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)

The regulation of the synthesis of the enzyme urease (urea amido hydrolase E.C. 3.5.1.5.) in Neurospora crassa was investigated. The biosynthesis of urease is repressed by ammonium ions. Under ammonium excess conditions the specific activity of urease decreases from 0.980 to 0.180 mumoles NH3/min/mg protein. By addition of cycloheximide it was shown that ammonia influences the synthesis of this enzyme. Enzyme induction by the substrate could be excluded. Even under the conditions of highest repression a specific activity of urease of 0.180 mumoles NH3/min/mg protein was measured. Possible causes of this constitutive enzyme level are discussed.
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PMID:[Repression of urease biosynthesis in Neurospora crassa by ammonium ions]. 12 30

Urease activity, expressed as mg N-NH3/g dry weight per 30 min at 25 degrees C, was determined in the various parts of the sheep, chicken and pig digestive apparatus. The results were as follows. Sheep: contents--rumen 1.25"/-0.09, reticulum 0.78+/-0.02, omasum 0.44+/-0.02, abomasum 0.002+/-0.001, duodenum 0.003+/-0.001, jejunum 0.18+/-0.03, ileum 0.42+/-0.03, caecum 1.34+/-0.11, colon 0.76+/-0.08, walls-rumen 0.88+/-0.16, reticulum 0.38+/-0.04, omasum 0.11+/-0.02, abomasum 0.01+/-0.002, ileum 0.092+/-0.01, caecum 0.14+/-0.03, colon 0.16+/-0.02. Chicken: contents--jejunum 0.028+/-0.009, ileum 0.043+/-0.013, caecum 0.17+/-0.03, colon and cloaca 0.04+/-0.013. Pigs: contents--jejunum 0.02+/-0.01, ileum 0.14+/-0.08, caecum 0.62+-0.12, colon 0.43+/-0.06. No urease activity was found in the walls of the digestive apparatus or the contents of the duodenum in chickens, or in the walls of the stomach and intestine and the contents of the duodenum in pigs. The results show that urease activity in the digestive apparatus of pigs and poultry is lower than in sheep. Inadequate urease activity in the digestive apparatus explains why chickens and pigs are significantly less capable than ruminants of utilizing urea nitrogen as a substitute for some of the protein in the diet.
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PMID:Urease activity in the contents and tissues of the sheep, pig and chicken gastrointestinal apparatus. 16 May 76

By counting the volatile molecules produced by an immobilized-enzyme catalyzed reaction which is interfaced to a mass spectrometer via a semi-permeable membrane, a general approach to biochemical measurement and detection is obtained which offers the potential of high sensitivity, specificity and speed. In combination with molecule microscopy, this method should allow, for example, a mapping of suitable enzyme distributions in non-stained and non-fixed tissue slices. Immobilized urease (urea amidohyrdrolase, EC 3.5.1.5) was used to assay urea using CO2 as the volatile product, and alcohol dehydrogenase (alcohol:NAD+ oxidoreductase, EC 1.1.1.1) was used to assay NADH using ethanol as the volatile product.
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PMID:Biochemical assay by immobilized enzymes and a mass spectrometer. 18 Oct 86

1. Urease from a sea urchin Lytechinus variegatus, was purified 300-fold, using heat precipitation, ethanol precipitation and gel filtration. 2. The pH optimum is 8.0. 3. The apparent Michaelis constant for urea is 0.13 mM at pH 8.0. 4. The inhibitory effects of seven reagents on urease were evaluated. The pattern of inhibition is similar to other invertebrate ureases. 5. L. variegatus urease is compared with that of several other invertebrates, and its possible significance in CaCO3 formation is discussed.
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PMID:Urease from a sea urchin Lytechinus variegatus: partial purification and kinetics. 31 93

A rapid, miniaturized, urea broth test useful for detecting urease activity of yeasts was compared to Christensen urea agar. All urease-producing yeasts tested were positive on both media; however, 60% were reactive in the urea R broth within 30 min, and the remainder were reactive within 4 h. This urea multiwell test may be useful as a rapid screening method for detecting urease-producing yeasts recovered from clinical specimens and as an adjunct test with other rapid methods of yeast identification.
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PMID:Rapid urea broth test for yeasts. 35 68

Uninduced cultures of Saccharomyces cerevisiae exhibit high basal levels of allantoinase, allantoicase, and ureidoglycolate hydrolase, the enzymes responsible for degrading allantoin to urea. As a result, these activities increase only 4- to 8-fold upon induction, whereas the urea-degrading enzymes, urea carboxylase and allophanate hydrolase, have very low basal levels and routinely increase 30-fold on induction. Differences in the inducibility of these five enzymes were somewhat surprising because they are all part of the same pathway and have the same inducer, allophanate. Our current studies reconcile these observations. S. cerevisiae normally contained up to 1 mM allantoin sequestered in a cellular organelle, most likely the vacuole. Separation of the large amounts of allantoin and the enzymes that degrade it provide the cell with an efficient nitrogen reserve. On starvation, sequestered allantoin likely becomes accessible to these degradative enzymes. Because they are already present at high levels, the fact that their inducer is considerably removed from the input allantoin is of little consequence. This suggests that at times metabolite compartmentation may play an equal role with enzyme induction in the regulation of allantoin metabolism. Metabolism of arginine, another sequestered metabolite, must be controlled both by induction of arginase and compartmentation because arginine serves both as a reserve nitrogen source and a precursor of protein synthesis. The latter function precludes the existence of high basal levels of arginase.
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PMID:Metabolite compartmentation in Saccharomyces cerevisiae. 35 30

In order to improve the isolation and identification of yeasts in a cancer research hospital, a protocol was developed utilizing an improved blood culture methodology and a four-test schema for rapid yeast identification. The blood culturing technique, based upon centrifugation, has shown a ten-fold increase in isolation of fungi from blood and has provided for: quantitation or organisms, unlimited selection of media and atmospheres for primary culturing, and a 1:200 dilution of microorganisms away from serum antimicrobial factors and antibiotics. The four-test schema, which may be adapted for the identification of any unknown yeast in pure culture, consists of a dye pour plate auxanogram (DPPA), Tween 80-Oxgall-Caffeic acid (TOC), a rapid nitrate-reductase test (swab test) and Urea 'R' Broth. Using this protocol, over 95% of the clinical isolates received were correctly identified within 24 hours and 100% by 48 hours. By using DPPA, a 14 sugar assimilation pattern for each isolate was determined within 12 to 16 hours; and in some cases, as little as 6 hours. Growth on TOC yielded one of the following results: (1) Candida albicans and Candida stellatoidea sequentially produced germ tubes and chlamydospores in 3 hours and 24 hours, respectively; (2) Cryptococcus neoformans produced a brown pigment specific for its identification in 12 hours or less. The swab test gave results on nitrate utilization in less than 15 minutes and urease was detected within 4 hours.
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PMID:Isolation and rapid identification of yeasts from compromised hosts. 37 Jun

The Micro-ID system for rapid (4 h) identification of Enterobacteriaceae was evaluated by testing 433 enteric bacilli and 9 other gram-negative bacilli. Each isolate was identified with conventional tubed media and was also tested in the Micro-ID and API 20E systems. The overall accuracy of both systems was 97%. Micro-ID tests for the Voges-Proskauer reaction, indole and H2S production, and ornithine and lysine decarboxylase all demonstrated a 97 to 99% correlation with conventional methods. Only 86% of the Micro-ID urease tests agreed with Christenson urea agar. Two inoculum densities were tested in Micro-ID panels, with 157 stock cultures. Over 90% of the tests were unaffected by changes in inoculum density. Tests with four control strains suggested that the Micro-ID system was more reproducible when a light inoculum was used. The Micro-ID system was found to be a very convenient method for rapid, accurate, and precise identification of the Enterobacteriaceae.
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PMID:Rapid identification of Enterobacteriaceae with the micro-ID system versus API 20E and conventional media. 38 17

Urinary stones form as a consequence of urinary supersaturation. Supersaturation occurs as a result of elevated concentrations of urinary solutes. Dietary, metabolic, endocrine, hereditary, and infectious processes alter urinary solute concentrations. Struvite (MgNH4PO. 6H2O) and carbonate-apatite [Ca10(PO4)6CO3] stones form in urine that becomes supersaturated as a by-product of the hydrolysis of urea by the bacterial enzyme urease. Urease-induced stones manifest primarily as branched renal calculi and as bladder calculi. Conventional therapy has usually consisted of surgical removal of the stone combined with a short course of antimicrobial therapy. Such treatment is curative in about 50% of cases. Recurrent stone formation and progressive pyelonephritis occur in those who are not cured. Adjunctive medical treatment with acetohydroxamic acid or hydroxyurea lessens the risk of calculogenesis and decreases growth of residual stones in patients who are not cured by conventional therapy. Patients with urea-splitting urinary infection and renal stones have a major life-threatening disease. The morbidity and expense that result from this disease are great. Long-term (perhaps lifetime) chemotherapy with antimicrobial agents and/or urease-inhibiting drugs combined with judicious and expert surgical intervention can be expected to significantly improve the plight of these unfortunate patients.
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PMID:Urease stones. 38 98

Pseudomonas aeruginosa AI 3 was able to grow in medium containing acetanilide (N-phenylacetamide) as a carbon source when NH4+ was the nitrogen source but not when urea was the nitrogen source. AIU mutants isolated from strain AI 3 grew on either medium. Urease levels in bacteria grown in the presence of urea were 10-fold lower when NH4+ or acetanilide was also in the medium, but there were no apparent differences in urease or its synthesis between strain AI 3 and mutant AIU 1N. The first metabolic step in the acetanilide utlization is catalyzed by an amidase. Amidases in several AIU strains showed altered physiochemical properties. Urea inhibited amidase in a time-dependent reaction, but the rates of the inhibitory reaction with amidases from the AIU mutants were slower than with AI 3 amidase. The purified amidase from AIU 1N showed a marked difference in its pH/activity profile from that obtained with purified AI 3 amidase. These observations indicate that the ability of strain AIU 1N and the other mutants to grow on acetanilide/urea medium is associated with a mutation in the amidase structural gene; this was confirmed for strain AIU 1N by transduction.
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PMID:Pseudomonas aeruginosa mutants resistant to urea inhibition of growth on acetanilide. 41 Jul 88


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