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)

Urease (urea amidohydrolase, EC 3.5.1.5) was extracted from the mixed rumen bacterial fraction of bovine rumen contents and purified 60-fold by (NH4)2SO4 precipitation, calcium phosphate-gel adsorption and chromatography on hydroxyapatite. The purified enzyme had maximum activity at pH 8.0. The molecular weight was estimated to be 120000-130000. The Km for urea was 8.3 X 10(-4) M+/-1.7 X 10(-4) M. The maximum velocity was 3.2+/-0.25 mmol of urea hydrolysed/h per mg of protein. The enzyme was stabilized by 50 mM-dithiothreitol. The enzyme was not inhibited by high concentrations of EDTA or phosphate but was inhibited by Mn2+, Mg2+, Ba2+, Hg2+, Cu2+, Zn2+, Cd2+, Ni2+ and Co2+. p-Chloromercuribenzenesulfphonate and N-ethylmaleimide inhibited the enzyme almost completely at 0.1 mM. Hydroxyurea and acetohydroxamate reversibly inhibited the enzyme. Polyacrylamide-gel electrophoresis showed that the mixed rumen bacteria produce ureases which have identical molecular weights and electrophoretic mobility. No multiple forms of urease were detected.
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PMID:Purification and properties of urease from bovine rumen. 1 37

The role of Corynebacterium renale urease in the establishment of pyelonephritis was studied by the oral administration of acetohydroxamic acid (AHA), a urease inhibitor, to experimentally infected rats. The bacteria were introduced by surgical insertion of a zinc disc containing 1 X 10(6) colony-forming units of C-renale into the urinary bladder whereas sterile discs were implanted in the bladders of the control animals. Daily administration of AHA via the drinking water did not halt the development of pyelonephritis. Larger doses, given by gavage, did accomplish this goal; that is, the pH of the urine was lowered, the number of colony-forming units of C. renale in the kidney was reduced drastically, and pyelonephritic lesions were observed in the kidney by light-microscopic examination. All experimental rats developed cystitis in varying degrees of severity. About 70% of the intact AHA given by gavage was excreted in the urine 24 h after administration of this compound. Rats implanted with a urease-negative mutant of C. renale displayed no signs of pyelonephritis but did develop cystitis.
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PMID:Influence of acetohydroxamic acid on experimental Corynebacterium renale pyelonephritis. 2 38

The role of urease in induction of pyelonephritis was studied by treatment of proteus-infected rats with acetohydroxamic acid, a potent inhibitor of urease. Infection was produced by introduction of Proteus mirabilis into the bladder along with a zinc disk. Controls were treated identically but received no acetohydroxamic acid. The number of bacteria per milliliter of urine was the same in both groups. The number of bacteria in the kidneys and the extent of renal damage was much greater in controls. Common enterobacteraceal antigen was not detected in the renal parenchyma of rats treated with acetohydroxamic acid. Treatment with acetohydroxamic acid thus prevented invasion of and damage to kidney tissue without reduction of urinary infection. Thus new evidence was found that the invasive properties of Proteus in the urinary tract are dependent on alkalinization of urine by urease and the resulting damage to the renal epithelium.
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PMID:Role of urease in pyelonephritis resulting from urinary tract infection with Proteus. 23 93

Papain (EC 3.4.22.2) has been coupled to supports of titanium (IV) oxide and cellulose, which are particulate and pre-coated with diazotised 1,3-diaminobenzene, giving water-insoluble and stable derivatives which possess low proteolytic activity but high esterolytic activity. In addition the reversible binding of zinc (II) at the active site of papain has been exploited to inhibit protectively the enzyme during its linkage to the aforementioned supports, thereby yielding water-insoluble derivatives of papain having superior activity upon reactivation with EDTA. Application of the improved procedure of enzyme coupling to macroporous cellulose particles gave a water-insoluble derivative of papain having further enhanced proteolytic activity. Other properties of the water-insoluble derivatives of papain and of similarly prepared water-insoluble conjugates of urease (EC 3.5.1.5) and cholinesterase (EC 3.1.1.8) with cellulose are also reported.
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PMID:Active water-insoluble derivatives of papain and other enzymes based on preformed diazonium-type supports. 40 36

Zinc reduced and citrate promoted the urease-induced pH increase in synthetic urine. Secondary to this, the precipitation of magnesium ammonium phosphate and calcium phosphate was influenced. Independent of this pH-related effect, zinc also increased the precipitation of magnesium ammonium phosphate and decreased the calcium phosphate precipitation. These observations were not totally reproducable in human urine.
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PMID:The influence of zinc and citrate on urease-induced urine crystallisation. 274 46

Thirty male calves were used in a 2 X 3 factorial arrangement of treatments to determine the effects of dietary nickel and protein on performance, urease activity and tissue concentrations of nickel, iron, zinc, copper and manganese. Protein levels evaluated were 10.0, 12.25 and 14.5%, and nickel was supplemented at a level of 0 or 5 mg/kg of diet. Nickel did not affect growth during the 140-d study but tended to increase efficiency of gain in calves fed 14.5% protein. Rumen fluid urease activity was increased by nickel only in animals receiving the low protein diet. Urease activity in rumen fluid was higher in calves fed 10.0% than in animals fed 12.25% or 14.5% protein. Neither nickel nor protein affected urease activity in rumen epithelium. Increasing dietary protein resulted in increased urease in cecal digesta. Lung, liver, kidney and serum nickel concentrations were increased by supplemental nickel. A nickel X protein interaction was noted for kidney nickel. Nickel supplementation increased kidney nickel to a greater degree in calves fed 10.0% protein than in calves fed higher protein levels. Nickel supplementation reduced iron concentrations in lung, liver and muscle and manganese concentrations in muscle. Increased dietary protein decreased iron in liver and spleen but increased manganese concentrations in heart. These findings indicate that dietary protein influences responses of ruminants to nickel supplementation and relatively small increases in dietary nickel and protein can influence metabolism of other trace elements.
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PMID:Effects of dietary nickel and protein on growth, nitrogen metabolism and tissue concentrations of nickel, iron, zinc, manganese and copper in calves. 377 17

Growing steers were used in a replicated 3 X 3 Latin square to study the influence of ionophores on mineral metabolism and ruminal urease activity. Treatments consisted of: 1) basal high energy diet; 2) basal plus 33 ppm lasalocid and 3) basal plus 33 ppm monensin. Each period was 33 days and apparent absorption and retention of macrominerals were measured during the last 5 days of each period. Mineral intake during the collection period was not affected by treatment. Both ionophores increased apparent absorption of sodium, magnesium and phosphorus. Retention of magnesium and phosphorus were higher for steers receiving either lasalocid or monensin. Potassium and calcium absorption were not significantly affected by treatment. Serum concentrations of macrominerals were similar for all treatments. Zinc and copper concentrations in serum were higher in animals fed monensin or lasalocid. Steers fed either ionophore had lower concentrations of soluble potassium and calcium in rumen fluid. Both ionophores also decreased ruminal osmolality. Bacterial urease, a nickel-dependent enzyme, was decreased by 28 and 66% in animals that received lasalocid and monensin, respectively. These findings indicate that lasalocid and monensin affect metabolism of certain minerals in ruminants.
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PMID:Influence of monensin and lasalocid on mineral metabolism and ruminal urease activity in steers. 669 34

Day-old pigs were individually fed a low nickel (0.16 ppm) liquid milk-based diet supplemented with either 0, 5 or 25 ppm nickel on a dry matter basis for a 21-day period. At the end of the liquid feeding period, five pigs per treatment were killed, and the remaining five were fed a dried skim milk-based diet (0.12 ppm nickel) with similar levels of added nickel for an additional 28 days. Dietary nickel did not affect animal gain, liver cholesterol, serum protein concentrations or bacterial urease activity in the gastrointestinal tract. The addition of 5 ppm nickel to the basal dry diet reduced ammonia concentrations in the cecum by 33%. Pigs receiving the high level of nickel had decreased serum alkaline phosphatase and increased serum glucose at 49 days, compared to controls. Animals receiving 5 ppm nickel had higher liver iron and zinc concentrations than controls at 21 days but not at 49 days. Control pigs had lower kidney and lung nickel concentrations than animals receiving 5 ppm nickel at 21 days but not at 49 days. Increasing dietary nickel from 5 to 25 ppm resulted in increased concentrations of nickel in serum, kidney, lung, spleen and muscle. These results suggest that 0.12-0.16 ppm nickel is adequate for growth of neonatal pigs fed milk-based diets. However, additional nickel may improve the iron and zinc status of the young pig.
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PMID:Effect of dietary nickel on growth, urease activity, blood parameters and tissue mineral concentrations in the neonatal pig. 672 54

The crystal structure of urease from Klebsiella aerogenes has been determined at 2.2 A resolution and refined to an R factor of 18.2 percent. The enzyme contains four structural domains: three with novel folds playing structural roles, and an (alpha beta)8 barrel domain, which contains the bi-nickel center. The two active site nickels are 3.5 A apart. One nickel ion is coordinated by three ligands (with low occupancy of a fourth ligand) and the second is coordinated by five ligands. A carbamylated lysine provides an oxygen ligand to each nickel, explaining why carbon dioxide is required for the activation of urease apoenzyme. The structure is compatible with a catalytic mechanism whereby urea ligates Ni-1 to complete its tetrahedral coordination and a hydroxide ligand of Ni-2 attacks the carbonyl carbon. A surprisingly high structural similarity between the urease catalytic domain and that of the zinc-dependent adenosine deaminase reveals a remarkable example of active site divergence.
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PMID:The crystal structure of urease from Klebsiella aerogenes. 775 94

Helicobacter pylori is a human gastrointestinal pathogen involved in gastritis, duodenal ulcers, and gastric neoplasia. This microorganism produces large amounts of a urease which, like all known ureases, has nickel in the active site. We have identified a protein in clinical isolates of H. pylori and an identical protein in the ferret pathogen Helicobacter mustelae that strongly binds Ni2+ and Zn2+. This protein has been named Hpn to emphasize its origins in H. pylori and its affinity for nickel. The encoding hpn gene, cloned and expressed in Escherichia coli ER1793, has an open reading frame (180 bp) that specifies a protein with a calculated molecular mass of 7,077 Da and with the same amino-terminal sequence as that of wild-type Hpn. The deduced sequence of Hpn consists of 60 amino acids, of which 28 (47%) are histidines. The hpn gene does not map with the urease gene cluster on the H. pylori chromosome. An Hpn-negative, isogenic H. pylori strain, generated by hpn gene deletion and grown on blood agar, had the same urease activity that wild-type cells did. Thus, the role of Hpn in helicobacters is unknown.
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PMID:Protein Hpn: cloning and characterization of a histidine-rich metal-binding polypeptide in Helicobacter pylori and Helicobacter mustelae. 779 85


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