Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.1.3.5 (5'-nucleotidase)
 3,167 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Enzymopathies are described concerning the enzymes of the oxidative pentose phosphate pathway including the glutathion system, of the majority of glycolytic enzymes as well as of the ATPase, adenylate kinase and pyrimidine-5'-nucleotidase. The distribution and the frequency of the enzymopathies differ strongly in the various regions of the world. Glucose-6-phosphate dehydrogenase and pyruvate kinase show the highest frequency. The detected polymorphism of the pathological enzyme variants is one of the reasons for the fact that no correlation between the decrease of the catalytic activity and the severity of the anaemias has been found. For the identification of risk-groups more precise methods are necessary. Till now the detailed relationships between enzymopathy and non-spherocytic haemolytic anaemias are not clarified. Furthermore the molecular mechanism of the instability of pathological enzyme variants is not yet clear.
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PMID:[Enzyme deficient non-spherocytic hemolytic anemias]. 67 10

1. Wheat shoot phosphotransferase has been employed, with p-nitrophenylphosphate as a phosphate donor, to specifically phosphorylate the 5'-position of a variety of nucleosides and nucleoside analogues. The specificity of the enzyme towards the 5'-position of pentose nucleosides is testified to by the complete resistance to phosphorylation of 5'-O-methylcytidine. 2. With the use of ion-exchange chromatography, the foregoing procedure has been applied to the large-scale preparation of nucleoside-5'-phosphates with overall yields of the order of 80-90%. Quantitative recovery of unreacted nucleoside makes it possible to use this method without risk of losses either on a small or large scale with rare nucleosides. It is also applicable to acid- and alkali-labile nucleosides which cannot readily be phosphorylated by chemical procedures. 3. The wheat shoot phosphotransferase also phosphorylated a galactopyranosyl nucleoside, as well as such derivatives as 1-(beta-hydroxyethyl)cytosine and 5-(beta-hydroxyethyl)uracil, showing that the enzyme does not have an absolute requirement for a 5-membered sugar ring, but rather for the presence of a primary hydroxyl group. 4. The phosphorylated derivatives of galactopyranosyluracil, and of both hydroxyethyl pyrimidines, were resistant to 5'-nucleotidase. E. coli alkaline phosphatase converted all three nucleotides quantitatively to the starting compounds. 5. A synthesis of 1-(beta-hydroxyethyl)cytosine is described.
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PMID:Preparative enzymic synthesis of nucleoside-5'-phosphates. 109 45

The human erythrocyte generates high-energy adenosine triphosphate by anaerobic glycolysis and cycles oxidized and reduced nicotinamide adenine dinucleotide phosphate by the aerobic pentose phosphate shunt pathway. Certain enzymopathies of the pentose phosphate shunt are associated with hemolysis resulting from oxidative denaturation of hemoglobin. Glucose-6-phosphate dehydrogenase deficiency, an X-chromosome-linked disorder, is the prototype of these diseases and is genetically and clinically polymorphic. Six enzymopathies of anaerobic glycolysis cause hemolytic anemia; lactate dehydrogenase deficiency does not. In 2,3-diphosphoglycerate mutase deficiency, 2,3-diphosphoglycerate is greatly reduced and asymptomatic polycythemia is noted. Pyrimidine-5'-nucleotidase deficiency, an enzymopathy of nucleotide metabolism, is characterized by intracellular accumulations of pyrimidine-containing nucleotides, marked basophilic stippling on the stained blood film, splenomegaly, and hemolysis. Lead inhibits the nucleotidase and an identical syndrome occurs during severe lead poisoning. Hemolysis also accompanies an unusual enzymopathy characterized by a 40- to 70-fold increase (not decrease) in adenosine deaminase activity.
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PMID:Hemolytic anemias and erythrocyte enzymopathies. 299 Feb 76

Muscle biopsies from six horses with clinical histories of muscle atrophy, muscle tremors, myopathic symptoms, unsteadiness of pelvic limbs and progressive ataxia were examined. Muscle biopsies were studied with enzyme histochemical techniques to evaluate the diagnostic values of these methods in cases suspected of suffering from neuromuscular disorders. Hypertrophy, atrophy, fibre splitting, waxy degeneration, phagocytosis and necrosis were seen in haematoxylin eosin stained sections of the different cases. Fibre type predominance and fibre type grouping were seen in the calcium ion stimulated myosine ATP-ase (Ca-ATP-ase) stained sections of some cases. 'Moth-eaten fibres' were demonstrated in three cases by staining with NADH: nitro blue tetrazolium oxidoreductase (NADH-TR), succinate dehydrogenase (SDH), NADH dependent malate dehydrogenase, cytochrome c oxidase and by lactate dehydrogenase. The catabolic enzymes, acid phosphatase (ACP) and 5'-nucleotidase were active in cases with fibre phagocytosis. The oxidative part of the pentose phosphate pathway in myopathic tissue seemed to be important in three cases, demonstrated by the increased activity of glucose-6-phosphate dehydrogenase (GPDH) and 6-phosphogluconate dehydrogenase (PGDH). The important feature of diseased horse muscle was that the pathohistochemical changes were exactly the same as in diseased skeletal muscles of humans. The application of tissue saving enzyme histochemical techniques can be recommended in the study of muscle tissue from horses suffering from suspected neuromuscular disorders.
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PMID:Enzyme histochemistry on muscle biopsies as an aid in the diagnosis of diseases of the equine neuromuscular system: a study of six cases. 336 6

Nitrogenase in Rhodospirillum rubrum is regulated in vivo by the covalent modification of the Fe protein. This paper reports the isolation, purification, and properties of the modifying group that has been heat released from the Fe protein. The molecule is isolated from the heated mixture by binding to a boronate affinity column. Purification is achieved on an ion-exchange high-performance liquid chromatography column. Structural properties of the molecule have been investigated by using proton and phosphorus NMR, mass spectrometry, enzyme susceptibility, and chromatographic methods. The heat-released modifying group exhibits an unusual signal in the proton NMR spectrum at 1.26 ppm. The molecule also contains a functional group which can be reduced by borohydride. This group is lost on breakdown of the molecule or upon treatment of the molecule with 5'-nucleotidase. The identity of the base and the pentose of modifying group as adenine and ribose, respectively, is confirmed. Ratios of the known components of the modifying group are established.
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PMID:Purification and properties of the heat-released nucleotide-modifying group from the inactive iron protein of nitrogenase from Rhodospirillum rubrum. 392 13

We evaluated the erythrocytes of two patients with hereditary pyrimidine 5'-nucleotidase deficiency. Significant findings included an increased reduced glutathione content, increased incubated Heinz body formation, a positive ascorbate cyanide test, and decreased intraerythrocytic pH. The pentose phosphate shunt activity of the patients' red cells as measured by the release of 14CO2 from 14C-1-glucose was decreased compared to high reticulocyte controls. Glucose-6-phosphate dehydrogenase (G6PD) activity in hemolysates from control erythrocytes was inhibited 43% by 5.5 mM cytidine 5'-triphosphate (CTP) and 50% by 5.5 mM in uridine 5'-triphosphate (UTP) at pH 7.1. CTP was a competitive inhibitor for G6P (Ki = 1.7 mM) and a noncompetitive inhibitor for NADP+ (Ki = 7.8 mM). Glutathione peroxidase, glutathione reductase, and 6-phosphogluconate dehydrogenase were not affected by these compounds. Pentose phosphate shunt activity in control red cell hemolysate at pH 7.1 was inhibited to a similar degree by 5.5 mM CTP or UTP. Since the intracellular concentrations of G6P and NADP+ are below their KmS for G6PD, these data suggest that high concentrations of pyrimidine 5'-nucleotides depress pentose phosphate shunt activity in pyrimidin 5'-nucleotidase deficiency. Thus, this impairment of the pentose phosphate pathway appears to contribute to the pathogenesis of hemolysis in pyrimidine 5'-nucleotidase deficiency hemolytic anemia.
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PMID:Hemolytic anemia in hereditary pyrimidine 5'-nucleotidase deficiency: nucleotide inhibition of G6PD and the pentose phosphate shunt. 628 44

An increased concentration of cytidine diphosphocholine (CDP-choline) has been observed in erythrocytes in the hemolytic anemia due to hereditary pyrimidine 5'-nucleotidase deficiency (P5Nase, EC 3.1.3.5) and in a patient with a chronic hemolytic anemia not due to P5Nase deficiency, as reported by Paglia and co-workers in 1983. In the current studies, we were unable to demosntrate a significant inhibitory effect of 4 mmol/l CDP-choline on the activities of the enzymes of the Embden-Meyerhof and pentose phosphate pathways. The physiologic significance of increased erythrocytic CDP-choline remains to be determined.
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PMID:CDP-choline does not inhibit erythrocyte glycolytic or pentose phosphate pathway enzyme activity. 652 98

Twenty eight enzymatic activities and four macromolecular substances have been histochemically compared in rat and rabbit aortas, embedded in a common block. The study was carried out at different stages of development: 3 days, 3 months, 7-9 months and 17-19 months. In addition, lipase and cholinesterase were biochemically assayed in adult rat and rabbit aortas. The rat aortas (atheroresistant) had a better supply of aerobic oxidoreductases [linked to the pentose pathway (G6PD, 6PGD) as well as to the Krebs cycle (SD, ICD)], lipolytic enzymes (acid esterases, cholinesterase, lipase), lysosomal enzymes (acid PH/ase, Aryl-sulf/ase - Betaglu/ase), ADPase - ATPase - AlK Ph/ase Alpha GPD and acid lipids. Rabbit aortas (atherosensitive) were richer in metachromatic GAG, UDPGD (GAG Anabolism), glycogen, and related enzymes (phosphorylase, glycogen synthetase) as well as 5'-nucleotidase, Beta HBD, Lactate D and Aldolase. These differences support the hypothesis that arterial atherosensitivity is related to the activity and efficiency of smooth muscle cell energetic and catabolic processes, which govern the behaviour of lipids, proteins and carbohydrates as they penetrate the arterial wall. The factors that determine the proliferative and sclerogenic responses of arterial tissues to aggressions and, in particular, the response to lipids, remain, however, to be determined.
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PMID:A comparative study of the arterial tissue metabolism in atherosensitive and atheroresistant species. I. Comparison between rabbit and rat aortas. 734 89