Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: 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)

We evaluated whether any monosaccharides inhibit glycolysis in erythrocytes and discovered that D-mannose does. In the presence of D-mannose, glucose can be accurately measured by either the hexokinase procedure or the glucose oxidase procedure. In comparison studies with other glucose preservatives, we found that after 2 h at room temperature glucose decreased by 21 (SD 13) mg/L in D-mannose-treated blood, 93 (SD 10) mg/L in sodium fluoride-treated blood, 28 (SD 21) mg/L in ice-cooled blood, and 144 (SD 28) mg/L in control blood (no preservative treatment). Because D-mannose acted in the early phase of glycolysis, it was a more effective preservative than sodium fluoride; moreover, its use did not preclude measurement of sodium and potassium in the blood samples. D-Mannose did not interfere with other routine chemical tests except for the assay of creatine kinase involving coupled enzymes hexokinase/glucose-6-phosphate dehydrogenase. Creatine kinase could be correctly assayed in the presence of D-mannose by using glucokinase instead of hexokinase. D-Mannose can be used with or without anticoagulant and is compatible with most types of multi-channel automated analyzers.
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PMID:D-mannose as a preservative of glucose in blood samples. 200 64

The creatine phosphate shuttle energy transfer mechanism was postulated on the basis of the hexokinase acceptor theory of insulin action. It proposes that the movement of chemical energy from the mitochondrion to the myofibril is in the form of creatine phosphate. This occurs because there are isozymes of creatine phosphokinase bound to the inner membrane of the sarcosome and to the A band of the myofibril. These isozymes have been shown to act as transducers of energy from ATP to creatine phosphate at the translocase site and from creatine phosphate back to ATP at the myofibrillar compartment. Calculations show that there is no significant amount of transformation of creatine phosphate to ATP in the intervening space between the mitochondrion and the myofibril so that, essentially, transport between the oxidative sites and the contractile apparatus is through the creatine phosphate shuttle. There is also evidence that another terminus for this shuttle is the microsome so that muscle activity tends to increase energy supply for protein synthesis.
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PMID:The creatine phosphate energy shuttle--the molecular asymmetry of a "pool". 357 9

The enzyme level profiles of some regulatory enzymes and the isozyme patterns of some marker enzymes in bovine adult specialized, adult ordinary and fetal ordinary heart muscles were examined in order to biochemically characterize specialized heart muscle. The activities of hexokinase, phosphofructokinase and glucose-6-phosphate dehydrogenase in adult specialized heart muscle were significantly higher than those in adult ordinary heart muscle, but were similar to those in fetal ordinary heart muscle. The carnitine content and carnitine acetyltransferase activity in adult specialized heart muscle were lower than those in adult ordinary heart muscle. The isozyme patterns of creatine kinase, fructose-bisphosphate aldolase and pyruvate kinase in adult specialized heart muscle resembled those in fetal ordinary heart muscle. These results indicate that adult specialized heart muscle has the biochemical characteristics of fetal ordinary heart muscle.
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PMID:Biochemical characterization of the conduction system of the bovine heart. 359 6

Individual muscle fibers from patients with Duchenne muscular dystrophy at an early stage in their disease, and from apparently normal boys of similar age, were analyzed for 13 enzymes of energy metabolism. This approach avoided the serious problems with muscle homogenate assays from increases in nonparenchymal components and permitted assessment of disease changes in different fiber types. Some enzymes of glycogenolysis (phosphorylase, phosphoglucomutase, and pyruvate kinase) were decreased in dystrophic fibers of all types. Phosphofructokinase was decreased in presumptive type II fibers. Lactate dehydrogenase was increased in type I fibers and essentially unchanged in type II. Phosphoglucoisomerase was near normal. Two enzymes of glucose metabolism not involved in glycogenolysis, hexokinase and glycogen synthase, were near normal, but a third, fructose bisphosphatase, was sharply reduced. Two enzymes of oxidative metabolism, citrate synthase, and beta-hydroxyacyl CoA dehydrogenase, were unchanged or increased. Two enzymes of high energy phosphate transfer, creatine kinase and adenylokinase, were only marginally affected. The net result is to leave the type II fibers, which normally exert the greatest force, with a severe deficit in the glycogenolytic enzyme machinery to maintain that force.
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PMID:Effect of Duchenne muscular dystrophy on enzymes of energy metabolism in individual muscle fibers. 360 Feb 88

The purpose of this study was to investigate the effects of repeated high-intensity intermittent training programs interspaced by detraining on human skeletal muscle and performances. First, nineteen subjects were submitted to a 15-week cycle ergometer training program which involved both continuous and high-intensity interval work patterns. Among these 19 subjects, six participated in a second 15-week training program after 7 weeks of detraining. Subjects were tested before and after each training program for maximal aerobic power and maximal short-term ergocycle performances of 10 and 90s. Muscle biopsy from the vastus lateralis before and after both training programs served for the determination of creatine kinase (CK), hexokinase, phosphofructokinase (PFK), lactate dehydrogenase (LDH), malate dehydrogenase, 3-hydroxyacyl-CoA dehydrogenase (HADH) and oxoglutarate dehydrogenase (OGDH) activities. The first training program induced significant increases in all performances and enzyme activities but not in CK. Seven weeks of detraining provoked significant decreases in maximal aerobic power and maximal 90s ergocycle performance. While the interruption of training had no effect on glycolytic enzyme markers (PFK and LDH), oxidative enzyme activities (HADH and OGDH) declined. These results suggest that a fairly long interruption in training has negligeable effects on glycolytic enzymes while a persistent training stimulus is required to maintain high oxidative enzyme levels in human skeletal muscle. The degree of adaptation observed after the second training program confirms that the magnitude of the adaptive response to exercise-training is limited.
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PMID:Effects of two high-intensity intermittent training programs interspaced by detraining on human skeletal muscle and performance. 365 91

Study on the mechanism of hexokinase isozyme II adsorption on mitochondrial membranes in the presence of 10 mM MgCl2 demonstrated that 0.16% of the total proteins of the soluble fraction and the total hexokinase pool are capable of reversible binding to the membrane. The plot for the dependence of the degree of enzyme adsorption on Mg2+ concentration is hyperbolic. Under these conditions, hexokinase competes favourably for the binding sites with lactate dehydrogenase and creatine kinase. Analysis of the adsorption capacity of natural and artificial phospholipid membranes showed that hexokinase isozyme II is adsorbed in much the same way on inner and outer mitochondrial membranes as well as on a mixture of membranes obtained from various sources and on lecithin liposomes. The adsorption properties of hexokinase isozyme II and of its functional analog--isozyme I--point to marked differences in the mechanism of their interaction with the membrane. In contrast with isozyme I, isozyme II of hexokinase undergoes kinetic alterations. Besides, it was found that mild autolysis of isozyme II is accompanied by a loss of the enzyme ability to bind to mitochondrial membranes. The data obtained suggest that the specificity of hexokinase isozyme II adsorption depends on the structural peculiarities of the protein but not on those of the mitochondrial membrane.
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PMID:[Specificity of interaction of hexokinase isozyme II with mitochondrial membranes]. 369 16

The role of heredity in the response of maximal anaerobic capacities and skeletal muscle histochemical and biochemical characteristics to a 15-week cycle ergometer training program involving both continuous and interval work patterns was investigated in 14 pairs of monozygotic twins. The training program consisted mainly of series of ergocycle supramaximal exercises lasting from 15 s to 90 s and performed 4 and 5 times a week. The subjects were submitted to 10 s and 90 s all-out ergocycle tests to estimate maximal anaerobic alactacid (AAC) and lactacid (ALC) capacities, respectively. Muscle fiber types and creatine kinase (CK), hexokinase (HK), phosphofructokinase (PFK), lactate dehydrogenase (LDH), malate dehydrogenase (MDH), 3-hydroxyacyl CoA dehydrogenase (HADH), and oxoglutarate dehydrogenase (OGDH) activities were determined in a biopsy from the vastus lateralis. Training increased AAC, ALC, fiber type I proportion, MDH, HADH, and OGDH (P less than 0.05) and decreased fiber type IIb proportion and the PFK/OGDH ratio. No significant change was observed for CK, HK, PFK, and LDH. Large interindividual differences in the response to training were observed for all variables. However, intraclass correlations indicated that the extent of the response of ALC and CK, HK, LDH, MDH, and OGDH activities and of the PFK/OGDH activity ratio to training were significantly similar within pairs of twins. Although the role of heredity appeared absent for the changes in fiber type proportions and in anaerobic alactacid capacity, the present results suggest that the response of anaerobic lactacid capacity and most enzyme activities to high-intensity intermittent training is significantly determined by the genotype.
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PMID:Inheritance of human skeletal muscle and anaerobic capacity adaptation to high-intensity intermittent training. 373 13

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

To investigate whether or not the mitochondrial intermembrane space together with the extramitochondrial space form a homogeneous pool for adenine nucleotides, rat-heart mitochondria were studied in reconstituted systems with pyruvate kinase and ADP-producing enzymes with varied localization. In the hexokinase system, ADP is produced extramitochondrially by added yeast hexokinase, whereas in the creatine kinase system mitochondrial creatine kinase is responsible for ADP regeneration in the intermembrane space. The dependence of mitochondrial respiration on the extramitochondrial [ATP]/[ADP] ratio in both systems was investigated experimentally and by means of computer simulation. Near the resting state, higher [ATP]/[ADP] ratios were found in the creatine kinase system than in the hexokinase system at the same rate of respiration. This and the maintaining of a substantial creatine kinase-stimulated respiration in the presence of pyruvate kinase in excess is explained by a two-compartment model considering diffusion limitations of adenine nucleotides. A diffusion rate constant of (8.7 +/- 4.7) 10(4) microliters X mg-1 X min-1 for ADP and ATP was estimated, resulting in rate-dependent concentration differences up to 13.7 microM AdN between the extramitochondrial space and the AdN-translocator at the maximum rate of oxidative phosphorylation of rat-heart mitochondria. The results support the assumption that ADP diffusion towards the AdN-translocator is limited if its extramitochondrial concentration is low, resulting in a dynamic compartmentation of adenine nucleotides in the mitochondrial intermembrane space.
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PMID:Dynamic compartmentation of adenine nucleotides in the mitochondrial intermembrane space of rat-heart mitochondria. 380 62

A large part of the hexokinase activity of the rat brain 20,000g supernatant became mitochondrial bound when incubated with rat heart mitochondria which had been pretreated with glucose-6-phosphate. This binding was dependent on small-molecular compounds (as yet unidentified) of the brain supernatant. Divalent cations, spermine, and pentalysine strongly stimulated the binding of brain supernatant hexokinase to heart mitochondria. Inorganic phosphate, alpha-glycerophosphate, and fructose-1,6-diphosphate showed some stimulatory effect. No effect was observed with insulin or glucose. Mitochondria isolated from hearts of fasted rats had less specific hexokinase activity than mitochondria from fasted and then carbohydrate refed rats. This dietary treatment had no significant effect on the total heart hexokinase activity. Oligomycin did not inhibit the formation of creatine phosphate or glucose-6-phosphate by isolated rabbit heart mitochondria incubated in the presence of phosphoenolpyruvate and pyruvate kinase. However, the presence of creatine inhibited the formation of glucose-6-phosphate when the ATP/ADP ratio was low, indicating that creatine kinase has a greater access to ATP/ADP translocation than has hexokinase.
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PMID:Some observations on mitochondrial-bound hexokinase and creatine kinase of the heart. 400 20


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