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Disease
Symptom
Drug
Enzyme
Compound
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Enzyme
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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.
...
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
.
...
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.
...
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.
...
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
.
...
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.
...
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.
...
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.
...
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.
...
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.
...
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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