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)

1. A comparative study was carried out on blood glucose partition and glucose metabolism of penguin erythrocytes and somatic tissues. Pygoscelidae penguins (Pygoscelis antarctica and P. papua) were used in these experiments. 2. Blood glucose partition was established by assaying whole blood and plasma glucose in several individuals of the gentoo and chinstrap penguins. 3. It was found that almost all the whole blood sugar is compartmentalized at the plasma site, the red blood cells being ineffective in regard to glucose metabolism. 4. Levels of hexokinase, phosphoglucose isomerase, phosphofructokinase, fructose bisphosphate aldolase, glyceraldehyde phosphate dehydrogenase, phosphoglycerate kinase, phosphopyruvate hydratase (enolase), pyruvate kinase, alpha-glycerolphosphate dehydrogenase and fructose bisphosphate phosphatase were estimated in the erythrocytes of both gentoo and chinstrap penguins, the same determinations being carried out also on the somatic tissues (leg muscle, breast muscle, heart muscle, liver and brain) of the gentoo.
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PMID:Blood glucose partition and levels of glycolytic enzymes in erythrocytes and somatic tissues of penguins. 292 38

The specific activities of each of the enzymes of the classical pentose phosphate pathway have been determined in both cultured procyclic and bloodstream forms of Trypanosoma brucei. Both forms contained glucose-6-phosphate dehydrogenase (EC 1.1.1.49), 6-phosphogluconolactonase (EC 3.1.1.31), 6-phosphogluconate dehydrogenase (EC 1.1.1.44), ribose-5-phosphate isomerase (EC 5.3.1.6) and transaldolase (EC 2.2.1.2). However, ribulose-5-phosphate 3'-epimerase (EC 5.1.3.1) and transketolase (EC 2.2.1.1) activities were detectable only in procyclic forms. These results clearly demonstrate that both forms of T. brucei can metabolize glucose via the oxidative segment of the classical pentose phosphate pathway in order to produce D-ribose-5-phosphate for the synthesis of nucleic acids and reduced NADP for other synthetic reactions. However, only procyclic forms are capable of using the non-oxidative segment of the classical pentose phosphate pathway to cycle carbon between pentose and hexose phosphates in order to produce D-glyceraldehyde 3-phosphate as a net product of the pathway. Both forms lack the key gluconeogenic enzyme, fructose-bisphosphatase (EC 3.1.3.11). Consequently, neither form should be able to engage in gluconeogenesis nor should procyclic forms be able to return any of the glyceraldehyde 3-phosphate produced in the pentose phosphate pathway to glucose 6-phosphate. This last specific metabolic arrangement and the restriction of all but the terminal steps of glycolysis to the glycosome may be the observations required to explain the presence of distinct cytosolic and glycosomal isoenzymes of glyceraldehyde-3-phosphate dehydrogenase and phosphoglycerate kinase. These same observations also may provide the basis for explaining the presence of cytosolic hexokinase and phosphoglucose isomerase without the presence of any cytosolic phosphofructokinase activity. The key enzymes of the Entner-Doudoroff pathway, 6-phosphogluconate dehydratase (EC 4.2.1.12) and 2-keto-3-deoxy-6-phosphogluconate aldolase (EC 4.1.2.14) were not detected in either procyclic or bloodstream forms of T. brucei.
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PMID:The enzymes of the classical pentose phosphate pathway display differential activities in procyclic and bloodstream forms of Trypanosoma brucei. 292 7

The effect of sesquiterpene lactones isolated from Geigeria was tested on three glycolytic enzymes. Phosphofructokinase was inhibited irreversibly by all of the sesquiterpene lactones, with ivalin(III) giving the highest extent of inhibition. Values for the kinetic constants Ki (1.3 mM) and kp (2.2 min-1) were established. Hexokinase and glyceraldehyde-3-phosphate dehydrogenase were also strongly inhibited at 1 mM and 3 mM concentrations of sesquiterpene lactones, respectively. Pre-incubation of ivalin with dithiothreitol decreased its inhibiting effect on phosphofructokinase, hexokinase and glyceraldehyde-3-phosphate dehydrogenase activities. Phosphofructokinase and hexokinase were protected against inhibition by ivalin by their respective substrates, adenosine-5'-triphosphate and glucose.
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PMID:The effect of the sesquiterpene lactones from Geigeria on glycolytic enzymes. 293 49

The intracellular distribution of the glycolytic enzymes hexokinase, glyceraldehyde-3-phosphate dehydrogenase, lactate dehydrogenase and the pyruvate kinase isoenzymes type M1 and type M2 within unfertilized hen eggs was studied. Most of glycolytic enzyme activities were found in the yolk fraction; 8-24% of total glycolytic enzyme activities were found in the vitelline membrane fraction. However, the specific activities of these enzymes in the vitelline membrane fraction are 19-72-fold higher (U/mg protein) and 45-178-fold more concentrated (U/g wet weight) than in the yolk fraction. The study of intracellular localization of pyruvate kinase isoenzymes shows that the blastodisc, latebra and vitelline membrane contain only pyruvate kinase type M2, whereas pyruvate kinase types M1 and M2 are found in the egg yolk. The exclusive occurrence of pyruvate kinase type M2 in the blastodisc is consistent with the concept that this isoenzyme is involved in the cell proliferation. The heterogeneous distribution of the glycolytic enzymes hexokinase, glyceraldehyde-3-phosphate dehydrogenase and lactate dehydrogenase, and the heterogeneous localization of the pyruvate kinase isoenzymes types M1 and M2 indicate that glycolysis is distributed heterogeneously within the unfertilized hen egg cell.
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PMID:Demonstration of a heterogeneous distribution of glycolytic enzymes and of pyruvate kinase isoenzymes types M1 and M2 in unfertilized hen eggs. 294 22

Preincubation with Mipafox and Methamidofos as well as Paraoxon (used as control) did not cause inhibition of hexokinase, phosphofructokinase, glyceraldehyde-3-phosphate dehydrogenase and lactate dehydrogenase. This is in contrast with the inhibition of glycolysis by other neurotoxic compounds (hexacarbons, acrylamide, carbon disulfide).
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PMID:Lack of inhibition of glycolytic enzymes by the neurotoxic organophosphorus compounds mipafox and methamidofos. 296 83

The in vitro effect of acrylamide and its analogues on rat brain glycolytic enzymes was examined to elucidate the biochemical lesions responsible for the pathogenesis of acrylamide-induced neuropathy. All test compounds inhibited glyceraldehyde-3-phosphate dehydrogenase, irrespective of their neurotoxicity, and their inhibitory potency was a linear function of the rate constant with reduced glutathione. Phosphofructokinase was also inhibited by some of the test compounds, independently of their neurotoxicity. The rate-limiting enzymes in glycolysis, hexokinase and pyruvate kinase, were not inhibited by acrylamide.
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PMID:Effect of acrylamide and related compounds on glycolytic enzymes of rat brain. 316 Dec 19

A latex phagocytosis technique was used to prepare relatively pure plasma membranes with inside-out orientation. This method was adapted through a number of modifications in order to evaluate the association of glycolytic enzymes with the cytoplasmic side of the plasma membrane of C6 glial cells. As phosphorylation is strictly coupled with transport in these cells, glycolytic enzymes, especially hexokinase, could metabolize glucose in close vicinity to its transporter. Of the enzymes tested, hexokinase is present in considerable quantities on these membranes (nearly 40% of homogenate specific activity), followed by D-glyceraldehyde-3-phosphate dehydrogenase (10%), pyruvate kinase (8%), and 3-phosphoglycerate kinase (1%). Except for hexokinase, the enzyme pattern presented here is different from that published for other membrane preparations.
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PMID:Association of glycolytic enzymes with the cytoplasmic side of the plasma membrane of glioma cells. 335 18

To determine whether respiratory muscles undergo alterations in enzyme activities of energy metabolism as a result of increased mechanical activity, adult male Wistar rats were subjected to a prolonged endurance training program. Analysis off maximal enzyme activity patterns in the diaphragm following 15 weeks of extreme training (final running duration: 210 min per day, 27 m.min-1 at 15 degrees grade, indicated significant reductions in the marker enzymes of the citric acid cycle (citrate synthase), glycolysis (pyruvate kinase, PK; lactate dehydrogenase, LDH), ketone body utilization (3-keto acid: CoA transferase) and transamination (glutamate pyruvate transaminase, GPT). No changes were found for the enzymes of glycogenolysis (phosphorylase, PHOSPH), glycolysis (glyceraldehyde phosphate dehydrogenase, GAPDH), glucose phosphorylation (hexokinase, HK) and beta-oxidation (3-hydroxyacyl: CoA dehydrogenase, HAD) following training. In contrast, in the external intercostal muscle, increases in the range of 57-77% were noted for the enzymes CS and HAD, whereas in the internal intercostal muscles no training induced alteration was evident for these enzymes. For both the intercostal muscles, a consistent trend was noted towards a reduction in all of the glycolytic enzymes investigated, however, significantly lower values were recorded for only PK and LDH in the internal intercostals. GPT was increased in the internal intercostal muscles. These findings indicate that the response pattern observed in the enzyme activities studied following training are to some degree specific to the respiratory muscle investigated.
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PMID:Differential response of enzyme activities in rat diaphragm and intercostal muscles to exercise training. 337 43

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

We have developed a simple and effective method to embed whole yeast cells in Lowicryl resins with excellent ultrastructural and antigenic preservation. Using affinity-purified antibodies eluted from electrophoretically separated proteins transferred to nitrocellulose, we have shown by immunoelectron microscopy that two glycolytic enzymes, glyceraldehyde-3-phosphate dehydrogenase and hexokinase, are present in the cytoplasm and the nucleus. Carboxypeptidase Y is localized in the yeast vacuole. These results agree with earlier localization studies based on subcellular fractionation.
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PMID:Immunolocalization of glyceraldehyde-3-phosphate dehydrogenase, hexokinase, and carboxypeptidase Y in yeast cells at the ultrastructural level. 354 82


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