Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:2.7.1.1 (hexokinase)
 5,274 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Mean levels of 2,3-diphosphoglycerate (DPG) were significantly increased in erythrocytes (RBC) from 43 nonanemic black blood donors (4.80 +/- 0.06 micromoles/l RBC) compared with 22 white donors 4.47 +/- 0.08 micromoles/l RBCs from eight of the 12 black donors with DPG levels greater than 5 micromoles/l RBC. Although a potentially hemolytic disorder could be defined in four (AS hemoglobin, beta-Thalassemia minor, G6PD deficiency), reticulocyte counts were normal. However, when RBCs from the subgroup were compared to RBCs from an additional 25 unselected white donors, the following suggested an abnormally large population of young RBCs in the subgroup: 1) normal or elevated RBC-ATP with normal serum phosphate level; 2) significantly increased activities of RBC age-dependent enzymes hexokinase (p less than 0.02), pyruvate kinase (p less than 0.05), and glutamicoxaloacetic transaminase (p less than 0.01), with normal activity of phosphoglycerate kinase, an age-independent enzyme; 3) decreased dense (older) RBCs as determined by sedimentation in phthalate esters. Since DPG is increased in young RBCs and falls as the RBC ages, loss of older relatively DPG depleted RBCs due to shortened survival could account for the elevated DPG levels seen in the subgroup.
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PMID:Elevated red blood cell 2,3-diphosphoglycerate levels in black blood donors. 62 75

Chronic (6 days) hyperinsulinaemia in young rats produced lower blood glucose concentrations and augmented body- and liver-weight gain. The insulin-treated rats had increased hepatic activities of citrate-cleavage enzyme, 'malic' enzyme and high-substrate (6.6 mM-phosphoenolpyruvate) pyruvate kinase, and decreased glucose 6-phosphatase. There were no changes in activities of phosphoenolpyruvate carboxykinase, phosphofructokinase, low-substrate (1.3 mM-phosphoenolpyruvate) pyruvate kinase, glucokinase and hexokinase.
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PMID:Effects of chronic hyperinsulinaemia on hepatic enzymes involved in lipogenesis and carbohydrate metabolism in the young rat. 66 50

31P NMR studies with Cd(II) and Zn(II) chelates of adenosine 5'-O-(3-thiotriphosphate) (ATPgammaS) and the Cd(II) chelate of adenosine 5'-O-(2-thiotriphosphate) (ATPbetaS) indicate that these metal ions chelate to the sulfur atom of the thiophosphate group. Since Mg(II) chelates to oxygen of the thiophosphate group of diastereoisomer is equivalent to the configuration of the Cd(II) chelate of the opposite diastereoisomer. As a consequence, an inversion of the stereospecificity is observed when Cd(II) is substituted for Mg(II) in the phosphoryl transfer reactions catalyzed by yeast hexokinase and rabbit muscle pyruvate kinase. When Co(II) is the activating ion for yeast hexokinase with ATPbetaS as substrate, no stereospecificity is observed. Since the absolute configuration for the diastereoisomer of Co(III)(NH3)4ATP which is the active substrate for yeast hexokinase has been established by Cornelius and Cleland (Cornelius, R. D., and Cleland, W. W. (1978) Biochemistry, in press), the absolute stereochemistry of the Mg(II) complex of the B isomer of ATPbetaS is now established by its stereospecificity in the hexokinase reaction.
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PMID:Divalent cation-dependent stereospecificity of adenosine 5'-O-(2-thiotriphosphate) in the hexokinase and pyruvate kinase reactions. The absolute stereochemistry of the diastereoisomers of adenosine 5'-O-(2-thiotriphosphate). 67 Jan 66

Metabolic activity of rat lungs were studied in normal state and in acute hypoxia, caused by an effect of rarefied atmosphere (3 hrs, "height" 10,000 m). Glycolytic splitting of carbohydrates and catabolism of proteins were increased in lungs under hypoxic stress. In hypoxia activities of adlobase, pyruvate kinase, succinate dehydrogenase, 5-hydroxytryptophan decarboxylase were increased, but hexokinase activity was decreased. Activities of lipase, lactate dehydrogenase and NAD-dependent malate dehydrogenase were not altered, whereas the ratio in specific activity of cytoplasmic malate dehydrogenase and lactate dehydrogenase was decreased.
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PMID:[Effect of acute hypoxia on the metabolic activity of lung tissue]. 70 55

Activities of four enzymes of the glycolytic pathway, hexokinase, glyceraldehyde 3-phosphate dehydrogenase, pyruvate kinase and lactate dehydrogenase, were determined in a vesicular brush-border preparation from rabbit kidneys. The specific activities of the enzymes were decreased several-hundredfold in the brush-border preparation compared with a kidney homogenate, but the enzymes were not totally absent. Density-gradient centrifugation of the brush-border preparation yielded brush border of even higher purity and also a characteristic pattern of distribution for each of the contaminating intracellular membranes. The presence of hexokinase in the brush-border preparation could be traced to contaminating mitochondria, and that of glyceraldehyde 3-phosphate dehydrogenase, pyruvate kinase and lactate dehydrogenase to contaminating vesicles derived from the endoplasmic reticulum. The brush-border vesicles contained some ATP. An intravesicular concentration of 0.1mm was estimated, indicating that the vesicles had retained at least a part of their original content. Experiments in which fluorescein isothiocyanate-dextran (mol.wt. 20000) was present during cell lysis revealed that much, but not all, of the brush-border contents had been exchanged with the medium. The complete absence of glycolytic enzymes from brush-border vesicles, which had retained part of their original content, indicates that the brush border does not contain glycolytic enzymes in vivo and can be thought of as a compartment of its own, somehow separated from the cytoplasm.
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PMID:The brush border of rabbit kidney, a cellular compartment free of glycolytic enzymes. 70 4

Despite the presence of a marked decrease in liver protein content 48 h after a single injection of D-galactosamine, increased activities of glucose-6-phosphate dehydrogenase, low-Km hexokinase and pyruvate kinase type M2 were observed in the injured liver. Microsomal aniline hydroxylase activity and cytochrome P-450 content in liver decreased significantly in 48 h of galactosamine treatment but not in the first 2 h in contrast with carbon tetrachloride (CCL4) intoxication. The extents of those changes were not so great as in CCl4-treated rats. The disaggreation of polyribosomes in liver was observed in 24 h of galactosamine treatment. However, the formation of microsomal lipoperoxidation did not increase in the entire course of acute liver injury by the amino sugar. These results taken together with our previous observations indicate that the dysregulation of protein synthesis is an essential biochemical event of hepatocyte injury induced by treatment of rats with galactosamine as well as CCl4.
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PMID:Dysregulation of protein synthesis in injured liver. A comparative study on microsomal and cytosole enzyme activities, microsomal lipoperoxidation and polysomal pattern in D-galactosamine and carbon tetrachloride-injured livers. 71 Mar 83

Untrained healthy male volunteers were studied to observe the effects of physical exercise (bicycle ergometer, 920 kpm/min for 10 min, 15 min and 30 min) upon glycolytic intermediates in red blood cells. The levels of glucose 6-phosphate, fructose 6-phosphate, pyruvate and lactate increased after each exercise. The levels of fructose 1,6-diphosphate increased and phosphoenolpyruvate decreased respectively only after 30 min of exercise. At the rest period of 30 min after 30 min of exercise the lactate level still remained unchanged, however all the other intermediates returned to the preexercise values. A negative crossover point seemed to exist between fructose 6-phosphate and fructose 1, 6-diphosphate after 15 min of exercise. A positive crossover point was observed between phosphoenolpyruvate and pyruvate after 30 min of exercise. There were significant increases in hexokinase and pyruvate kinase activities, but not in phosphofructokinase activity after 30 min of exercise. These facts suggested that the increase in pyruvate kinase activity was due to the elevated fructose 1,6-diphosphate level after 30 min of exercise. A significant increase in plasma dopamine-beta-hydroxylase activity was found after each exercise. A close positive correlation was observed between pyruvate-phosphoenolpyruvate ratio and dopamine-beta-hydroxylase activity after 30 min of exercise. It was suggested that pyruvate-phosphoenolpyruvate ratio provided a reliable index of physical exercise.
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PMID:[Effect of physical exercise on glycolysis in human red blood cells (author's transl)]. 71 Nov 26

Haemoglobin fractions and 16 enzymatic activities of red cells of a patient with juvenile chronic myeloid leukaemia are compared to normal, to comparably reticulocyte-rich, non-neonatal and to fetal red cells. The activities of hexokinase, triosephosphate isomerase, glyceraldehyde-3-phosphate dehydrogenase, monophosphoglyceromutase, enolase and glucose-6-phosphate dehydrogenase are significantly increased in fetal red cells beyond the activities of cell populations with comparable reticulocytosis. The activities of these enzymes are also increased in the patient's erythrocytes. Together with a haemoglobin F concentration of 54% and a concentration of haemoglobin Bart's of 1% these variations reflect the fetal nature of the red cells. Simultaneously, signs of dyserythropoiesis are found in the red cells of the patient: a very high activity of hexokinase and a low pyruvate kinase activity.
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PMID:Fetal erythropoiesis and dyserythropoiesis in juvenile chronic myeloid leukaemia. 82 74

The stability of various glycolytic enzymes of human erythrocytes has been studied by the mechanical shaking method. The rate of denaturation apparently followed first order kinetics. The t1/2, the shaking time required to denature 50% of the original activity, for glucose-6-phosphate dehydrogenase, phosphofructokinase, and pyruvate kinase was less than 1 min; that for hexokinase, 6-phosphogluconate dehydrogenase, and monophosphoglyceromutase was between 2 and 13 min; that for all the other enzymes was more than 30 min. Since the t1/2 value for each enzyme is highly reproducible if the shaking conditions are kept constant, these parameters may be used as an indicator of protein stability in solution. The mechanical denaturation method may also be used to remove unstable components from a mixture of proteins with different stabilities.
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PMID:Stability of glycolytic enzymes of human erythrocytes. 83 47

The authors investigated the in vitro functional differentiation of fetal mouse liver cultured in Rose's circumfusion system with the use of two biochemical markers: The analysis of the inductive response of key enzymes in carbohydrate metabolism to insulin, and the analysis of the liver-specific isozyme of pyruvate kinase [EC 2.7.1.40]. The glucokinase [EC 2.7.1.2] activity, which is only found in mammalian adult liver, emerged on cultivation of 2-3 days and reached a maximum level equivalent to one-half of the adult level. Two- or 3-fold increases in the glucokinase, pyruvate kinase, and glucose-6-phosphate dehydrogenase [EC 1.1.1.49] were induced by a single dose of insulin in fetal liver after 12 days of cultivaton. Hexokinase [EC 2.7.1.1] activity was barely influenced by insulin. These results suggested that fetal mouse liver cultured in this system for 2 weeks maintained the same response to insulin as in vivo adult mouse liver. The pyruvate kinase isozyme patterns of mouse livers in various developmental stages and of cultured fetal mouse liver in the present system were investigated by isoelectric fractionation. The pyruvate kinase isozymes having the highest relative activity were the pI-5.5 isozyme for the adult liver and the pI-6.5 isozyme for 13- to 14-day-old fetal liver. As development in vivo proceeded, a gradual change in isozyme pattern occurred; this consisted of a progressive decrease of the pI-6.5 pyruvate kinase isozyme, "fetal type," in favor of the pI-5.5 isozyme, "adult type." The pyruvate kinase isozyme pattern in 13- to 14-day fetal liver cultured in the system for 2 weeks was similar to that found in adult liver. Thus, it was shown that "fetal type" pyruvate kinase was also replaced by "adult type" pyruvate kinase in vitro. It can be concluded from these findings that fetal mouseliver cultured in the circumfusion system for 2 weeks maintains its functional and morphological identitites as it differentiates toward the adult liver.
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PMID:Functional differentiation of mouse fetal liver in circumfusion system cultures. 93 74


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