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:1.17.3.2 (xanthine oxidase)
8,383 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Vegetative and reproductive cells of Basidiobolus haptosporus possess naturally occurring organelles identified as microbodies. Cells of four other species of the genus contained morphologically indistinguishable organelles. Microbodies were invariably present in cells of the fungi grown on routine mycological media. The constitutive microbody was characterized by a single, intensely electron-opaque crystalloid body which rapidly enlarged to fill the organellar compartment. The microbody then underwent degeneration by an autolytic-like process. Growth of the fungi on xanthine and its catabolites as sole nitrogen sources (but not urea) greatly enhanced the production of new microbodies in which protein was initially accumulated as paracrystalline arrays. These inclusions then underwent reorganization and compaction to form crystalloid bodies. Key enzymes of the purine degradation pathway are believed to be core proteins of the crystalloid. D-amino acid oxidase, alpha-hydroxy acid oxidase, xanthine oxidase and urate oxidase (but not catalase) were detected cytochemically in mature microbodies. Significant levels of phosphorus and molybdenum were present in the microbody crystalloid by X-ray dispersive microanalysis; iron and copper were not detected. The ability of Basidiobolus species to assimilate xanthine and its catabolites might explain their ecological association with the gut and cloacal contents of various amphibia, reptiles and fish.
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PMID:Ultrastructural cytology of Basidiobolus haptosporus: morphology and electron cytochemistry of microbodies. 615 82

A study has been made of e.p.r. signals due to Mo(V) in reduced sulphite oxidase (EC 1.8.3.1) from chicken liver. Reduction by SO3(2-), or photochemically in the presence of a deazaflavin derivative, produces spectra indistinguishable from one another. Three types of spectra from the enzyme were distingusihed and shown to correspond to single chemical species, since they could be simulated at both 9 and 35 GHz by using the same parameters. These were the low-pH form of the enzyme, with gav. 1.9805, the high-pH form, with gav. 1.9681 and a phosphate complex, with gav. 1.9741. The low-H form shows interaction with a single exchangeable proton, with A(1H)av. (hyperfine coupling constant) = 0.98 mT, probably in the form of an MoOH group. Parameters of the signals are compared with those for signals from xanthine oxidase and nitrate reductase. The signal from the phosphate complex of sulphite oxidase in unique among anion complexes of Mo-containing enzymes in showing no hyperfine coupling to protons. There is no evidence for additional weakly coupled protons or nitrogen nuclei in the sulphite oxidase signals. The possibility is considered that the enzymic mechanism involves abstraction of a proton and two electrons from HSO3- by a Mo = O group in the enzyme.
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PMID:Electron-paramagnetic-resonance parameters of molybdenum(V) in sulphite oxidase from chicken liver. 624 54

The inhibition by alloxanthine of oxidation of xanthine by xanthine oxidase is characterized by a prolonged transient phase. Kinetic data accord with a mechanism that involves rapid formation of a reduced enzyme-alloxanthine complex that subsequently undergoes a relatively slow-reversible reaction. In this scheme the slowly formed complex cannot be fully reoxidized by oxygen. From the Ki value for the dissociation of alloxanthine from the rapidly formed complex (1.15 microM) and values of 0.37 min-1 and 0.011 min-1 for the forward and reverse rate constants of the slow reaction, an overall inhibition constant for alloxanthine of 35 nM was calculated. A molybdenum (V) e.p.r. signal from the slowly formed reduced enzyme-alloxanthine complex is described. The rate of appearance of this new signal is consistent with this assignment. The signal (the "Alloxanthine signal") was simulated with g1 2,0269, g2 1,9593, g3 11.9444 and shows indications of hyperfine coupling to nitrogen. Similarities between it and the Very Rapid signal are discussed. Close structural analogies between the catalytic intermediate represented by the Very Rapid signal and the inhibitor complex represented by the Alloxanthine signal are suggested.
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PMID:Kinetic and e.p.r. studies on the inhibition of xanthine oxidase by alloxanthine (1 H-pyrazolo [3, 4-d] pyrimidine-4,6-diol). 627 12

The molybdenum EXAFS of the Mo(2Fe-2S) protein from Desulfovibrio gigas has been examined using fluorescence detection and synchrotron radiation. In the oxidized form the molybdenum environment is found to contain two terminal oxo groups and two long (2.47 A) Mo-S bonds. Evidence was also found for an oxygen or nitrogen donor ligand at 1.90 A. Addition of dithionite to the oxidized enzyme results in loss of a terminal oxo group, perhaps due to protonation. In addition, a 0.1 A contraction in the Mo-S bond lengths is observed. The behavior of both oxidized and dithionite-treated forms is similar to that observed previously with "desulfo" xanthine oxidase.
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PMID:Molybdenum EXAFS of the Desulfovibrio gigas Mo(2Fe-2S) protein--structural similarity to "desulfo" xanthine dehydrogenase. 632 97

Studies were carried out on the inhibitory complex of alloxanthine (1H-pyrazolo[3,4-d]pyrimidine-4,5-diol) with xanthine oxidase, in extension of the work of Williams & Bray [Biochem. J. (1981) 195, 753-760]. By suitable regulation of the reaction conditions, up to 10% of the functional enzyme could be converted into the complex in the Mo(V) oxidation state. The e.p.r. spectrum of the complex was investigated in detail with the help of computer simulation and substitution with stable isotopes. Close structural analogy of the signal-giving species to that of the Very Rapid intermediate in enzyme turnover is shown by g-values (2.0279, 1.9593 and 1.9442) and by coupling to 33S in the cyanide-labile site of the enzyme [A(33S) 0.30, 3.10 and 0.70mT]. However, whereas in the Very Rapid signal there is strong coupling to 17O [Gutteridge & Bray, Biochem. J. (1980) 189, 615-623], instead, in the Alloxanthine signal there is strong coupling to a single nitrogen atom [A(14N) 0.35, 0.35, 0.32 mT]. This is presumed to originate from the 2-position of the heterocyclic ring system. From this work and from earlier kinetic studies it is concluded that alloxanthine, after being bound reversibly at the active centre, reacts slowly with it, in a specific manner, distinct from that in the normal catalytic reaction with substrates. This reaction involves elimination of an oxygen ligand of molybdenum and co-ordination, in this site, of alloxanthine via the N-2 nitrogen atom, to give a complex that is structurally but not chemically closely analogous to that of the Very Rapid species.
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PMID:The structure of the inhibitory complex of alloxanthine (1H-pyrazolo[3,4-d]pyrimidine-4,6-diol) with the molybdenum centre of xanthine oxidase from electron-paramagnetic-resonance spectroscopy. 632 52

Formamide is a substrate of xanthine oxidase. At pH 8.2 and 1.14 mM-O2, Vmax.(app.) is 3.1 s-1 and Km (app.) is 0.7 M. Mo(V) e.p.r. signals obtained by treating the enzyme with formamide were studied, and these provide new information about the ligation of molybdenum in the enzyme and about the enzymic mechanism. The substrate is the first compound that is not a nitrogen-containing heterocycle to give a Very Rapid signal. This supports the hypothesis that the Very Rapid signal, though it is not detectable with all substrates, represents an essential intermediate in turnover. Formamide also gives the Inhibited signal and is the first non-aldehyde substrate to do so. The Rapid type 1 signal obtained in the presence of formamide was examined in H2O enriched with 2H or with 17O. The single oxygen atom detectable in the signal is shown to be strongly and anisotropically coupled. This indicates that this atom remains as an oxo ligand of molybdenum in this signal-giving species. Other structural features of this species are discussed.
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PMID:Formamide as a substrate of xanthine oxidase. 633 8

Fractionation of cell organelles of nitrogen-fixing nodules of cowpea (Vigna unguiculata L. Walp) by discontinuous and continuous sucrose density centrifugation indicated that starch-containing plastids possessed the complete pathway for purine nucleotide synthesis together with significant activities of some other enzymes associated with the provision of substrates in purine synthesis; triosephosphate isomerase (EC 5.3.1.1), NADH-glutamate synthase (EC 2.6.1.53), aspartate aminotransferase (EC 2.6.1.1), phosphoglycerate oxidoreductase (EC 1.1.1.95), and methylene tetrahydrofolate oxidoreductase (EC 1.5.1.5). Enzymes of purine oxidation, xanthine oxidoreductase (EC 1.2.3.2), and urate oxidase (EC 1.7.3.3) were recovered in the soluble fraction; glutamine synthetase (EC 6.3.1.2) occurred in bacteroids and in the cytosol. Intact, infected (bacteroid-containing) and uninfected cells were prepared by enzymatic maceration of the central zone of the nodule and partially separated by centrifugation on discontinuous sucrose gradients. Glutamine synthetase was largely restricted to infected cells whereas plastid enzymes, de novo purine synthesis, and urate oxidase were present in both cell types. Although the levels of all enzymes assayed were higher in infected cells, both cell types possessed the necessary enzyme complement for ureide formation. A model for the cellular and subcellular organization of nitrogen metabolism and the transport of nitrogenous solutes in cowpea nodules is proposed.
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PMID:Cellular and subcellular organization of pathways of ammonia assimilation and ureide synthesis in nodules of cowpea (Vigna unguiculata L. Walp.). 687 Feb 68

Oxygen-based free radicals have been shown to play a major role in the acute destruction of neurons following cerebral ischemia and may be involved in the chronic neurodegeneration seen in Parkinson's disease, Alzheimer's disease, and other conditions characterized by the progressive death of neurons in the central nervous system. Drugs belonging to a group of antioxidant compounds, collectively known as the lazaroids, have strong neuroprotective effects in experimental models of acute ischemia. However, the specific mechanisms by which these drugs reduce the harmful actions of free radicals have not been established. Using electron paramagnetic resonance (EPR) spectroscopy with spin trapping, we investigated the interaction of U-74500A, a first-generation lazaroid, and U-78517F, a second-generation lazaroid, with two species of oxygen-based free radicals in aqueous solution and with the stable nitrogen-based free radical diphenylpicrylhydrazyl in dimethyl sulfoxide. Superoxide radicals were generated by the action of xanthine oxidase on hypoxanthine. Hydroxyl radicals were generated by the Fenton reaction involving aqueous ferrous iron and hydrogen peroxide. Both lazaroids reduce the EPR signal of all three radicals, but the drugs differ in potency and relative radical selectivity. These observations are consistent with the lazaroids being scavengers of oxygen-based and nitrogen-based free radicals and suggest that the neuroprotective actions of the lazaroids in cerebral ischemia may involve direct interactions of the lazaroids with several different species of free radicals.
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PMID:An in vitro EPR study of the free-radical scavenging actions of the lazaroid antioxidants U-74500A and U-78517F. 763 55

It is currently believed that reactive oxygen species are produced in the heart post-ischemia reperfusion, causing pathophysiological disorders. Studies reported in the literature dealing with this subject have generated contradictory findings. The aim of this study was to assess the catalytic activity of the superoxide anion-producing enzyme xanthine oxidase, and the level of lipid peroxides in isolated rat heart muscle undergoing ischemia of varying duration and severity followed by reperfusion. Three levels of ischemia were investigated: total, and partial at either 0.10 or 0.35 ml/min (residual flow rate). Three different periods of ischemia were examined in each case. After each period of ischemia, followed by 10 min of reperfusion, the heart was frozen in liquid nitrogen. Xanthine oxidase activity and lipid peroxide levels were assayed in the cardiac homogenate and in the centrifuged supernatant, respectively. In the different experimental protocols studied here, both cardiac xanthine oxidase and lipid peroxide levels remained statistically unchanged compared to the continuously perfused control hearts. Moreover, in a recent study (Boucher et al., FEBS Lett. 203, 261-264, 1992), we were unable to detect reactive oxygen species in perfusate upon reperfusion of ischemic rat hearts. These results suggest that changes in xanthine oxidase activity during myocardial ischemia-reperfusion, and lipid peroxidation, as assessed by measuring thiobarbituric acid reactants and lipid hydroperoxides, are not predominant phenomena in ischemia-reperfusion-induced injury, at least in the experimental model used in this study.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Xanthine oxidase activity and lipid peroxide content following different types of ischemia in the isolated rat heart. 794 21

Active sodium (Na+) transport by alveolar type II (ATII) cells plays an important role in limiting the volume of alveolar fluid. Reactive oxygen and nitrogen species, released in the epithelial lining fluid by activated inflammatory cells or present in inspired gases, may damage Na+ transporters and decrease fluid reabsorption. To test this hypothesis we exposed ATII cells to xanthine and xanthine oxidase (1 or 10 mU/ml), or to boluses of peroxynitrite (0.1-1 mM final concentration) for 15 min and measured 1) cellular oxygen consumption (VO2); 2) amiloride-inhibitable 22Na+ uptake, as an index of Na+ movement through apically located Na+ channels; and 3) ouabain-sensitive 86Rb+ uptake, as an index of the activity of the basolaterally located Na(+)-K(+)-ATPase. After exposure of ATII cells to 0.5 or 1 mM peroxynitrite, amiloride-inhibitable 22Na+ uptake decreased to 68 +/- 7 and 56 +/- 11 of their control values, respectively (mean +/- SE; n > or = 6). Exposure to 0.5 mM peroxynitrite decreased ATII cell VO2 from 76 +/- 6 to 25 +/- 5 microM.h-1 x 10(6) cells-1 (mean +/- SE; n = 5). Cell viability and ouabain-sensitive 86Rb+ uptake remained at control levels for either peroxynitrite concentration. Exposure of ATII cells to 10 mU/ml xanthine oxidase decreased their VO2 from 94 +/- 8 to 63 +/- 6 (mean +/- SE; n = 5), but did not alter amiloride-inhibitable 22Na+ uptake. These findings indicate that physiological concentrations of peroxynitrite, but not of reactive oxygen species, decrease ATII cell Na+ transport by damaging apically located amiloride-sensitive Na+ channels.
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PMID:Peroxynitrite inhibition of oxygen consumption and sodium transport in alveolar type II cells. 802 51


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