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 adaptation to repeated periods of intermittent normobaric hypoxia (oxygen:nitrogen = 10:90, 12 hr daily for 5 days) of some specific enzymatic activities related to energy metabolism has been observed in different rat brain areas (cerebral cortex, hippocampus, corpus striatum, hypothalamus, cerebellum, and medulla oblongata). The evaluation of the maximum rate (Vmax) of the enzymes was carried out on: the homogenate "in toto," the nonsynaptic mitochondrial fraction, and the crude synaptosomal fraction. The adaptation to intermittent normobaric hypoxic exposure was characterized by significant modifications of some enzyme activities in the homogenate "in toto" (decrease of hexokinase activity in cerebellum), in the nonsynaptic mitochondrial fraction (increase of succinate dehydrogenase activity in corpus striatum and decrease of cytochrome oxidase activity in cerebral cortex), and, particularly, in the synaptosomal fraction (decrease of cytochrome oxidase activity in cerebral cortex, hippocampus, corpus striatum, and cerebellum, and decrease of malate dehydrogenase and lactate dehydrogenase activity in cerebellum). The adaptation to normobaric intermittent hypoxia differs according to the brain area, subcellular fraction, and enzyme activity tested.
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PMID:Brain enzyme adaptation to mild normobaric intermittent hypoxia. 376 87

To determine whether sensitivity of muscle characteristics and aerobic performances to endurance training was genotype-dependent, 6 pairs of monozygotic (MZ) twins, 21 +/- 4 yr of age (mean +/- SD), took part in a 15-wk ergocycle endurance training program. Tests were performed before and after 7 and 15 weeks of training. A biopsy of the vastus lateralis muscle was obtained for the determination of fiber type composition and activities of creatine kinase, hexokinase, phosphofructokinase, lactate dehydrogenase, malate dehydrogenase, 3-hydroxyacyl CoA dehydrogenase, and oxoglutarate dehydrogenase. Maximal oxygen uptake was measured with a progressive maximal ergocycle test, while endurance performance was determined as the total work output during a 90-min maximal ergocycle test. Results indicated that maximal oxygen uptake X kg-1 and endurance performance X kg-1 increased significantly (14 and 31%, respectively) with training, and intra-pair resemblance (intra-class) in response to 15 wk of training ranged from 0.65 to 0.83. Hexokinase (31%), phosphofructokinase (37%), lactate dehydrogenase (21%), malate dehydrogenase (31%), and 3-hydroxyacyl CoA dehydrogenase (60%) were significantly increased with training whereas no mean change in fiber-type proportions, oxoglutarate dehydrogenase and creatine kinase activities and the phosphofructokinase/oxoglutarate dehydrogenase ratio was observed. Similarity within twin pairs in the response to enzyme activities was mainly detected in the second half of the training program. The present results confirm, therefore, that both maximal oxygen uptake and endurance performance responses to training are largely genotype-dependent.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Heredity and muscle adaptation to endurance training. 378 81

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

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

Six men and three women with insulin-dependent diabetes (without complications) participated in physical training three times a week for 20 weeks. Physical training did not change the concentration of fasting blood-glucose, glucose excretion in urine or glucosylated haemoglobin (HbA1). However, the glucose disposal rate during euglycaemic clamp increased after training. In two patients a minor reduction of insulin dosage was necessary to alleviate slight hypoglycaemic episodes. The training resulted in significant increases in quadriceps isometric and dynamic strength and endurance. Maximal oxygen uptake increased by 8%, the activity of glycolytic enzymes in vastus lateralis muscle by 47% for hexokinase, and 30% for tri-osephosphate dehydrogenase and 25% for lactic dehydrogenase, the activity of oxidative enzymes by 42% for citrate synthase and 46% for 3-hydroxy-acyl-CoA-dehydrogenase. The glycogen concentration in the vastus lateralis muscle did not change significantly. Lipoprotein lipase activity did not change in muscle, nor in adipose tissue. The mean muscle fibre area increased by 25% and the area of FTa fibres by 30%. The new formation of capillaries around different muscle fibres was significant for FTb fibres (26%). The proliferation of capillaries, however, appeared to be insufficient to cope with the increased area of muscle fibres. As a result, the mean area of muscle fibre supplied by one capillary (a measure of diffusion distance) significantly increased after training for FTa fibres. It is concluded that with the exception of deficient proliferation of capillaries, patients with insulin-dependent diabetes mellitus show a normal central and peripheral adaptation to physical training. Physical training does not apparently improve blood glucose control in most cases, despite an increased insulin sensitivity.
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PMID:Muscle adaptations and glucose control after physical training in insulin-dependent diabetes mellitus. 394 85

5-Thioglucose (5-TG) had a marked effect on the energy metabolism of Schistosoma mansoni in vitro: the conversion of external glucose into lactate by intact worms was severely inhibited. This inhibition of glycolysis was instantaneous, independent of the oxygen concentration and competitive with respect to glucose. Degradation of 0.5 mM external (14C-labelled) glucose was inhibited for 80% in the presence of 20 mM 5-TG. On the other hand the degradation of endogeneous glycogen to lactate was uninhibited. This shows that the inhibition of glucose breakdown occurred at the entrance of glucose into the cell and/or at the hexokinase reaction. It was demonstrated that 5-TG inhibited both the uptake of glucose and the activity of hexokinase. However, it was concluded that in the intact worm 5-TG blocked glycolysis by its competitive inhibition of hexokinase. In intact S. mansoni worms hexokinase is probably the rate-limiting enzyme of glycolysis. Krebs-cycle activity and lactate production do not occur at a fixed ratio: at lower rates of pyruvate formation Krebs-cycle activity was favoured.
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PMID:The effect of 5-thioglucose on the energy metabolism of Schistosoma mansoni in vitro. 403 43

The metabolic properties of mitochondria from rat cerebral cortex and olfactory bulb were investigated. The pyruvate-supported oxygen uptake rates by olfactory bulb mitochondria were significantly lower than those by cerebrocortical mitochondria. This is consistent with the differences in pyruvate dehydrogenase complex activities between these mitochondrial preparations. Pyruvate dehydrogenase kinase, NAD-linked isocitrate dehydrogenase, and hexokinase activities in olfactory bulb mitochondria were significantly lower than those in cerebrocortical mitochondria. However, NADP-linked isocitrate dehydrogenase, and NAD-linked and NADP-linked glutamate dehydrogenase activities in olfactory bulb mitochondria were significantly higher than those in cerebrocortical mitochondria. The differences between these two mitochondrial preparations in terms of the activities of these energy-metabolizing enzymes reflect the differences detected in the homogenates of these regions.
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PMID:Differences in some of the metabolic properties of mitochondria isolated from cerebral cortex and olfactory bulb of the rat. 404 57

1. Superovulated rat ovary slices from rats treated with 20mug. of luteininzing hormone/100g. body wt. 2hr. before death and from control animals have been incubated in vitro. Output of Delta(4)-3-oxo steroids (0.2mumole/g. wet wt./hr. in control tissue) was linear for 4hr., and was increased by approx. 70% in slices from luteinizing hormone-treated rats. Rate of oxygen consumption (90.0+/-4.6mumoles/g. wet wt./hr.) was linear for 3hr. and unaltered by luteinizing hormone treatment or addition of glucose (1mg./ml.) to the medium. 2. In slices from control animals, steady-state rate of glucose uptake was 78.0+/-2.9mug. atoms of carbon/g. wet wt./hr.; steady-state rates of lactate output, pyruvate output and incorporation of [U-(14)C]-glucose carbon atoms into carbon dioxide and total lipid extract were 60.7+/-0.9, 2.4+/-0.1, 18.0+/-1.1 and 0.7+/-0.1mug. atom of carbon/g. wet wt./hr. and accounted for 104.5+/-1.9% of the glucose uptake. In slices from luteinizing hormone-treated rats, glucose uptake and outputs of lactate, pyruvate and [(14)C]carbon dioxide were increased by approx. 25%, and 108.4+/-3.2% of the glucose uptake could be accounted for. 3. The total lipid extract was separated by thin-layer chromatography and saponification. Of the (14)C incorporated into this fraction during incubation with [U-(14)C]glucose 97% was found in the fractions containing glyceride glycerol and less than 3% in the fractions containing sterols, steroids or fatty acids. Appreciable quantities of (14)C were incorporated into these lipid fractions from [1-(14)C]acetate. 4. From a consideration of the tissue glycogen content, the specific activities of [(14)C]lactate and glucose 6-phosphate (C-1) derived from [1-(14)C]-, [6-(14)C]- and [U-(14)C]-glucose, and the ratio of [(14)C]carbon dioxide yields from [1-(14)C]glucose and [6-(14)C]glucose, it was concluded that there was no appreciable glycogenolysis or flow through the pentose phosphate cycle. 5. In ovary slices from both control and luteinizing hormone-treated animals, glucose in vitro raised the incorporation rate of (14)C from [1-(14)C]acetate into sterols and steroids. Luteinizing hormone in vivo stimulated the incorporation rate in vitro but only in the presence of glucose. 6. In slices incubated in medium containing [(3)H]water, [(14)C]sorbitol and glucose (1mg./ml.), the total water space (865+/-7.1mul./g.) and the extracellular water space (581+/-22mul./g.) were unchanged by luteinizing hormone treatment in vivo but the glucose space was raised from 540+/-23.6mul./g. to 639+/-31.3mul./g. 7. Luteinizing hormone treatment was found to lower the tissue concentration of the hexose monophosphates and to increase the total activity of hexokinase, glucose 6-phosphate dehydrogenase and 6-phosphogluconate dehydrogenase and possibly of phosphofructokinase. 8. The kinetic properties of a partially purified preparation of phosphofructokinase were found to be qualitatively similar to those from other mammalian tissues. 9. The results are discussed with reference to both the role of glucose metabolism in steroidogenesis and the mechanism by which luteinizing hormone increases the rate of glucose uptake.
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PMID:Glucose metabolism in the superovulated rat ovary in vitro. Effects of luteinizing hormone and the role of glucose metabolism in steroidogenesis. 424 Jul 7

1. The growth of the lactoperoxidase-sensitive Streptococcus cremoris 972 in a synthetic medium was inhibited by lactoperoxidase and thiocyanate. The glycolysis and oxygen uptake of suspensions of Strep. cremoris 972 in glucose or lactose were also inhibited. The lactoperoxidase-resistant Strep. cremoris 803 was not inhibited under these conditions but was inhibited in the absence of a source of energy. 2. Lactoperoxidase (EC 1.11.1.7), thiocyanate and hydrogen peroxide completely inhibited the hexokinases of non-metabolizing suspensions of both strains. The inhibition was reversible, hexokinase and glycolytic activities of Strep. cremoris 972 being restored by washing the cells free from inhibitor. The aldolase and 6-phosphogluconate-dehydrogenase activities of Strep. cremoris 972 were partially inhibited but several other enzymes were unaffected. 3. The resistance of Strep. cremoris 803 to inhibition was not due to the lack of hydrogen peroxide formation, to the destruction of peroxide, to the inactivation of lactoperoxidase or to the operation of alternative pathways of carbohydrate metabolism. 4. A ;reversal factor', which was partially purified from extracts of Strep. cremoris 803, reversed the inhibition of glycolysis of Strep. cremoris 972. The ;reversal factor' also catalysed the oxidation of NADH(2) in the presence of an intermediate oxidation product of thiocyanate and was therefore termed the NADH(2)-oxidizing enzyme. 5. The NADH(2)-oxidizing enzyme was present in lactoperoxidase-resistant streptococci but was absent from lactoperoxidase-sensitive streptococci.
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PMID:The inhibition of streptococci by lactoperoxidase, thiocyanate and hydrogen peroxide. The effect of the inhibitory system on susceptible and resistant strains of group N streptococci. 429 Sep 83

1. The maximum activities of hexokinase, phosphorylase and phosphofructokinase have been measured in extracts from a variety of muscles and they have been used to estimate the maximum rates of operation of glycolysis in muscle. These estimated rates of glycolysis are compared with those calculated for the intact muscle from such information as oxygen uptake, glycogen degradation and lactate formation. Reasonable agreement between these determinations is observed, and this suggests that such enzyme activity measurements may provide a useful method for comparative investigations into quantitative aspects of maximum glycolytic flux in muscle. 2. The enzyme activities from insect flight muscle confirm and extend much of the earlier work and indicate the type of fuel that can support insect flight. The maximum activity of hexokinase in some insect flight muscles is about tenfold higher than that in vertebrate muscles. The activity of phosphorylase is greater, in general, in vertebrate muscle (particularly white muscle) than in insect flight muscle. This is probably related to the role of glycogen breakdown in vertebrate muscle (particularly white muscle) for the provision of ATP from anaerobic glycolysis and not from complete oxidation of the glucose residues. The activity of hexokinase was found to be higher in red than in white vertebrate muscle, thus confirming and extending earlier reports. 3. The maximum activity of the mitochondrial glycerophosphate dehydrogenase was always much lower than that of the cytoplasmic enzyme, indicating that the former enzyme is rate-limiting for the glycerol 3-phosphate cycle. From the maximum activity of the mitochondrial enzyme it can be calculated that the operation of this cycle would account for the reoxidation of all the glycolytically produced NADH in insect flight muscle but it could account for only a small amount in vertebrate muscle. Other mechanisms for this NADH reoxidation in vertebrate muscle are discussed briefly.
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PMID:The activities of phosphorylase, hexokinase, phosphofructokinase, lactate dehydrogenase and the glycerol 3-phosphate dehydrogenases in muscles from vertebrates and invertebrates. 434 85


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