Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:6.3.4.6 (urease)
 7,490 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Proteus mirabilis, a cause of serious urinary tract infection, produces urease, an important virulence factor for this species. The enzyme hydrolyzes urea to CO2 and NH3, which initiates struvite or apatite stone formation. Genes encoding urease were localized on a P. mirabilis chromosomal DNA gene bank clone in Escherichia coli by deletion analysis, subcloning, Bal31 nuclease digestion, transposon Tn5 mutagenesis, and in vitro transcription-translation. A region of DNA between 4.0 and 5.4 kilobases (kb) in length was necessary for urease activity and was located within an 18.5-kb EcoRI fragment. The operon was induced by urea and encoded a multimeric, cytoplasmic enzyme comprising subunit polypeptides of 8,000, 10,000, and 73,000 daltons that were encoded by a single polycistronic mRNA and transcribed in that order. Seventeen urease-negative transposon insertions were isolated that synthesized either none of the structural subunit polypeptides, the 8,000-dalton polypeptide alone, or both the 8,000- and 10,000-dalton subunit polypeptides. The molecular weight of the native enzyme was estimated to be 212,000 by Superose-6 chromatography. Homologous sequences encoding the urease of Providencia stuartii synthesized subunit polypeptides of similar sizes and showed a similar genetic arrangement. However, restriction maps of the operons from the two species were distinct, indicating significant divergence.
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PMID:Proteus mirabilis urease: genetic organization, regulation, and expression of structural genes. 284 Dec 83

We studied the biochemical properties of the urease of Staphylococcus saprophyticus and the possible role of the urease in experimental urinary tract infections. For this purpose, the nonhemagglutinating and nonadherent strain 9325, which was isolated from a case of symptomatic urinary tract infection, was used. The urease was shown to have a Km of 6.64 mM urea and a Vmax of 4.59 mumol NH3.min-1.mg-1. The enzyme was inhibited by acetohydroxamic acid in a noncompetitive manner. By means of Sephacryl S-300 column chromatography, we determined a mean molecular weight (+/- standard error of the mean) of 420,000 +/- 16,000. To assess the contribution of S. saprophyticus urease to uropathogenicity, a urease-negative mutant was constructed by nitrosoguanidine mutagenesis. In the rat model of ascending unobstructed urinary tract infection, higher numbers of CFU.gram of tissue-1 and more-severe lesions were detected with the parent strain. Moreover, bladder stones were found in animals infected with the urease-positive strain only. Interestingly, the difference in mean bacterial counts of the bladders was found to be significant by the Wilcoxon two-sample test (P less than 0.05), whereas that between the kidney bacterial counts was not. Immunoblot studies revealed a faint antibody response in rats infected with the mutant strain, although bacteria could still be detected in the kidneys after 7 days. Sera of animals challenged with the parent strain reacted strongly with many antigens of S. saprophyticus. Our data indicate that urease is a major factor for invasiveness of S. saprophyticus, especially in the tissue of the bladder, whereas persistence in the urinary tract and nephropathogenicity of this organism are governed by factors other than urease.
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PMID:Staphylococcus saprophyticus urease: characterization and contribution to uropathogenicity in unobstructed urinary tract infection of rats. 290 83

The origin of ureolytic activity in artificial-mouth plaques was established by assessing the contribution to plaque ureolytic activity of the isolated bacteria. To overcome losses of ureolytic activity caused by the unstable presence of urease in oral bacteria, ureolytic bacteria were isolated from an exceptionally active plaque (1 mumol NH3/min per mg protein) in which 63 per cent of the flora was ureolytic. After their ability to metabolize urea was stabilized, 13 ureolytic bacteria remained: seven strains of Streptococcus salivarius, one Streptococcus bovis, two Staphylococcus epidermidis and three Staphylococcus haemolyticus. Their urease activity, measured after growth into stationary phase, was reproducible and strain specific with a 20-fold range within each genus. The mean ureolytic activity of each species, when weighted by its calculated incidence in the original plaque, accounted for 40 per cent of the total plaque ureolytic activity. However, these values for urease levels were only a small fraction of the bacterial ureolytic potential. Urease per mg cell protein measured during the growth cycle of a selected Strep. salivarius, and Staph. epidermidis, varied 10-fold, and reached much higher activities (i.e. 6-8 mumol NH3/min per mg of cell protein) than under the growth conditions that were used to assess the contribution of these species to total plaque ureolysis. Thus urea metabolism in artificial plaque was due mainly to Strep. salivarius, with a small contribution from Staph. epidermidis. The presence of further unidentified species of ureolytic oral bacteria need not be invoked.
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PMID:The bacteria responsible for ureolysis in artificial dental plaque. 307 50

The detrimental effects of excessive Ni on plant growth have been well known for many years. More recent evidence indicates that Ni is required in small amounts for normal plant growth and development. Ni is an essential component of urease in plants and microorganisms. A deficiency of Ni in plants is reported to result in necrotic lesions in leaves in response to toxic accumulations of urea. Urease plays an essential role in mobilization of nitrogenous compounds in plants, a process that is especially important during seed germination and fruit formation when protein reserves are degraded into amino acids. Arginine, an abundant amino acid in plants, when degraded produces urea as a product and urease is needed for urea utilization. Theories of urea formation during allantoin degradation in Glycine max have been recently refuted. In G. max ureides apparently are metabolized via an amidohydrolase reaction with subsequent degradation of ureidoglycine, yielding glyoxylate, NH+4 and CO2. No evidence is available for the formation of urea in this pathway. Nitrogen-fixing symbionts, such as Rhizobium and Bradyrhizobium, contain two known Ni enzymes: urease and hydrogenase. Optimum growth of nodulated legumes and actinorhizal plants may depend on an adequate supply of Ni to meet the requirements of the Ni-requiring enzymes in host plants and endophytes. The seeds of severely Ni-deficient Hordeum are completely inviable, thus providing conclusive evidence for the essentiality of Ni for this species. The evidence indicates that Ni must be added to the list of micronutrient elements generally required by plants.
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PMID:Nickel as a micronutrient element for plants. 307 27

Relative deficiencies of ornithine or arginine occur in the presence of excessive ammonia, excessive lysine, growth, pregnancy, trauma, or protein deficiency and malnutrition. Ammonia excess may occur in the presence of a normal liver when amino acid mixtures lacking ornithine, arginine, or citrulline are infused; when specific amino acids such as glycine are injected; when ammonium salts, urea, or urease are injected; or when the gastrointestinal tract contains an excess of protein, urea, or NH4+, as occurs after a gastrointestinal hemorrhage. In these states, ornithine is often rate-limiting for urea cycle function. Ornithine is also rate-limiting when ammonia excess occurs in the presence of hepatic failure. In three of the inherited urea cycle disorders, ornithine insufficiency and ammonia excess also occur. These disorders are citrullinemia, argininosuccinic aciduria, and argininemia. In the presence of excessive lysine the availability of arginine is reduced and the formation of ornithine is decreased in the liver; urea synthesis is reduced, but orotic acid synthesis is increased, and orotic aciduria results as carbamyl phosphate is directed toward the pyrimidine pathway. Hereditary lysinuric protein intolerance results in ornithine depletion, hyperammonemia, and orotic acid uria. Optimal growth in several species of animals requires 0.4-1.0% arginine in the diet. Diets deficient in arginine are associated with poor wound healing as well as stunted growth. The measurement of orotic acid excretion has been a convenient indicator of insufficiency of ornithine or arginine during growth or pregnancy in animals and should prove useful in assessing the requirement for arginine after trauma. Normal human pregnancy is associated with low-grade orotic aciduria. Protein deficiency and malnutrition increase the vulnerability of the animal or child to ammonia toxicity. This is presumably due to insufficient ornithine for normal urea cycle responsiveness.
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PMID:Conditional deficiencies of ornithine or arginine. 308 83

The urease from Ureaplasma urealyticum strain T 960 was isolated by the use of affinity chromatography, hydrophobic chromatography and gel filtration. The enzyme was purified by a factor of 155. The urease appeared as a single band of molecular weight (MW) 75,000 using reducing conditions in SDS-polyacrylamide gel electrophoresis. By gel filtration the native MW was determined to be 150,000. Isoelectric focusing showed the presence of two closely migrating enzyme species with a pI of pH 5.1-5.2. These findings show multiple forms of the urease and that these forms are composed of subunits. The electrophoresis experiments also indicate that this enzyme is a major component of the cytoplasm of U. urealyticum. The Km of the purified enzyme was 4.5 mM urea and the specific activity was 33530 mumoles NH3 x min-1 x mg-1. The optimum pH was pH 7-7.5. The urease activity was inhibited by flurofamide, acetohydroxamic acid, N-ethylmaleimide and p-chloromercuribenzoate but not by iodoacetate.
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PMID:Purification and characterization of urease from Ureaplasma urealyticum. 319 54

Campylobacter pylori, a suspected agent of gastritis and peptic ulceration, rapidly hydrolyzes urea. Because urease serves as the basis of detection of the organism in gastric biopsies and may represent an important virulence factor, biochemical characteristics of the enzyme were determined. C. pylori was isolated from antral biopsies from 10 patients with complaints of abdominal pain or history of peptic ulcer disease. All isolates were urease positive, with an average rate of hydrolysis by cell lysates being 36 +/- 28 mumol of NH3 per min per mg of protein, more than twice that of Proteus mirabilis and 10 times that of other urinary tract isolates. The enzyme had an apparent molecular weight of 625,000 +/- 15,000 by column chromatography, an isoelectric point of 5.9, a Km of 0.8 +/- 0.1 mM urea, an optimal temperature of 45 degrees C, and an optimal pH of 8.2. Ten isolates tested produced ureases with identical electrophoretic mobilities on nondenaturing 5% polyacrylamide activity gels. Acetohydroxamic acid (100 micrograms/ml), hydroxyurea (85 micrograms/ml), flurofamide (0.05 micrograms/ml), and EDTA (8 mM) inhibited enzyme activity by 50%. Cell lysates retained 50% of initial urease activity after 6 days and 40% activity after 18 days when stored at 4 degrees C in 20 mM sodium phosphate, pH 6.8. At -70 degrees C for 18 days, 1 mM EDTA or 15% glycerol preserved 40 or 34%, respectively, of initial activity. The urease of C. pylori appears to be biochemically unique from the enzymes of other common urease-producing species.
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PMID:Characterization of urease from Campylobacter pylori. 338 8

Ten strains of Proteus penneri isolated from geographically diverse laboratories were tested for urease activity. Cell lysates from urea-induced cells had a mean activity of 4.9 +/- 4.1 mumol of NH3 per min per mg of protein. On nondenaturing 6% polyacrylamide activity gels, the enzymes of P. penneri had very similar electrophoretic mobilities within species and within the Proteus genus but were distinct from the ureases of Providencia and Morganella species. On lower-percentage polyacrylamide, differences in mobilities of the ureases could be detected between the Proteus species. From representative strains, the P. penneri urease was found to be inducible by growth in urea and had an apparent molecular weight of 246,000 +/- 9,000, an isoelectric point of 5.1, and a Km for urea of 14 mM and was inhibitable by acetohydroxamic acid, hydroxyurea, and EDTA. In an in vitro model of struvite formation, a P. penneri strain produced abundant crystals on a glass rod submerged in synthetic urine in the absence but not presence of acetohydroxamic acid (500 micrograms/ml).
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PMID:Urease activity of Proteus penneri. 342 22

Artificial cells containing leucine dehydrogenase (EC 1.4.1.9), alcohol dehydrogenase (EC 1.1.1.1; or glucose dehydrogenase, EC 1.1.1.47; or lactic dehydrogenase, EC 1.1.1.27; or malic dehydrogenase, EC 1.1.1.37), urease (EC 3.5.1.5) and dextran-NAD+ were prepared. Ammonia or urea could be converted into L-leucine, L-valine and L-isoleucine using artificial cells with four different multienzyme systems.
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PMID:Conversion of urea or ammonia into essential amino acids (L-leucine, L-valine, and L-isoleucine) using multienzyme systems and NADH-dextran immobilised in artificial cells. 344 45

Two experiments were conducted with growing male rats to determine the effects of 120 ppm of dietary sarsaponin (S) on nitrogen (N) metabolism when urea or protein are added to the diet. Growth, feed efficiency, N digestibility and balance, urinary N and ammonia-N (NH3-N), and cecal urease and NH3-N were measured. Growth and feed utilization were unaffected by dietary S. Adding urea or protein to the diet increased apparent N digestibility and increased urinary-N excretion. Urea did not affect N balance, whereas growth, feed utilization and N balance were maximized with 22% compared with either 16 or 28% dietary protein. Urinary NH3-N excretion was decreased by S when urea was added to the diet but was not affected when fed with increasing dietary protein. Cecal urease was decreased by S when urea was added or when the protein level was increased in the diet; effects on cecal NH3-N varied between the two experiments. Plasma urea-N was decreased by S. It is concluded that S has minor effects on N metabolism in rats and that NH3-N formation or excretion is only marginally affected by dietary S. If S decreases NH3-N level in confinement facilities, it is concluded that the effect is after the waste material is excreted by the animal, perhaps through reduced urease activity.
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PMID:Influence of sarsaponin on growth, feed and nitrogen utilization in growing male rats fed diets with added urea or protein. 362 98


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