Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.5.1.5 (urease)
7,257 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The authors compared three urea nitrogen methods using six instruments: (1) the diacetyl monoxime method used with a continuous flow analyzer Sequential Multiple Analyzer Model 4 + 2; (2) the diacetyl monoxime method used with an older continuous flow analyzer (Sequential Multiple Analyzer Model 6/60; (3) the diacetyl monoxime method used with a third continuous flow system, AutoAnalyzer Model I; (4) the urease-conductivity method performed on the Beckman System I; (5) the urease-glutamate dehydrogenase method performed on the DuPont Automatic Clinical Analyzer; (6) the urease-glutamate dehydrogenase method done on a centrifugal analyzer, CentrifiChem. We evaluated each method for the following: (1) within-run precision; (2) between-day precision; (3) linearity of the relationship between concentration and instrument output; (4) specificity; (5) carry-over; (6) comparison of urea nitrogen values for samples from patients.
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PMID:Evaluation of three methods for the measurement of urea nitrogen in serum as used on six instruments. 736 15

The nitrogen excretory metabolism of the myxomycete Physarum polycephalum was studied. When cultured in partially defined broth medium or on agar, the principal excretory product was ammonia nitrogen. A small, variable quantity of urea was excreted in liquid culture. No uric acid or other purines were detected in the cultures. When microplasmodia were incubated with sodium [14C]bicarbonate, radioisotope was incorporated into citrulline, arginine, and urea. Incubation with L-[carbamoyl-14C]citrulline yielded labelled arginine, urea, and CO2. Substantial urease activity was found in extracts of the microplasmodia. These results, in conjunction with the lack of an absolute nutritional requirement for arginine, provide evidence that Physarum has a functional arginine biosynthetic pathway, an arginase, and a urease.
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PMID:Arginine synthesis and nitrogen excretion in the myxomycete Physarum polycephalum. 737 43

Mycobacterium tuberculosis urease (urea amidohydrolase [EC 3.5.1.5]) was purified and shown to contain three subunits: two small subunits, each approximately 11,000 Da, and a large subunit of 62,000 Da. The N-terminal sequences of the three subunits were homologous to those of the A, B, and C subunits, respectively, of other bacterial ureases. M. tuberculosis urease was specific for urea, with a Km of 0.3 mM, and did not hydrolyze thiourea, hydroxyurea, arginine, or asparagine. The enzyme was active over a broad pH range (optimal activity at pH 7.2) and was remarkably stable against heating to 60 degrees C and resistant to denaturation with urea. The enzyme was not inhibited by 1 mM EDTA but was inhibited by N-ethylmaleimide, hydroxyurea, acetohydroxamate, and phenylphosphorodiamidate. Urease activity was readily detectable in M. tuberculosis growing in nitrogen-rich broth, but expression increased 10-fold upon nitrogen deprivation, which is consistent with a role for the enzyme in nitrogen acquisition by the bacterium. The gene cluster encoding urease was shown to have organizational similarities to urease gene clusters of other bacteria. The nucleotide sequence of the M. tuberculosis urease gene cluster revealed open reading frames corresponding to the urease A, B, and C subunits, as well as to the urease accessory molecules F and G.
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PMID:Purification, characterization, and genetic analysis of Mycobacterium tuberculosis urease, a potentially critical determinant of host-pathogen interaction. 755 54

Urease (urea amidohydrolase; EC 3.5.1.5) catalyzes the hydrolysis of urea to yield ammonia and carbamate. The latter compound spontaneously decomposes to yield another molecule of ammonia and carbonic acid. The urease phenotype is widely distributed across the bacterial kingdom, and the gene clusters encoding this enzyme have been cloned from numerous bacterial species. The complete nucleotide sequence, ranging from 5.15 to 6.45 kb, has been determined for five species including Bacillus sp. strain TB-90, Klebsiella aerogenes, Proteus mirabilis, Helicobacter pylori, and Yersinia enterocolitica. Sequences for selected genes have been determined for at least 10 other bacterial species and the jack bean enzyme. Urease synthesis can be nitrogen regulated, urea inducible, or constitutive. The crystal structure of the K. aerogenes enzyme has been determined. When combined with chemical modification studies, biophysical and spectroscopic analyses, site-directed mutagenesis results, and kinetic inhibition experiments, the structure provides important insight into the mechanism of catalysis. Synthesis of active enzyme requires incorporation of both carbon dioxide and nickel ions into the protein. Accessory genes have been shown to be required for activation of urease apoprotein, and roles for the accessory proteins in metallocenter assembly have been proposed. Urease is central to the virulence of P. mirabilis and H. pylori. Urea hydrolysis by P. mirabilis in the urinary tract leads directly to urolithiasis (stone formation) and contributes to the development of acute pyelonephritis. The urease of H. pylori is necessary for colonization of the gastric mucosa in experimental animal models of gastritis and serves as the major antigen and diagnostic marker for gastritis and peptic ulcer disease in humans. In addition, the urease of Y. enterocolitica has been implicated as an arthritogenic factor in the development of infection-induced reactive arthritis. The significant progress in our understanding of the molecular biology of microbial ureases is reviewed.
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PMID:Molecular biology of microbial ureases. 756 14

Proteus mirabilis urease catalyzes the hydrolysis of urea, initiating the formation of urinary stones. The enzyme is critical for kidney colonization and the development of acute pyelonephritis. Urease is induced by urea and is not controlled by the nitrogen regulatory system (ntr) or catabolite repression. Purified whole-cell RNA from induced and uninduced cultures of P. mirabilis and Escherichia coli harboring cloned urease sequences was probed with a 4.2-kb BglI fragment from within the urease operon. Autoradiographs of slot blots demonstrated 4.2- and 5.8-fold increases, respectively, in urease-specific RNA upon induction with urea. Structural and accessory genes necessary for urease activity, ureD, A, B, C, E, and F, were previously cloned and sequenced (B. D. Jones and H. L. T. Mobley, J. Bacteriol. 171:6414-6422, 1989). A 1.2-kb EcoRV-BamHI restriction fragment upstream of these sequences confers inducibility upon the operon in trans. Nucleotide sequencing of this fragment revealed a single open reading frame of 882 nucleotides, designated ureR, which is transcribed in the direction opposite that of the urease structural and accessory genes and encodes a 293-amino-acid polypeptide predicted to be 33,415 Da in size. Autoradiographs of sodium dodecyl sulfate-polyacrylamide gels of [35S]methionine-labeled polypeptides obtained by in vitro transcription-translation of the PCR fragments carrying only ureR yielded a single band with an apparent molecular size of 32 kDa. Fragments carrying an in-frame deletion within ureR synthesized a truncated product. The predicted UreR amino acid sequence contains a potential helix-turn-helix motif and an associated AraC family signature and is similar to that predicted for a number of DNA-binding proteins, including E. coli proteins that regulate acid phosphatase synthesis (AppY), porin synthesis (EnvY), and rhamnose utilization (RhaR). These data suggest that UreR governs the inducibility of P. mirabilis urease.
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PMID:Proteus mirabilis urease: transcriptional regulation by UreR. 767 44

Bacillus fastidiosus was cultivated in batch and continuous culture on various carbon and nitrogen sources. The enzymes involved in allantoin degradation (allantoinase, urease, carboligase) of B. fastidiosus were hardly affected by either carbon or nitrogen source. In contrast, the enzymes involved in glycerol utilization (glycerol kinase, glycerol 3-phosphate dehydrogenase) were induced during growth on glycerol, but were not affected by the amount of allantoin present.
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PMID:The level of enzymes involved in the allantoin metabolism of Bacillus fastidiosus grown under different conditions. 776 82

In Arabidopsis thaliana, urease transcript levels increased sharply between 2 and 4 d after germination (DAG) and were maintained at maximal levels until at least 8 DAG. Seed urease specific activity declined upon germination but began to increase in seedlings 2 DAG, reaching approximately 75% of seed activity by 8 DAG. Urea levels showed a small transient increase 1 DAG and then approximately paralleled urease activity, reaching maximal levels at approximately 9 DAG. Urease inhibition with phenylphosphorodiamidate resulted in a 2- to 4-fold increase in urea levels throughout seedling development. Arginine pools (0-8 DAG) changed approximately in parallel with the urea pool. Consistent with arginine being a major source of urea, arginase activity increased 10-fold in the interval 0 to 6 DAG. Allopurinol, a xanthine dehydrogenase inhibitor, had no effect on urea levels up to 3 DAG but reduced the urea pool by 30 to 40% during the interval 5 to 8 DAG, suggesting that purine degradation contributed to the urea pool well after germination, if at all. in aged Arabidopsis seeds, there was correlation between phenylphosphorodiamidate inactivation of urease and germination inhibition, the latter overcome by NH4NO3 or amino acids. Since urease activity, urea precursor, and urea increase in young seedlings, and since urease inactivation results in a nitrogen-reversible inhibition of germination, we propose that urease recycles urea-nitrogen in the seedling.
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PMID:Essential role of urease in germination of nitrogen-limited Arabidopsis thaliana seeds. 777 May 20

The nickel metalloenzyme urease catalyses the hydrolysis of urea to ammonia and carbamate, and thus generates the preferred nitrogen source of many organisms. When produced by bacterial pathogens in either the urinary tract or the gastroduodenal region, urease acts as a virulence factor. At both sites of infection urease is known to enhance the survival of the infecting bacteria. Ammonia resulting from the action of urease is believed to increase the pH of the environment to one more favourable for growth, and to injure the surrounding epithelial cells. In addition, in the urinary tract urease activity can result in the formation of urinary calculi. Bacterial urease gene clusters contain from seven to nine genes depending upon the species. These genes encode the urease structural subunits and accessory polypeptides involved in the biosynthesis of the nickel metallocentre. So far, three distinct mechanisms of urease gene expression have been described for ureolytic bacteria. Some species constitutively produce urease; some species produce urease only if urea is present in the growth medium; and some species produce urease only during nitrogen-limiting growth conditions. For either the urea-inducible genes or the nitrogen-regulated genes transcription appears to be positively regulated. In the nitrogen-regulated systems, urease gene expression requires Nac (nitrogen assimilation control), a member of the LysR family of transcriptional activators. Urea dependent expression of urease requires UreR (urease regulator), a member of the AraC family of transcriptional activators. An evolutionary tree for urease genes of eight bacterial species is proposed.
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PMID:Bacterial ureases: structure, regulation of expression and role in pathogenesis. 793 18

Restricted ventilation was used to experimentally induce ascites in commercial male broilers. The role of a dietary urease inhibitor (0, 125, and 250 ppm) and ceiling fans to reduce ascites was investigated. At 6 wk of age, birds were bled, euthanatized, weighed, scored for ascites, and heart, liver, and small intestine weights were obtained. Random samples were analyzed for intestinal ammonia. Blood samples were analyzed for blood gases, hemoglobin, red blood cell count, blood urea nitrogen, ammonia, and uric acid. Birds fed 125 and 250 ppm urease inhibitor were significantly (P < .001) lighter at 6 wk, when compared with controls. Urease inhibitor (125 and 250 ppm) significantly decreased large intestine ammonia. Urease inhibitor significantly increased small intestine (250 ppm) and liver weights (125 and 250 ppm), whereas urease inhibitor at 125 ppm decreased right ventricular heart weight. Urease inhibitor had no effect on ascites scores, blood gases, or blood ammonia, but hemoglobin, blood urea nitrogen, red blood cell count, and uric acid were significantly (P < .05) decreased by 125 ppm urease inhibitor.
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PMID:Effect of a urease inhibitor and ceiling fans on ascites in broilers. 2. Blood variables, ascites scores, and body and organ weights. 807 23

1. The relationship of the decreased caecal urease activity by dietary penicillin to nitrogen utilisation was assessed in chickens fed a low protein diet plus urea. 2. Dietary penicillin at 20 and 100 mg/kg decreased anaerobic bacteria counts, urease activity and ammonia concentration in caecal contents (P < 0.05, except for ammonia in the case of the 100 mg/kg penicillin diet). 3. The 20 mg/kg penicillin diets significantly increased the excretion of urea and total nitrogen (P < 0.05) and decreased ammonia excretion, and significantly reduced nitrogen retention (P < 0.05). The 100 mg/kg penicillin diet also resulted in similar but not significant changes, which tended to be less than those by the 20 mg/kg penicillin diet. 4. Ammonia, urea, glutamine and uric acid concentrations in blood, liver and kidney were unchanged by dietary penicillin. 5. It is concluded that caecal ammonia production from urea was closely correlated with nitrogen utilisation in chickens fed a low protein diet plus urea.
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PMID:Relationship of decreased caecal urease activity by dietary penicillin to nitrogen utilisation in chickens fed on a low protein diet plus urea. 819 93


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