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)

Alkylation at the N-1 position of the adenine moiety of NAD+, ADP or ATP with 2,3-epoxypropyl acrylate, followed by polymerization with or without acrylamide at pH 8, gave water-soluble polymers of NAD+ and ADP where the alkyl chain was located at the exocyclic adenine C-6 amino group. Cofactor incorporations were good to high: 145-447 mumol NAD+/g polymer and 667 mumol ADP/g polymer. About 30% of the bound NAD+ could be reduced with rabbit muscle lactae dehydrogenase, yeast alcohol dehydrogenase and Bacillus subtilis alanine dehydrogenase; 84% of the bound ADP was phosphorylated with rabbit muscle creatine kinase. High cofactor activities were obtained with polymerized NAD+ with alcohol dehydrogenase as enzyme: the initial rate of NAD+ polymer reduction was 35-81% that of free NAD+. These values remained substantially high with agarose-immobilized alcohol dehydrogenase (15-36%) and should eventually allow their use in continuous enzymatic reactors. Enzymatic phosphorylation of ADP polymer by creatine kinase gave an ATP polymer with high biological activity: 480 mumol ATP/g polymer were transformed with yeast hexokinase.
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PMID:A two-step synthesis of new water-soluble polymers of NAD+ and ADP. The biological properties of these polymers. 625 Aug 24

Changes in extractability and activity of hexokinase (HK) were studied under the action of heating and of urea on skeletal muscles of Rana temporaria L., and besides the stability of this enzyme in muscle extract to those agents in vitro was examined. Under a 15 minutes heating of muscle, a decrease in extractability (the activity calculated for 1 g of tissue) and activity (the activity calculated for 1 mg of protein) of hexokinase is first revealed at 37 degrees C. Then the enzyme extractability decreases gradually in accordance to the decrease in extractability of the total water-soluble protein; the level of hexokinase activity attained at 37 degrees does not change up to 40 degrees. At 42 degrees the activity of the enzyme is completely inhibited. Under the heating of the muscle extract, the decrease of enzyme activity takes place at 36 degrees, the level achieved being stable up to 42 degrees C. Under the action of urea on the muscle at the reversible phase of alteration (1 M urea from 5 minutes to 2 hours at room temperature, 1 M urea for 9 hours at + 4 degrees C), hexokinase activity increases, calculated for 1 g of tissue and for 1 mg of protein. Under the irreversible disappearance of muscle excitability (1 M urea during 9 hours, 2 M urea during 2 hours at room temperature) no hexokinase activity was revealed. The activation of the enzyme is discussed in connection with the data on the increase of ATP content in muscle under the urea alteration. The treatment of the enzyme in muscle extract with 1 M urea decreases its activity in 30 minutes down to 67%; the level achieved does not change during 20 hours.
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PMID:[Changes in hexokinase activity during muscle alteration]. 651 16

The radiobiological consequences of chronic exposure to 3H at a dose level of 37 kBq/ml or 1 muCi/ml is reported. An inbred strain of Swiss albino mice was exposed up to 5 generations. Metabolic disorders were recorded by monitoring quantitative and qualitative changes in hexokinase and its isozymes from brain, liver and spleen from both sexes. The delivered dose ranged from approximately 41 mGy to 98 mGy. Nonetheless, the changes in enzyme activities as well as electrophoretic mobilities were significant. Deviations from normal levels were recorded in both sexes. The evidence indicates that direct effects of beta-irradiation can cause conformational changes in enzyme molecules. However, damage to DNA and membranes as being causal factors for variations in the enzyme levels cannot be ruled out. These disorders culminated in a gradual reduction in litter size. The implications of exposure to this dose of tritiated water is discussed in the light of NCRP recommendations and relevant literature.
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PMID:Effects of tritiated water ingestion on mice: III. Hexokinase isozymes in brain, liver and spleen up to five generations. 661 23

Recently, it has been reported that paromomycin sulfate has marked anthelmintic efficacy against tapeworm infections in man. In the present study this drug was used in the treatment of 14 cases of diphyllobothriasis latum and 1 case of taeniasis saginata. Also, the actions of paromomycin sulfate on Diphyllobothrium ditremum and D. erinacei were examined pharmacologically using Magnus apparatus and biochemical methods. The results obtained were as follows. For the treatment, a total of 50 mg/kg of paromomycin sulfate divided into 2 doses was given orally at intervals of 30 minutes. Two hours after medication, 20 g of magnesium sulfate dissolved in 200--300 ml of water was given as purgative. One or 2 worms were found in the stools of 11 cases with D. latum and 1 case with T. saginata within 24 hours after medication, but scolex was found in only 2 of them. All cases were negative for the eggs or segments in stool examinations at 1 and 3 months after treatment. Except 1 case complained mild and transient vomiting no side effects were noticed. All cases showed no abnormality in blood examination, liver function test and urinalysis. Both of the proglottids of D. ditremum and D. erinacei showed muscle relaxation in Tyrode solution containing 10(-4) g/ml of paromomycin sulfate. In D. ditremum the recovery of muscle tonus was observed within 10--15 minutes after affection of this drug, while the persistence of muscle relaxation was seen in D. erinacei. The activity of phosphoglucose isomerase was slightly inhibited by 10(-3) M paromomycin sulfate while those of hexokinase, phosphofructokinase and glucose-6-phosphate dehydrogenase were not inhibited. In phosphoenolpyruvate-succinate pathway, the activity of fumarate reductase was slightly inhibited 10(-3) M paromomycin sulfate while those of phosphoenolpyruvate carboxykinase and malate dehydrogenase were not inhibited.
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PMID:[Efficacy of paromomycin sulfate against human cestodiasis and its pharmacological action on tapeworm in vitro]. 687 66

1. The following were measured in adipose-tissue pieces, obtained from 7-9 month-old sheep, before or after the tissue pieces had been maintained in tissue culture for 24 h: the rates of synthesis from glucose of fatty acids, acylglycerol glycerol, pyruvate and lactate; the rate of glucose oxidation to CO(2); the rate of glucose oxidation via the pentose phosphate pathway; the activities of hexokinase, glucose 6-phosphate dehydrogenase, phosphofructokinase, pyruvate kinase, pyruvate dehydrogenase and ATP citrate lyase; the intra- and extra-cellular water content; the concentration of various metabolites and ATP, ADP and AMP. 2. The proportion of glucose carbon converted into the various products in sheep adipose tissue differs markedly from that observed in rat adipose tissue. 3. There was a general increase in the rate of glucose utilization by the adipose-tissue pieces after maintenance in tissue culture; largest changes were seen in the rates of glycolysis and fatty acid synthesis from glucose. These increases are paralleled by an increase in pyruvate kinase activity. There was no change in the activities of the other enzymes as measured, although the net flux through all the enzymes increased. 4. Incubation of fresh adipose-tissue pieces for 2-6h led to an increase in the affinity of pyruvate kinase for phosphoenolpyruvate. 5. The rate of pyruvate production by glycolysis was greater than the activity of pyruvate dehydrogenase of the tissue. 6. The results suggest that both pyruvate kinase and pyruvate dehydrogenase have important roles in restricting the utilization of glucose carbon for fatty acid synthesis in sheep adipose tissue.
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PMID:Regulation of glycolysis and fatty acid synthesis from glucose in sheep adipose tissue. 715 Feb 63

This study determined how selected functional, metabolic, and contractile properties were impacted by sodium pivalate, a compound which creates a secondary carnitine deficiency. Young male rats received either sodium pivalate (20 mM, PIV) or sodium bicarbonate (20 mM, CONTR) in their drinking water. After 11-12 weeks cardiac function and glucose oxidation rates were measured in isolated, perfused working heart preparations. Hearts were also analyzed for carnitine content, activities of hexokinase (HK), citrate synthase (CS), and B-hydroxyacyl CoA dehydrogenase (HOAD), and myosin isoenzyme distribution. Sodium pivalate treatment significantly reduced cardiac carnitine content and increased glucose oxidation but did not alter cardiac functional capacity. HK activity was increased in the PIV group (p < 0.05), and HOAD activity decreased (p < 0.05). CS activity and myosin isoform distribution (VI > 85%) remained unchanged. These results demonstrate that pivalate treatment of this duration and the accompanying carnitine deficiency shift cardiac substrate utilization without compromising cardiac functional capacity.
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PMID:Sodium pivalate reduces cardiac carnitine content and increases glucose oxidation without affecting cardiac functional capacity. 747 77

Hexokinase I (ATP:D-hexose 6-phosphotransferase, EC 2.7.1.1) is the first enzyme required in the metabolism of glucose in the central nervous system and plays a major role in regulation of the cerebral glycolytic rate. The distribution of hexokinase I mRNA was examined throughout the central nervous system of the rat by use of oligonucleotide probes and in situ hybridization histochemistry. In the rhinencephalon, strong hexokinase I mRNA labeling was demonstrated in the glomerular, mitral, internal granular, and internal plexiform layers, whereas the olfactory nerve, external plexiform, and subependymal layers and ependyma were devoid of labeling. Within the telencephalon, strong labeling was present in all layers (with the exception of the molecular layer) of the cerebral cortex, in the septum, in CA1-4 and dentate gyrus of the hippocampus, and in several amygdaloid nuclei. There was only weak labeling in the nucleus accumbens and caudate putamen. In the diencephalon, there was in general a strong labeling in the epithalamus, in several thalamic nuclei, including the anteriodorsal, anterioventral, anteriomedial, reticular, paravetricular, intermediodorsal, anteriomedial, interanteriomedial, rhomboid, reuniens, and parafascicular thalamic nuclei. Several hypothalamic regions, including the subfornical organ, the medial preoptic area, the suprachiasmatic, supraoptic, paraventricular, dorsomedial, ventromedial nuclei, and the zona incerta, were strongly labeled. In the mesencephalon, there was particularly strong labeling in the pars compacta and reticulata of the substantia nigra, central gray, and red nucleus, in the Darkschewitsch nucleus, and in the medial accessory oculomotor nucleus. In the rhombencephalon, there was strong hybridization in all raphe nuclei, pontine, tegmental, lateral parabrachial, olivary nuclei, and several cranial motor nuclei. All neurons of the locus ceruleus were heavily labeled. Very strong labeling was present in Purkinje and granular cells of the cerebellar cortex. Neurons of the medulla oblongata area postrema, nucleus tractus solitarius, reticular nucleus, nucleus cuneatus and several motor nuclei were strongly labeled. In the spinal cord, labeled cells were present in all laminae, and also neurons of the dorsal root ganglion were heavily labeled. Hexokinase I mRNA was also demonstrated in the epithelium lining the the choroid plexus. In the E15 fetus, very strong labeling was seen in the liver, heart, and trigeminal ganglion, with less intense labeling in in the brain and other tissues having more moderate labeling. Administration of 2% saline as drinking water resulted in a marked increase in hexokinase I mRNA in the magnocellular neurons of the supraoptics and paraventricular nuclei. In summary, the results show extensive neuronal distribution of hexokinase I mRNA with regional differences in the expression pattern.
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PMID:Hexokinase I messenger RNA in the rat central nervous system. 770 41

Glucuronoxylomannan (AC) from the fruiting bodies of Tremella fuciformis exhibited a significant dose-dependent hypoglycemic activity in normal mice and also showed a significant activity in streptozotocin-induced diabetic mice, by intraperitoneal (i.p.) administration. The activities of AC-derivatives such as a product of AC which side chains had been removed were lower than that of native AC. AC raised the plasma insulin level in normal mice. Administration of AC to normal mice significantly increased the activities of hepatic hexokinase and glucose-6-phosphatase dehydrogenase, but it decreased that of hepatic glucose-6-phosphatase. Furthermore, AC reduced the glycogen content in the liver, increased the total lipid in epididymal adipose tissue, and lowered the plasma cholesterol level. The foregoing results indicated that the hypoglycemic activity of AC in normal mice was at least responsible for the increase of insulin secretion and for the acceleration of glucose metabolism. Single oral administration at a dose of 50-300 mg/kg of AC did not affect the plasma glucose level in normal mice, but continuous oral administrations of the AC solution (0.75 g/l) instead of water for a long time was found to be effective on the plasma glucose level in both experiments of the mice injected once i.p. with streptozotocin (170 mg/kg) at 0 d of AC administration and streptozotocin-induced diabetic mice.
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PMID:[Polysaccharides in fungi. XXXIII. Hypoglycemic activity of an acidic polysaccharide (AC) from Tremella fuciformis]. 801 40

Aqueous two-phase partition and temperature-induced phase separation using a non-ionic, random copolymer composed of 20% ethylene oxide, 80% propylene oxide (EO20 PO80) has been used for purification of glucose-6-phosphate dehydrogenase, hexokinase and 3-phosphoglycerate kinase from bakers' yeast. This EO20PO80 copolymer has a cloud point of 18 degrees C, at which temperature it phase separates from water. Enzymes were first partitioned at 4 degrees C in an initial EO20PO80-dextran T500 aqueous two-phase system. This system had an upper copolymer-rich phase and a lower dextran-rich phase. After phase separation had occurred the upper EO20PO80-rich phase was removed and placed at 24 degrees C. This resulted in formation of a new two-phase system with an upper water phase and a lower phase containing 98% copolymer and 2% water. Enzymes were recovered exclusively in upper water phase leaving a polymer-rich lower phase free of contamination. The phase diagram for the system EO20PO80 and dextran T500 at 4 degrees C has been determined.
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PMID:Application of temperature-induced phase partitioning at ambient temperature for enzyme purification. 812 71

Twelve isomers formed by the reaction of monoamminechromium(III) with ATP have been synthesized. Isomerism in this system results from chirality around the beta-phosphorus of the ATP, the position of the ammonia ligand, the relative orientation of the ammonia and the AMP, and the presence of ring-puckering conformers. By using chromatography on cross-linked cycloheptaamylose, reverse-phase C-18 HPLC, and cation-exchange FPLC, these isomers have been separated and purified. Their structures have been identified by (1) cleavage by periodate, followed by elimination in the presence of diethylenetriamine and subsequent phosphate insertion to give lambda, delta, or meso facial monoamminechromium tripolyphosphate with molar ellipticities of +240, -240, or 0 deg cm2 dmol-1 at 550 nm, respectively, (2) cleavage by nucleotide pyrophosphatase to give meridional or facial monoamminechromium pyrophosphate, (3) spectral data, and (4) rates of interconversion of isomers. All possible isomers are seen except those with ammonia syn to AMP. Since the substitution of ammonia for water in the inner coordination sphere appears to diminish affinity for enzymes when the ammonia is in contact with the protein but not when it faces the solvent, these isomers are useful for mapping of enzyme active sites. Their use as probes of enzyme structure is illustrated by their behavior with yeast hexokinase.
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PMID:Characterization of isomers of monoamminechromium-ATP and their use in mapping enzyme active sites. 821 84


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