Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: 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)

Mutants were isolated from Pseudomonas aeruginosa that were impaired in the utilization of a number of nitrogen sources. In contrast to the wild-type strain, these mutants appeared to be unable to derepress the formation of glutamine synthetase and urease under nitrogen-limited growth conditions, whereas NADP-dependent glutamate dehydrogenase became derepressed. This GlnR- phenotype appeared to be caused by a mutation located in the early region of the P. aeruginosa PAO chromosomal map, close to hisIV59. Partial suppression of the GlnR- phenotype due to a mutation located close to hisII4 was observed. These revertants were different from both the wild-type strain and the GlnR- mutant with respect to the regulation of the synthesis of glutamine synthetase, urease, and NADP-dependent glutamate dehydrogenase (GlnRc phenotype). Also the regulation of glutamine synthetase activity by adenylylation/deadenylylation was altered in the revertants. The results suggest the presence of a regulatory gene that plays a role in the regulation of enzyme formation in response to the availability of ammonia.
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PMID:Nitrogen control in Pseudomonas aeruginosa: mutants affected in the synthesis of glutamine synthetase, urease, and NADP-dependent glutamate dehydrogenase. 612 99

Measurement of urinary urea excretion has been suggested as a means of estimating nitrogen balance in hospitalized patients who are malnourished. Because proficiency-testing surveys show gross variations in mean urea as determined by various automated methods and extremely poor precision occasionally, we compared urinary urea measurements and ammonia interference in three widely used methods. The coupled urease/glutamate dehydrogenase method (used in the DuPont aca) showed positive interference from ammonia, as expected; with the diacetylmonoxime (Technicon (12/60) and the urease conductivity (Beckman ASTRA) methods we saw no such interference. Generally, interference by ammonia is less than 10%, but (rarely) it may exceed 25%. However, if urine specimens are properly diluted and potential sources of interference recognized, all three methods appear capable of providing clinically useful data.
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PMID:Urinary urea: are currently available methods adequate for revival of an almost abandoned test? 708 63

The purpose of this paper is to investigate the specific metabolism of the protein and amino acid during pregnancy from a standpoint of urea nitrogen recycling hydrolyzed by intestinal bacterial urease of pregnant rat. For this purpose, the activity of urease of the intestinal flora, and L-glutamate dehydrogenase (GDH) in liver mitochondria, the concentration of free ammonia and urea in the intestinal tract, portal vein and right ventricle of the rat were discussed. The results were: 1) The activity of urease moderately increased during pregnancy with the peak on 19th gestational day. 2) The concentration of free ammonia in the intestinal tract elevated slightly, and markedly elevated in portal vein, but seemed to be no specific change in right ventricle. The peak showed on 19th gestational day. 3) The activity of GDH increased markedly during pregnancy, and the protein synthesis was thought to be accelerated. 4) Urea concentration in intestinal tract and blood stream seemed somewhat increased. This results revealed that the urea recycling system and protein synthesis accelerated during pregnancy because of high urease and GDH activity. This phenomenon adapted the pregnant to nutrient of the fetus for growing and development, and introduced a new concept of maternal-fetal unit of nutrition, especially in protein metabolism.
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PMID:[Studies on entero hepatic circulation of urea nitrogen in pregnant rat (author's transl)]. 724 Aug 47

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

We describe a coupled-enzyme equilibrium method for measuring urea in serum, which is performed on supernates prepared by treating each specimen with Ba(OH)2 and ZnSO4 (Somogyi reagent). Analytical recovery of [14C]urea added to a variety of matrices was essentially complete (mean, 100.6%) for the supernates after precipitation. Nine variables were univariately examined in arriving at the reaction conditions for the method: glutamate dehydrogenase, urease, 2-oxoglutarate, ADP, Tris . HCI, NADH, EDTA, pH, and temperature. The reagent is stable for at least 48 days at--20 degrees C and for 23 days at 4 degrees C. Mean analytical recovery of urea (14 mmol/L) added to seven different specimens (three different matrices) was 100.8%. The analytical linear range of the method extends to 30 mmol of urea per liter. Of 22 potential interferents, only bilirubin at 1 mmol/L (580 mg/L), hemoglobin at 10 g/L, and hydroxyurea at 6 mmol/L showed more than 2% interference. We discuss precision and effects of specimen dilution, and compare results for 100 human serum specimens with those measured for the same specimens with four other urea methods. We examined the effects of measuring a blank, consisting of sample and reagent without urease, with each specimen.
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PMID:A coupled-enzyme equilibrium method for measuring urea in serum: optimization and evaluation of the AACC study group on urea candidate reference method. 737 2

A strategy for the multifunctionalization of the FIA biosensor was developed. The described multifunctional FIA system offers a fast and simple method for the simultaneous determination of ammonia, creatinine, and urea. The hydrolysis of creatinine by creatinine deiminase (CRDI) or of urea by urease forms ammonia, which is amperometrically detected by an oxygen electrode, based on an enzyme conversion system, glutamate dehydrogenase (GLDH)/glutamate oxidase (GLOD). The split of the stream into three after sample injection and confluence before the GLDH reactor resulted in a three-channel system, into which were set three parallel columns, respectively, filled with immobilized CRDI, urease, and CPG. A triple-peak recording was obtained by putting two delay coils at the channels involving CRDI and urease. Thus the interfering of the endogenous ammonia on the creatinine and urea assay is simultaneously compensated. Furthermore, the problem of great difference in concentration between urea and the other two components is resolved by taking advantage of the differentiated dilution effect for each channel caused from the split-stream, flow-injection system. Linear calibration ranges for ammonia, creatinine, and urea were 0.1-5, 0.2-10, and 2-40 mM, respectively. One run was finished within 5 minutes, and the system was reproducibility good (3 to 5%). The results of the urine assay obtained by the present method will be described in the near future.
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PMID:A multifunctional flow-injection biosensor for the simultaneous determination of ammonia, creatinine, and urea. 778 57

A two-step method for assaying creatinine in serum and urine samples, suitable with automated analyzers, is reported. Reagent 1, for the first step, contains a blanking system [creatine amidinohydrolase (CRTase), urease, glutamate dehydrogenase, NADPH, and 2-oxoglutarate] and a NADPH-regenerating system [Mg(2+)-dependent isocitrate dehydrogenase (ICD), MgCl2, and excess isocitrate]. Reagent 2, for the second step, contains the metal-chelating reagent trans-1,2-cyclohexanediamine-N,N,N',N'-tetraacetic acid (CyDTA) and a trigger system [creatinine amidohydrolase (CRNase)]. When a specimen is mixed with reagent 1, all the creatine, urea, and NH3 present are removed by the blanking and NADPH systems. On adding reagent 2, CyDTA inactivates ICD to inhibit the NADPH system. Simultaneously, the creatinine (1 mol) in the specimen is hydrolyzed into creatine by CRNase, and then releases NADP+ (2 mol) through the blanking system. Our optimized method can determine creatinine linearly up to 500 mg/L, with within-day CVs < 1.2% and day-to-day CVs < 2.7%.
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PMID:Enzymatic rate assay of creatinine in serum and urine. 840 98

In Klebsiella aerogenes, the formation of a large number of enzymes responds to the quality and quantity of the nitrogen source provided in the growth medium, and this regulation requires the action of the nitrogen regulatory (NTR) system in every case known. Nitrogen regulation of several operons requires not only the NTR system, but also NAC, the product of the nac gene, raising the question of whether the role of NAC is to activate operons directly or by modifying the specificity of the NTR system. We isolated an insertion of the transposon Tn5tac1 which puts nac gene expression under the control of the IPTG-inducible tac promoter rather than the nitrogen-responsive nac promoter. When IPTG was present, cells carrying the tac-nac fusion activated NAC-dependent operons and repressed NAC-repressible operons independent of the nitrogen supply and even in the absence of an active NTR system. Thus, NAC is sufficient to regulate operons like hut (encoding histidase) and gdh (encoding glutamate dehydrogenase), confirming the model that the NTR system activates nac expression and NAC activates hut and represses gdh. Activation of urease formation occurred at a lower level of NAC than that required for glutamate dehydrogenase repression, and activation of histidase formation required still more NAC.
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PMID:The product of the Klebsiella aerogenes nac (nitrogen assimilation control) gene is sufficient for activation of the hut operons and repression of the gdh operon. 845 54

Amperometric enzyme probes for ammonium and urea have been assembled and evaluated using immobilized glutamate dehydrogenase and urease enzymes coupled with platinum electrodes. Analytical parameters such as pH, buffer, temperature, probe life-time, enzyme immobilization, cofactor concentration and response time have been optimized. Ammonium was detected in the range 10(-5)-3 x 10(-4) mol l-1. Better reproducibility and stability were achieved using the enzyme GLDH type III and NADH at a concentration of 10(-3) mol l-1. Urea has been determined in the range 10(-5)-3 x 10(-4) mol l(-1) using the enzyme urease first in solution and then immobilized on nylon net. The analysis was based on an amperometric measurement which gives a linear relationship between current and analyte concentration. This considerably improved the sensitivity of the analysis when compared with the potentiometric-based procedures. Moreover, this method does not suffer from the potassium ion interference which affects the potentiometric nonactin-based NH+4 electrodes. Analysis of ammonium and urea were carried out in standard solutions and in saliva samples. Results compared with a spectrophotometric reference procedure correlated well.
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PMID:Amperometric ammonium ion and urea determination with enzyme-based probes. 860 Sep 14

Axenic mycelia of the ectomycorrhizal basidiomycete, Suillus bovinus, were grown in liquid media under continuous aeration with compressed air at 25 degrees C in darkness. Provided with glucose as the only carbohydrate source, they produced similar amounts of dry weight with ammonia, with nitrate or with alanine, 60-80% more with glutamate or glutamine, but about 35% less with urea as the respectively only exogenous nitrogen source. In crude extracts of cells from NH4(+)-cultures, NADH-dependent glutamate dehydrogenase exhibited high aminating (688 nmol x mg protein(-1) x min(-1)) and low deaminating (21 nmol x mg protein(-1) x min(-1)) activities. Its Km-values for 2-oxoglutarate and for glutamate were 1.43 mM and 23.99 mM, respectively. pH-optimum for amination was about 7.2, that for deamination about 9.3. Glutamine synthetase activity was comparatively low (59 nmol x mg protein(-1) x min(-1)). Its affinity for glutamate was poor (Km = 23.7 mM), while that for the NH4+ replacing NH2OH was high (Km = 0.19 mM). pH-optimum was found at 7.0. Glutamate synthase (= GOGAT) revealed similar low activity (62 nmol x mg protein(-1) x min(-1)), Km-values for glutamine and for 2-oxoglutarate of 2.82 mM and 0.28 mM, respectively, and pH-optimum around 8.0. Aspartate transaminase (= GOT) exhibited similar affinities for aspartate (Km = 2.55 mM) and for glutamate (Km = 3.13 mM), but clearly different Km-values for 2-oxoglutarate (1.46 mM) and for oxaloacetate (0.13 mM). Activity at optimum pH of about 8.0 was 506 nmol x mg protein(-1) x min(-1) for aspartate conversion, but only 39 nmol x mg protein(-1) x min(-1) at optimum pH of about 7.0 for glutamate conversion. Activity (599 nmol x mg protein(-1) x min(-1)), substrate affinities (Km for alanine = 6.30 mM, for 2-oxoglutarate = 0.45 mM) and pH-optimum (6.5-7.5) proved alanine transaminase (= GPT) also important in distribution of intracellular nitrogen. There was comparatively low activity of the obviously constitutive enzyme, urease, (42 nmol x mg protein(-1) x min(-1)) whose substrate affinity was rather high (Km = 0.56 mM). Nitrate reductase proved substrate induced; activity could only be measured after exposure of the mycelia to exogenous nitrate. Routes of entry of exogenous nitrogen and tentative significance of the various enzymes in cell metabolism are discussed.
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PMID:Investigations into enzymes of nitrogen metabolism of the ectomycorrhizal basidiomycete, Suillus bovinus. 1081 9


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