolizable sugar, by fat pads from deficient rats was greater than uptake by fat pads from control rats. These observations suggest that the increased glucose utilization by adipose tissue and liver of vitamin B6-deficient rats is not directly related to changes in the enzymes studied, but in the case of adipose tissue, may be explained, at least in part, by enhanced glucose uptake.
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PMID:Effects of vitamin B6 deficiency on liver, kidney, and adipose tissue enzymes associated with carbohydrate and lipid metabolism, and on glucose uptake by rat epididymal adipose tissue. 13 63

Mutants have been isolated in S. cerevisiae with the phenotype of growth on pyruvate but not on glucose, or growth on rich medium with pyruvate but inhibition by glucose. Screening of mutagenized cultures was either without an enrichment step, or after enrichment using the antibiotic netropsin (Young et al. 1976) or inositol starvation (Henry, Donahue and Culbertson 1975). One class of mutants lacked pyruvate kinase (pyk), another class had all the enzymes of glycolysis, and one mutant lacked phosphoglucose isomerase (pgi, Maitra 1971). Partial reversion of pyruvate kinase mutants on rich medium containing glucose gave double mutants now also lacking hexokinase (hxk), phosphofructokinase (fk), or several enzymes of glycolysis (gcr). In diploids the mutations were recessive. pyk, pgi, pfk, and gcr segregated 2:2 from their wild-type alleles. PYK hxk, PYK pfk, and PYK gcr segregrants grew on glucose.
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PMID:Glycolysis mutants in Saccharomyces cerevisiae. 14 95

An ultramicrochemical technique has been adapted to the evolution of enzyme profiles within individual human mammary tumors. Tandem observation of adjacent stained and lyophilized sections permitted dissection of microgram quantities of freeze-dried material within confirmed regions of malignancy. Enzymes frequently monitored to examine glycolytic, respiratory, and metastatic capacity were microanalyzed successfully: lactic dehydrogenase (LDH), phosphoglucose isomerase (PGI), malate dehydrogenase (MDH), acid phosphatase (AP), aldolase (ALD), glucose-6-phosphate dehydrogenase (G6PDH), pyruvate kinase (PK), alpha-glycerophosphate dehydrogenase (alpha-GOPDH), hexokinase (HK), and phosphofructokinase (PRK). All enzyme activities were higher in infiltrating ductal carcinomas than in fibroadenomas. Extracts of tumor cells mixed in varying proportions with brain or muscle extracts of rat evidenced no modification of expected activity. The technical adaptation described provided a sensitive methodology to resolve problems of relication, profile analysis, sample quantity, and selectivity within heterogeneous tissues.
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PMID:Application of a microchemical technique to the elucidation of enzyme activity profiles within single human mammary tumors. 20 41

This paper starts a series on red blood cell (RBC) metabolism in patients with chronic renal failure (CRF). The glycolytic enzyme levels and in vitro half-lives of these patients' RBCs were determined. A number of enzymes (hexokinase, glucose-6-phosphate isomerase, fructose-6-phosphate kinase, aldolase, glyceraldehyde-3-phosphate dehydrogenase and lactate dehydrogenase) showed higher activities than in normal control RBCs. Other enzyme activities were normal. These results were discussed and several possible mechanisms considered. We favour the point of view of a shortened life span of the RBCs in CRF, making the most unstable enzymes of the glycolytic sequence appear increase as compared with normal controls.
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PMID:Metabolism of red blood cells in chronic renal failure. I. Glycolytic enzyme levels. 22 98

The denaturation of eight purified yeast enzymes, glucose-6-phosphate dehydrogenase, 6-phosphogluconate dehydrogenase, glyceraldehyde-3-phosphate dehydrogenase, 3-phosphoglycerate kinase, alcohol dehydrogenase, beta-fructosidase, hexokinase and glucose-6-phosphate isomerase, promoted under controlled conditions by the free fatty acids myristic and oleic, is selective. Glucose-6-phosphate dehydrogenase (D-glucose-6-phosphate:NADP+ 1 oxidoreductase, EC 1.1.1.49) is extremely sensitive to destabilization and was studied in greater detail. Results show that chain length and degree of unsaturation of fatty acids are important to their destabilizing effect, and that ligands of the enzyme can afford protection. The denaturation process results in more than one altered form. These results can be viewed in the perspective of the possibility that amphipathic substances, and in particular free fatty acids, may play a role for enzyme degradation in vivo, by initiating steps of selective denaturation.
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PMID:Selective denaturation of several yeast enzymes by free fatty acids. 35 87

A method is described for the measurement of enzyme activity under xeric conditions. The reaction mixtures had water contents ranging between 0.1 and 0.6g/g of reaction mixture. For glucose 6-phosphate dehydrogenase, hexokinase and fumarase, enzyme activity became detectable (about 0.05% of the fully hydrated rate) when the water content was about 0.2g/g of reaction mixture, and for phosphoglucose isomerase, around 0.15g/g of reaction mixture. With the water content raised to 0.3g/g of reaction mixture the reaction rates were only increased to 0.1-3% of the fully hydrated rate. When the combined rates for phosphoglucose isomerase and glucose 6-phosphate dehydrogenase were measured, reasonable agreement was found between the experimental data and those calculated from the individual experimentally determined rates on the assumption that diffusion was not further limiting. A method was devised for measuring the diffusion coefficients of low-molecular-weight substances in solutions having low water contents. The diffusion coefficients of riboflavin in sorbitol solution decreased by about 100-fold when the water content of the latter was reduced from 3 to 0.25g/g of sorbitol. It is concluded that to detect enzyme activity a certain minimal amount of water is required and that above this minimum the rate is still restricted by diffusion limitation. The relevance of the results to the physical state of water in reaction mixtures and to metabolism in seeds and spores in xeric conditions is discussed.
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PMID:The effect of restricted hydration on the rate of reaction of glucose 6-phosphate dehydrogenase, phosphoglucose isomerase, hexokinase and fumarase. 47 53

Various enzymes of glycolysis (hexokinase, phosphoglucoisomerase, aldolase and lactate dehydrogenase), the Krebs cycle (isocitrate, succinic and malate dehydrogenases), and the pentose phosphate cycle (glucose-6-phosphate and 6-phosphogluconate dehydrogenases) were studied in buffalo spermatozoa by biochemical and cytochemical methods. The enzymes of glycolysis were found to be loosely bound whereas those of the Krebs and pentose phosphate cycles were strongly bound to mitochondrial membranes. All the enzymes studied were localized histochemically in the mid-piece.
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PMID:Glycolytic, Krebs cycle and pentose phosphate cycle enzymes in spermatozoa of the buffalo (Bubalus bubalis). 51 3


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