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:3.2.1.17 (lysozyme)
21,489 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Thermothrix thiopara is isolated from hot sulfur springs. It occurs in situ at a temperature of 72 degrees C, a pH of 7.0, and an HS concentration of 17.4 mumol/liter (0.8 ppm). The organism was capable of autotrophic growth. Sulfite, sulfur, and polythionates were formed and subsequently degraded to sulfate during growth with thiosulfate as the sole energy source. Thiosulfate was oxidized by the polythionate pathway, and the stoichiometry of growth on thiosulfate was determined. The organism was also capable of heterotrophic growth in amino acids and simple sugars. A source of reduced sulfur (methionine, glutathione) was required for heterotrophic growth. Growth occurred aerobically or anaerobically with nitrate as a terminal oxidant. Both nitrous oxide and dinitrogen were produced. At 73 degrees C the maximum autotrophic growth rate in batch culture using thiosulfate was 0.56 generation per h. Under the same conditions in continuous culture, washout occurred at a dilution rate of 0.3 to 0.4 per h, corresponding to a cellular growth rate of 0.43 to 0.58 generation per h. This was nearly three times the growth rate for Thiobacillus denitrificans. T. thiopara is gram negative. It was also found to be both lysozyme and penicillin susceptible. As a result, this organism cannot be considered an archaebacterium.
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PMID:Thermothrix thiopara: Growth and Metabolism of a Newly Isolated Thermophile Capable of Oxidizing Sulfur and Sulfur Compounds. 1634 1

The three-dimensional structure of hen egg-white lysozyme (HEWL) in a hexagonal crystal form has been determined and refined to 1.46 A resolution. This hexagonal crystal form crystallizes from a saturated sodium nitrate solution at pH 8.4. The crystals belong to space group P6(1)22, with unit-cell parameters a = b = 85.64, c = 67.93 A. A total of 165 water molecules, 16 nitrate ions and five sodium ions were located in the electron-density map. The hexagonal crystal form exhibits a higher solvent content and a higher degree of disorder than other crystal forms of lysozyme. The flexibility of the protein depends on the crystal packing, although some residue ranges are flexible in all native HEWL crystal forms.
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PMID:The structure of the hexagonal crystal form of hen egg-white lysozyme. 1655 35

Two monoclinic crystals (space group P2(1)) of hen egg-white lysozyme, a type I crystal grown at room temperature in a D2O solution with pD 4.5 containing 2%(w/v) sodium nitrate and a type II crystal grown at 313 K in a 10%(w/v) sodium chloride solution with pH 7.6, were each transformed into another monoclinic crystal with the same space group by dehydration-induced phase transition. Changes in X-ray diffraction were recorded to monitor the progress of the crystal transformation, which started with the appearance of diffuse streaks. In both crystals, the intensity of h + l odd reflections gradually weakened and finally disappeared on completion of the transformation. X-ray diffraction in the intermediate state indicated the presence of lattices of both the native and transformed crystals. In the native type I crystal, two alternate conformations were observed in the main chain of the region Gly71-Asn74. One conformer bound a sodium ion which was replaced with a water molecule in the other conformer. In the transformed crystal, the sodium ion was removed and the main-chain conformation of this region was converted to that of the water-bound form. The transformed crystal diffracted to a higher resolution than the native crystal, while the peak width of the diffraction spots increased. Analysis of the thermal motion of protein molecules using the TLS model has shown that the enhancement of the diffraction power in the transformed crystal is mainly ascribable to the suppression of rigid-body motion owing to an increase in intermolecular contacts as a result of the loss of bulk solvent.
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PMID:Structural phase transition of monoclinic crystals of hen egg-white lysozyme. 1655 38

Nickel(II)-xylylbicyclam is a potent anti-HIV agent and binds strongly to the CXCR4 co-receptor. We have investigated configurational equilibria of Ni(II)-cyclam derivatives, since these are important for receptor recognition. Crystallographic studies show that both trans and cis configurations are readily formed: [Ni(cyclam)(OAc)(2)] x H(2)O adopts the trans-III configuration with axial monodentate acetates, as does [Ni(benzylcyclam)(NO(3))(2)] with axial nitrate ligands, whereas [Ni(benzylcyclam)(OAc)](OAc)2 x H(2)O has an unusual folded cis-V configuration with Ni(II) coordination to bidentate acetate. UV/Vis and NMR studies show that the octahedral trans-III configuration slowly converts to square-planar trans-I in aqueous solution. For Ni(II)-xylylbicyclam, a mixture of cis-V and trans-I configurations was detected in solution. X-ray diffraction studies showed that crystals of lysozyme soaked in Ni(II)-cyclam or Ni(II) (2)-xylylbicyclam contain two major binding sites, one involving Ni(II) coordination to Asp101 and hydrophobic interactions between the cyclam ring and Trp62 and Trp63, and the second hydrophobic interactions with Trp123. For Ni(II)-cyclam bound to Asp101, the cis-V configuration predominates.
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PMID:Configurations of nickel-cyclam antiviral complexes and protein recognition. 1712 Feb 66

In protein crystallography, spherulites are considered the result of a failed crystallization experiment. Understanding the formation of these structures may contribute to finding methods to prevent their formation. Here, we present an in situ study on lysozyme spherulites grown from sodium nitrate and sodium thiocyanate solutions, investigating their morphology and growth kinetics using optical microscopy. In a morphodrom, we indicate the conditions at which spherulites form for the lysozyme-nitrate system, showing that liquid-liquid phase separation is not a prerequisite to form sheaflike spherulites and that supersaturation is not the only factor determining their creation. Despite their sheaflike morphology, the spherulites all appear to be formed through heterogeneous nucleation. The spherulites are of a new polymorphic form and are less stable than the monoclinic form. For a single needle, growth kinetics indicate surface processes to be the rate-limiting step during growth, but for an entire spherulite volume, diffusion still plays a role. Spherulites simulated by using a time-dependent, tip-splitting model are found to compare well to experimentally observed spherulites.
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PMID:Spherulitic growth of hen egg-white lysozyme crystals. 1726 69

The application of five water-soluble, halogen-free, alkylammonium-based ionic liquids (ILs) as additives for advanced crystallization of lysozyme was investigated. Their biocompatibility was determined by long-term measurement of the overall mean relative enzyme activities. These were maximally reduced by about 10-15% when up to 200 g IL l(-1) was added. Sitting-drop vapor diffusion crystallization experiments revealed that the addition of some of the ILs led to less crystal polymorphism and precipitation was avoided reliably even at larger NaCl concentrations. The addition of ILs tended to result in larger crystals. The kinetics of lysozyme crystallization were significantly enhanced using ILs as crystallization additives, e.g. by a factor of 5.5 when 100 g ethanolammonium formate l(-1 )was added. ILs with "soft" anions, such as formate or glycolate, were superior to ILs with "hard" anions, like nitrate.
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PMID:Advanced protein crystallization using water-soluble ionic liquids as crystallization additives. 1766 51

The crystal structure of triclinic hen egg-white lysozyme (HEWL) has been refined against diffraction data extending to 0.65 A resolution measured at 100 K using synchrotron radiation. Refinement with anisotropic displacement parameters and with the removal of stereochemical restraints for the well ordered parts of the structure converged with a conventional R factor of 8.39% and an R(free) of 9.52%. The use of full-matrix refinement provided an estimate of the variances in the derived parameters. In addition to the 129-residue protein, a total of 170 water molecules, nine nitrate ions, one acetate ion and three ethylene glycol molecules were located in the electron-density map. Eight sections of the main chain and many side chains were modeled with alternate conformations. The occupancies of the water sites were refined and this step is meaningful when assessed by use of the free R factor. A detailed description and comparison of the structure are made with reference to the previously reported triclinic HEWL structures refined at 0.925 A (at the low temperature of 120 K) and at 0.95 A resolution (at room temperature).
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PMID:Triclinic lysozyme at 0.65 A resolution. 1808 73

The protozoan Perkinsus marinus is considered the most important pathogen of the eastern oyster Crassostrea virginica, causing high mortality in natural and farmed oysters on the Atlantic coast of the US. In Mexico, no serious P. marinus epizootic has been reported. This study describes the current state of P. marinus prevalence in Terminos Lagoon (Mexico) associated with environmental factors including salinity, temperature, ammonium, nitrate, nitrite, silica, and phosphorus. In addition, the association of physiological (hemocyte density, protein concentration) and immunological (lysozyme, agglutination) parameters with the infection were studied. The prevalence was significantly different among seasons with mean values of 70, 23, and 7% in the dry (February to May), rainy (June to September) and north-wind (October to January) seasons, respectively. Only light infection intensity (Mackin scale value < 1) was observed. Prevalence of P. marinus was associated with seasonal salinity, phosphorus, and silica variations. Comparisons of oyster health demonstrates that the rainy and north-wind seasons are stressful periods. Redundancy analysis showed that only 34% of the variation in seasonal P. marinus prevalence was explained by protein concentration (21%), lysozyme (12%), and agglutination (1%). Overall, the data suggest that freshwater input associated with high nutrient concentrations during the rainy and north-wind seasons has a strong negative effect on P. marinus prevalence and also influences the oysters' physiology. It is probable that this seasonal stress was responsible for the absence of an epizootic event in Terminos Lagoon.
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PMID:Factors associated with the prevalence of Perkinsus marinus in Crassostrea virginica from the southern Gulf of Mexico. 1859

Photocleavage of chicken hen egg lysozyme by three Co(III)ammine complexes, hexamminecobalt(III) chloride ([Co(NH3)6]+3), pentamminechloro cobalt(III)chloride ([Co(NH3)5Cl]+2), and tetramminecarbonato cobalt(III) nitrate ([Co(NH3)4CO3]+), is reported here. Photocleavage resulted in two fragments of molecular masses of approximately 10.5 kDa and approximately 3.5 kDa which add-up to that of the parent molar mass. Detailed studies on the influence of irradiation time, excitation wavelength, the type of ligand coordinated to Co(III), concentration of the metal complex, the addition of competing metal ions, and quenchers on the protein photocleavage are reported. The Co(III) complexes also photocleaved apotransferrin, bovine serum albumin, and yeast enolase. Near-equimolar concentrations of Ni(II), Co(II) or Gd(III) inhibited the photocleavage, and therefore, binding of Co(III) metal complexes to Ni(II)/Co(II)/Gd(III) binding sites on lysozyme is necessary for the observed photocleavage. Since these ions are known to bind to Asp52 on lysozyme, we suspect that the above Co(III) complexes bind at this site, and initiate the protein cleavage. The Co(III) complexes have appropriate photochemical reactivities to cleave the peptide backbone, and they may be useful in the design of novel photochemical approaches to cleave the protein backbone.
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PMID:Inorganic photochemical protein scissors: photocleavage of lysozyme by Co(III) complexes. 1903 6

It is well-known that the addition of salts influences the properties of proteins in solution. The essential nature of this phenomenon is far from being fully understood, partly due to the absence of the relevant thermodynamic information. To help fill this gap, in this work isothermal titration calorimetry (ITC) was employed to study the ion-lysozyme association in aqueous buffer solutions at pH = 4.0. ITC curves measured for NaCl, NaBr, NaI, NaNO3, NaSCN, KCl, CaCl2, and BaCl2 salts at three different temperatures were described by a model assuming two sets of independent binding sites on the lysozyme. The resulting thermodynamic parameters of binding of anions (counterions) to the first class of sites (N approximately 7) indicate that the binding constant (K approximately 102 M-1) increases in the order Cl- < Br- < I- < NO3- < SCN-. The anion-lysozyme association is entropy driven, accompanied by a small favorable enthalpy contribution and a positive change in heat capacity. It seems that the entropy and heat capacity increase is due to the water released upon binding, while the net exothermic effect originates from the anion-NH3+ pair formation. Moreover, the results reveal that the nature of the cation has little effect on the thermodynamics of the anion-lysozyme association under the given experimental conditions. Taken together, it seems that the observed thermodynamics of association is a result of a combination of both electrostatic and short-range interactions. The anion ordering reflects the strength of water mediated interactions between anions and lysozyme.
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PMID:Thermodynamics of the lysozyme--salt interaction from calorimetric titrations. 2021 69


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