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 influence of prolactin (Prl) and bromocriptine on the specific activities of neural and glial cellular enzymes involved in carbohydrate metabolism in cerebral cortex, hypothalamus, cerebellum and pons-medulla was studied. Both Prl and bromocriptine stimulated the activity of hexokinase (HK) in the neural as well as in the glial cells. While Prl increased the activity of phosphofructokinase (PFK), glyceraldehyde-3-phosphate dehydrogenase (G-3-PDH) and pyruvate kinase (PK) in the neural cells, it decreased the same in the glial cells. On the other hand, bromocriptine elevated the activity of all these enzymes in the neural cells without any effect on the glial cells. The activities of neural cellular glucose-6-phosphate dehydrogenase (G-6-PDH) and 6-phosphogluconate dehydrogenase (6-PGDH) were inhibited by Prl, whereas bromocriptine increased the same. The activities of these enzymes in the glial cells were enhanced by both Prl and bromocriptine. Thus, the present study suggests that Prl has a differential effect on the activities of enzymes involved in Embden-Meyerhoff pathway (EMP) and hexosemonophosphate shunt (HMP) in the neural and glial cells of immature male bonnet monkeys.
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PMID:Role of prolactin on neural and glial cellular enzymes involved in carbohydrate metabolism. I. Studies on immature male bonnet monkeys. 340 16

The enzymes of 35 adult Paragonimus uterobilateralis were analysed using thin-layer starch gel electrophoresis. From a total of 21 enzyme systems studied, 15 proved to be useful for the description and recognition of this species. All individuals were identical concerning 11 enzymes. In four remaining enzymes, alanine aminotransferase (ALAT, hexokinase, aspartate aminotransferase and phosphogluconate dehydrogenase, two or three variants, also being partly typical for this species were observed. In a comparison involving seven different enzymes, there were no differences between the electrophoretic patterns of 35 adult and 24 juvenile P. uterobilateralis. Additional examinations of 30 adult P. uterobilateralis with isoelectric focusing on ultrathin-layer polyacrylamide gels revealed clearer separations of enzymes. The method showed corresponding results or identiy of all individuals tested with three representative enzymes (ALAT, glucosephosphate isomerase and adenylate kinase).
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PMID:Isoenzymes of the lung fluke Paragonimus uterobilateralis from Liberia. 344 38

Glucose-6-phosphate dehydrogenase (EC 1.1.1.49) prepared from baker's yeast binds to immobilized Cibacron Blue F3G-A and Procion Red HE-3B. In this paper the two dyes are compared with respect to their use in the purification of this enzyme. Cibacron Blue chromatography was found useful at an early stage of purification for the removal of contaminating hexokinase, phosphoglucose isomerase and phosphoglucomutase. With Procion Red HE-3B Sepharose the NADP dependent enzymes phosphogluconate dehydrogenase and glutathione reductase are separable from glucose-6-phosphate dehydrogenase. Unlike Cibacron Blue gel chromatography, the enzyme can be specifically eluted from Procion Red HE-3B Sepharose by a NADP gradient. Other monochlorotriazine dyes like Xirone Brillant Red BHD, 4BHD, 6BHD and GHD and the dichlorotriazine dye Procion Brown MX-5BR immobilized to Sepharose have only little binding affinity to glucose-6-phosphate dehydrogenase. The binding behaviour of different immobilized triazine dyes for pre-purified and purified glucose-6-phosphate dehydrogenase is compared. In addition, the influence of the free dyes on the activity of glucose-6-phosphate dehydrogenase is studied. It is demonstrated that the results of kinetic and binding studies with the purified enzyme are not uncritically applicable for the selection of a dye as ligand for affinity chromatography during enzyme preparation.
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PMID:Interactions of immobilized and free triazine dyes with glucose-6-phosphate dehydrogenase from yeast. 351 9

Glucose utilization by different metabolic pathways in bovine adrenal medulla has been studied using freshly isolated adrenal chromaffin cells. The rate of net glucose utilization in resting cells was 10.5 mumoles X g-1 X h-1. 50% was transformed into lactate and pyruvate, the lactate to pyruvate ratio ranging from 3 to 7.27% was metabolized through the tricarboxylic acid cycle and 3.1% was oxidized in the pentose phosphate pathway. The ratio of 14CO2 production from [1-14C] glucose and [6-14C] glucose was close to 2 at one hour of incubation. 3.2% of total glucose consumed was used in protein synthesis, and 1% was incorporated into lipids. Oxygen utilization in respiration by isolated adrenal chromaffin cells was 18.2 mumoles X g-1 X h-1, corresponding to 3.1 mumoles glucose X g-1 X h-1 or about 30% of total glucose consumed. The activities of hexokinase, enolase, pyruvate kinase, lactate dehydrogenase, glucose 6-phosphate dehydrogenase and 6-phosphogluconate dehydrogenase were assayed in extracts of bovine adrenal medulla, being 1.0, 23, 40, 37, 6.0 and 3.0 U/g respectively. Hexokinase activity was identified as belonging mainly to isoenzyme I, with some isoenzyme II. Enolase was predominantly the alpha gamma hybrid. Pyruvate kinase activity corresponded to a mixture of isoenzymes K and M. Lactate dehydrogenase activity corresponded to isoenzymes 1, 2 and 3, with smaller proportions of isoenzymes 4 and 5. Results are discussed mainly with respect to those reported for the brain.
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PMID:Enzymes and pathways of glucose utilization in bovine adrenal medulla. 371 7

Agarose gel electrophoresis was used to identify metabolic enzymes in Babesia bovis and B. bigemina. Glutamate dehydrogenase, lactate dehydrogenase, glucose phosphate isomerase, and hexokinase were identified in B. bovis- and B. bigemina-infected erythrocytes and B. bovis merozoite preparations. A specific electrophoretic mobility was observed for each enzyme. Malate dehydrogenase, glucose 6-phosphate dehydrogenase, 6-phosphogluconate dehydrogenase, and adenylate kinase were only detected in normal erythrocyte preparations. Inter-species, but not intra-species, variation was noted when comparing electrophoretograms of both species. Kinin-activating activity was not detected in B. bovis-infected erythrocyte or merozoite preparations at pH 4.2 or 7.6.
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PMID:Enzymatic characterization of Babesia bovis. 379 41

Enzymes of the Embden-Meyerhof-Parnas pathway and hexose monophosphate shunt were examined in cytoplasmic extracts of three serovars of Ureaplasma urealyticum. We found no glucose-6-phosphate or 6-phosphogluconate dehydrogenase, hexokinase, phosphoglucose isomerase, aldolase, or lactic dehydrogenase activities. We failed to find cytochrome pigments in extracts and found no significant production of 14CO2 from [U-14C]glucose, nor did we find oxygen-dependent reduced nicotinamide adenine dinucleotide oxidase activity. Lactic acid was found only at trace levels in spent culture fluids. Ureaplasmas are apparently nonfermentative and are unlike all other mollicutes in that they have no detectable oxygen-dependent reduced nicotinamide adenine dinucleotide oxidase activity.
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PMID:Metabolic distinctiveness of ureaplasmas. 379 29

Maximum activities of some key enzymes of metabolism were studied in elicited (inflammatory) macrophages of the mouse and lymph-node lymphocytes of the rat. The activity of hexokinase in the macrophage is very high, as high as that in any other major tissue of the body, and higher than that of phosphorylase or 6-phosphofructokinase, suggesting that glucose is a more important fuel than glycogen and that the pentose phosphate pathway is also important in these cells. The latter suggestion is supported by the high activities of both glucose-6-phosphate dehydrogenase and 6-phosphogluconate dehydrogenase. However, the rate of glucose utilization by 'resting' macrophages incubated in vitro is less than the 10% of the activity of 6-phosphofructokinase: this suggests that the rate of glycolysis is increased dramatically during phagocytosis or increased secretory activity. The macrophages possess higher activities of citrate synthase and oxoglutarate dehydrogenase than do lymphocytes, suggesting that the tricarboxylic acid cycle may be important in energy generation in these cells. The activity of 3-oxoacid CoA-transferase is higher in the macrophage, but that of 3-hydroxybutyrate dehydrogenase is very much lower than those in the lymphocytes. The activity of carnitine palmitoyltransferase is higher in macrophages, suggesting that fatty acids as well as acetoacetate could provide acetyl-CoA as substrate for the tricarboxylic acid cycle. No detectable rate of acetoacetate or 3-hydroxybutyrate utilization was observed during incubation of resting macrophages, but that of oleate was 1.0 nmol/h per mg of protein or about 2.2% of the activity of palmitoyltransferase. The activity of glutaminase is about 4-fold higher in macrophages than in lymphocytes, which suggests that the rate of glutamine utilization could be very high. The rate of utilization of glutamine by resting incubated macrophages was similar to that reported for rat lymphocytes, but was considerably lower than the activity of glutaminase.
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PMID:Metabolism of glucose, glutamine, long-chain fatty acids and ketone bodies by murine macrophages. 380 Sep 71

Activities of the red cell enzymes hexokinase, glucose 6-phosphate dehydrogenase, 6-phosphogluconate dehydrogenase, lactic dehydrogenase and aspartate aminotransferase were measured in 17 chronic haemodialysis patients receiving androgen therapy, 15 untreated chronic haemodialysis patients and 15 normal subjects. Compared to normal subjects, untreated haemodialysis patients had similar reticulocyte counts but significantly increased levels of all five enzymes studied. This finding suggests the presence of a younger red cell population in the peripheral blood and is consistent with the shortened red cell survival known to occur in this clinical setting. Red cell enzyme activities in untreated haemodialysis patients were significantly correlated with one another and with the serum phosphate level. Moreover, in this population, red cell DPG content was directly related to hexokinase and glucose 6-phosphate dehydrogenase activities while haemoglobin-oxygen affinity (P50) was inversely related to all five enzyme activities. In contrast, in androgen-treated haemodialysis patients, despite higher reticulocyte counts, red cell enzyme activities were the same or lower than those in the untreated haemodialysis group and only slightly higher than those in normal subjects, suggesting an overall older red cell population. Moreover, relationships of red cell enzymes to one another, to serum phosphate levels and to both red cell DPG content and haemoglobin-oxygen affinity were significantly different in androgen-treated subjects than in the untreated haemodialysis group. These changes are consistent with a direct effect of androgens on red cell metabolism and an improved red cell survival during androgen therapy.
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PMID:Androgen therapy in haemodialysis patients. II. Effects on red cell metabolism. 382 30

The natural product of the glucose-6-phosphate dehydrogenase reaction is 6-phosphoglucono-delta-lactone, which must be hydrolyzed to 6-phosphogluconic acid before it can be further metabolized by 6-phosphogluconate dehydrogenase. Because this lactone is very unstable, it has been uncertain whether the enzyme that hydrolyzes it, 6-phosphogluconolactonase, is required for functioning of the hexose monophosphate pathway. We have purified glucose-6-phosphate dehydrogenase, 6-phosphogluconolactonase, and 6-phosphogluconate dehydrogenase from human erythrocytes to the point where each enzyme is essentially free of each of the other activities. We constructed an artificial hexose monophosphate pathway from these enzymes, providing as substrate 14C-labeled glucose-6-phosphate either directly or by continual generation from 14C-glucose by yeast hexokinase and adenosine triphosphate. The oxidation of 6-phosphogluconic acid was estimated by measuring the CO2 formed. In the absence of a reduced nicotinamide-adenine dinucleotide phosphate (NADPH)-oxidizing system, such as oxidized glutathione (GSSG)-glutathione reductase or phenazine methosulfate, little CO2 was formed, and the presence of 6-phosphogluconolactonase did not affect the amount that was produced. When the hexose monophosphate pathway was stimulated by providing an NADPH-oxidizing system, CO2 was produced two and a half to five times as fast in the presence of 6-phosphogluconolactonase as in its absence. These studies suggest that 6-phosphogluconolactonase is required for the functioning of the hexose monophosphate pathway when the rate of oxidation of NADPH is accelerated.
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PMID:Limiting role of 6-phosphogluconolactonase in erythrocyte hexose monophosphate pathway metabolism. 393 73

The effects of exogenously administered 3',5'-monophosphate (cyclic AMP) on glycogen synthesis and hexose monophosphate shunt enzymes were studied in the uteri of immature and ovariectomized rats to determine whether cyclic AMP mimics the known effects of estrogenic hormones. The injection of cyclic AMP concurrently with theophylline, significantly increased the activity of uterine hexokinase, phosphofructokinase, pyruvate kinase, glucose 6-phosphate dehydrogenase, 6-phosphogluconate dehydrogenase, and uterine glycogen content in immature rats (p less than .05). These increases were related to the dose of cyclic AMP, and as little as .2 mg was able to stimulate uterine glycogen to 169% of control values. The treatment did not significantly increase the activity of the key glycolytic or hexose monophosphate shunt enzymes in the lung and thymus, although these tissues are also not receptive to estrogen. Neither estradiol-17beta or cyclic AMP and theophylline produced any measurable effect on the uterine enzymes, isocitrate dehydrogenase, or alpha-glycerophosphate dehydrogenase. In ovariectomized and adrenalectomized-ovariectomized animals, cyclic AMP and theophylline significantly stimulated the activity of key glycolytic and hexose monophosphate shunt enzymes (p less than .05); the N6, 02-dibutyryl analog of cyclic AMP being more potent than the parent compound. Pretreatment with actinomycin or cycloheximide significantly inhibited the effects of cyclic AMP and theophylline (p less than .05), which indicates that neither cyclic AMP stimulation or the inhibition of the effects of cyclic AMP were dependent on adrenal function. The results support the possiblity that cyclic AMP may be involved in mediating the metabolic effects of estrogen on the uterus.
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PMID:Metabolic control mechanisms in mammalian systems. XV. Studies on the role of adenosine 3' ,5'-monophosphate in estrogen action on the uterus. 411 Aug 9


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