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)

Two zinc (Zn)-resistant strains, AnZn-1 and AnZn-2, which were resistant to ZnSO4 up to 12.5 mg ml(-1) were isolated from industrial effluents. Both were Gram-negative with motile cells. They exhibited tolerance to Ba2+, Ni+, Co2+, Mn2+, Cu2+, Fe2+, Ni2+, Cd2+, kanamycin, chloramphenicol, ampillicin and tetracycline, but were sensitive to Hg2+ and streptomycin. For AnZn-1 and AnZn-2, the optimum pH for growth was 7. Both were facultative anaerobes and had cytochrome oxidase and urease enzymes, while catalase was present only in AnZn-2. Both strains had the ability to hydrolyse gelatin, reduce nitrate, and yield acid from arabinose and rhamnose. The two strains shared maximum characters with Vibrionaceae. Each strain carries a single Zn-resistant conjugative plasmid. The plasmid residing in AnZn-1 (pSH1211) displayed a lower level of resistance than the plasmid of AnZn-2 (pSH1212). Both required a minimum of 24 h for mating and showed highest transfer frequency at 25 degrees C. pSH1211 preferred pH 7 and pSH1212 pH 8.5 for their transfer. Both plasmids, when allowed to mate with Escherichia coli at 25 degrees C, alkaline pH values of 8-8.5 (pSH1211) of pH 7.5 (pSH1212), showed increased transfer frequency.
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PMID:Effects of temperature and pH on conjugal transfer of zinc-resistant plasmids residing in Gram-negative bacteria isolated from industrial effluents. 1509 89

The main effects of pollutions including acid rain, Cu2+, atrazine and their combined products on the activities of urease, invertin, acid phosphatase and catalase were studied by means of orthogonal test. The results showed that H+ and Cu2+ had significant influence on the activities of four enzymes and the ability of their inhibiting followed the order: H+ > Cu2+. Al3+ and atrazine only had litter effects on the activity of urease and phosphatase, respectively. Furthermore, interaction analysis revealed that Cu2+ -H+ affected on the activity of acid phosphatase significantly and antagonism on invertin and urease, Cu2+ -atrazine only exhibited the synergism on the activity of acid phosphatase. But atrazine-H+ had non-interaction within the investigated concentration range. Among four enzymes, acid phosphatase was the most sensitive one to the contaminations.
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PMID:Effect of organic/inorganic compounds on the enzymes in soil under acid rain stress. 1513 33

The effects of acid rain, Cu2+ and atrazine on the activities of soil urease, invertase and acid phosphatase were studied by means of orthogonal test. The results showed that the inhibition rate was H+ > Cu2+, and atrazine had no significant influence on urease and intertase. Interaction analysis revealed that Cu x atrazine exhibited synergism on soil acid phosphatase activity, Cu x H had antagonism on soil invertase and urease, but atrazine x H had no interaction within the investigated concentration range. Among the three enzymes, soil acid phosphatase was the most sensitive one to the contaminations.
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PMID:[Effect of acid rain, copper, and atrazine on soil hydrolase activity]. 1513 4

The kinetics of heavy metal ions inhibition of jack bean urease was studied by progress curve analysis in a reaction system without enzyme-inhibitor preincubation. The inhibition was found to be biphasic with an initial, small inhibitory phase changing over the time course of 5-10 min into a final linear steady state with a lower velocity. This time-dependent pattern was best described by mechanism B of slow-binding inhibition, involving the rapid formation of an EI complex that subsequently undergoes slow conversion to a more stable EI* complex. The kinetic parameters of the process, the inhibition constants Ki and Ki* and the forward k5 and reverse k6 rate constants for the conversion, were evaluated from the reaction progress curves by nonlinear regression treatment. Based on the values of the overall inhibition constant Ki*, the heavy metal ions were found to inhibit urease in the following decreasing order: Hg2+ > Cu2+ > Zn2+ > Cd2+ > Ni2+ > Pb2+ > Co2+ > Fe3+ > As3+. With the Ki* values as low as 1.9 nM for Hg2+ and 7.1 nM for Cu2+, 100-1000 times lower than those of the other ions, urease may be utilized as a bioindicator of the trace levels of these ions in environmental monitoring, bioprocess control or pharmaceutical analysis.
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PMID:Heavy metal ions inhibition of jack bean urease: potential for rapid contaminant probing. 1520 95

A screen-printed three-electrode amperometric biosensor based on urease and the nicotinamide adenine dinucleotide hydrogen (NADH)-glutamic dehydrogenase system was developed and applied to the screening of heavy metals in environmental samples. The development of an amperometric sensor for the monitoring of urease activity was feasible by coupling the urea breakdown reaction catalysed by urease to the reductive ammination of ketoglutarate catalysed by glutamic dehydrogenase (GLDH). The ammonia provided by the urea conversion is required for the conversion of ketoglutarate to glutamate with the concomitant oxidation of the NADH cofactor. NADH oxidation is monitored amperometrically at 0.3 V (vs. Ag/AgCl) after urease immobilization onto the screen-printed three-electrode configuration. Immobilization of urease on the surface of screen-printed electrodes was performed by entrapment in alginate gel and adsorption on the electrode in a nafion film. Low sensitivity to inactivation by metals was recorded after urease entrapment in alginate gel with detection limits of 2.9 and 29.8 mg L(-1) for Hg(II) and Cu(II), respectively. The use of the negatively charged nafion film created a more concentrated environment of cations in proximity to the enzyme, thus enhancing the urease inhibition when compared to gel entrapment. The calculated detection limits were 63.6 and 55.3 microg L(-1) for Hg(II) and Cu(II), respectively, and 4.3 mg L(-1) for Cd(II). A significant urease inactivation was recorded in the presence of trace amounts of metals (microg L(-1)) when the enzyme was used free in solution. Analysis of water and soil samples with the developed nafion-based sensor produced inhibition on urease activity according to their metal contents. The obtained results were in agreement with the standard methods employed for sample analysis. Nevertheless, the use of the amperometric assay (with free urease) proved more feasible for the screening of trace amounts of metals in polluted samples.
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PMID:Urease-glutamic dehydrogenase biosensor for screening heavy metals in water and soil samples. 1530 Mar 52

Low nutrient density in weaning foods is the major cause of under-nutrition among infants and young children in developing countries. Ten types of composite weaning diets (namely, maize-rojo beans-peanut, maize-peanut-sardines, maize-peanut-sardine-rojo beans, maize-peanut-soaked rojo beans, maize-peanut-germinated rojo beans, sorghum-rojo beans-peanut, sorghum-peanut-sardines, sorghum-peanut-sardine-rojo beans, sorghum-peanut-soaked rojo beans, and sorghum-peanut-germinated rojo beans) were formulated and assayed for proximate composition, energy, mineral density, tannin content and residual urease activity. The diets were also evaluated for storage stability under ambient conditions, sensory quality and overall acceptability. Results of the study indicated that, concentrations of protein, fat, ash, calcium, iron, zinc and copper were significantly (P<0.05) increased when plain maize and sorghum gruels were enriched with rojo beans, peanut paste and/or ground sardines. Soaking and germinating the rojo beans and dehulling the sorghum reduced the concentration of tannins in the gruels significantly (P<0.05). Residual urease activity ranged between 0.00 and 0.07 units, about 10-fold lower than the maximum level (0.8 units) allowed in weaning foods. Both maize and sorghum-based composite gruels had a short shelf-life under ambient conditions (26.4 degrees C) ranging between 4 and 6 h, with gruels containing ground sardines showing a tendency to spoil faster. All composite gruels except those containing germinated rojo beans were highly liked and accepted by consumers (P<0.05), similar to the plain maize and sorghum gruels. The maize and sorghum-based composite products therefore have a potential for use as weaning and/or supplementary foods for older infants and young children. Further investigations are suggested to extend the shelf-life of the composite products and improve the organoleptic quality of the diets containing germinated rojo beans.
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PMID:Nutritional value and acceptability of homemade maize/sorghum-based weaning mixtures supplemented with rojo bean flour, ground sardines and peanut paste. 1536 84

An array-based optical biosensor for the simultaneous analysis of multiple samples in the presence of unrelated multi-analytes was fabricated. Urease and acetylcholinesterase (AChE) were used as model enzymes and were co-entrapped with the sensing probe, FITC-dextran, in the sol-gel matrix to measure pH, urea, acetylcholine (ACh) and heavy metals (enzyme inhibitors). Environmental and biological samples spiked with metal ions were also used to evaluate the application of the array biosensor to real samples. The biosensor exhibited high specificity in identifying multiple analytes. No obvious cross-interference was observed when a 50-spot array biosensor was used for simultaneous analysis of multiple samples in the presence of multiple analytes. The sensing system can determine pH over a dynamic range from 4 to 8.5. The limits of detection (LODs) of 2.5-50 microM with a dynamic range of 2-3 orders of magnitude for urea and ACh measurements were obtained. Moreover, the urease-encapsulated array biosensor was used to detect heavy metals. The analytical ranges of Cd(II), Cu(II), and Hg(II) were between 10 nM and 100 mM. When real samples were spiked with heavy metals, the array biosensor also exhibited potential effectiveness in screening enzyme inhibitors.
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PMID:Simultaneous determination of pH, urea, acetylcholine and heavy metals using array-based enzymatic optical biosensor. 1568 Nov 96

Poly(acrylonitrile-methylmethacrylate-sodium vinylsulfonate) membranes were subjected to seven different chemical modifications and the amount of the newly formed groups was measured for each membrane. Urease was then covalently immobilized onto the modified membranes and the amount of bound protein was determined. The kinetic parameters V(max) and K(m) of the immobilized urease were studied under static and dynamic conditions. Results showed that the rate of the enzyme reaction was higher for the membranes modified with NH(2)OH . H(2)SO(4), NH(2)NH(2) . H(2)SO(4), NaOH + EDA and NaOH + GA + EDA. It was confirmed that the reaction rate, measured under dynamic conditions, was higher than that one determined under static conditions. The influence of Cu(II) ions, as inhibitors, on the enzyme reaction kinetics (V(i) and K(i)) was also investigated. It turned out that the most sensitive membranes towards Cu(II) were those modified with NH(2)NH(2) . H(2)SO(4), NaOH + EDA and H(2)O(2). The results initiated further investigations on the influence of other heavy metal ions (Cd(II), Zn(II), Ni(II) and Pb(II)) over urease bound to a NH(2)OH . H(2)SO(4)-modified membrane. It was found that the inhibition effect of the heavy metal ions over immobilized urease decreases in the order: Cu(II) > Cd(II) > Zn(II) > Ni(II) > Pb(II). [Diagram: see text]
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PMID:Kinetic parameters of urease immobilized on modified acrylonitrile copolymer membranes in the presence and absence of Cu(II) ions. 1589 77

The pathogenic bacteria Helicobacter pylori require nickel as a cofactor of the enzymes urease and hydrogenase. One of the proteins that controls nickel homeostasis in this organism is Helicobacter pylori NikR (HpNikR), a homologue of nickel-dependent transcription factors from other organisms, which regulates the expression of multiple proteins such as the urease structural subunits and itself. To examine the properties of this protein, metal analysis was used to demonstrate that HpNikR can bind stoichiometric nickel or copper, and electronic absorption spectroscopy revealed that HpNikR binds nickel with picomolar affinity in what is likely a conserved square-planar site. In vitro DNA-binding assays revealed that HpNikR can bind directly to the promoter region of the ureA operon in response to nickel, and the location of the binding site was defined. Nickel also induces DNA binding to the nikR promoter sequence but the complex is much weaker. These experiments suggest that HpNikR directly controls the expression of multiple genes by binding to separate DNA sequences, and the possible mechanisms for differential regulation are discussed.
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PMID:The metal- and DNA-binding activities of Helicobacter pylori NikR. 1634 30

Maintaining metal homeostasis is crucial for the adaptation of Helicobacter pylori to the gastric environment. Iron, copper, and nickel homeostasis has recently been demonstrated to be required for the establishment of H. pylori infection in animal models. Here we demonstrate that the HP0969-0971 gene cluster encoding the Czc-type metal export pump homologs HP0969, HP0970, and the H. pylori-specific protein HP0971 forms part of a novel H. pylori metal resistance determinant, which is required for gastric colonization and for the modulation of urease activity. Insertional mutagenesis of the HP0971, HP0970, or HP0969 genes in H. pylori reference strain 26695 resulted in increased sensitivity to cadmium, zinc, and nickel (czn), suggesting that the encoded proteins constitute a metal-specific export pump. Accordingly, the genes were designated cznC (HP0971), cznB (HP0970), and cznA (HP0969). The CznC and CznA proteins play a predominant role in nickel homeostasis, since only the cznC and cznA mutants but not the cznB mutant displayed an 8- to 10-fold increase in urease activity. Nickel-specific affinity chromatography demonstrated that recombinant versions of CznC and CznB can bind to nickel and that the purified CznB protein interacted with cadmium and zinc, since both metals competitively inhibited nickel binding. Finally, single cznA, cznB, and cznC mutants did not colonize the stomach in a Mongolian gerbil-based animal model. This demonstrates that the metal export functions of H. pylori cznABC are essential for gastric colonization and underlines the extraordinary importance of metal ion homeostasis for the survival of H. pylori in the gastric environment.
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PMID:The novel Helicobacter pylori CznABC metal efflux pump is required for cadmium, zinc, and nickel resistance, urease modulation, and gastric colonization. 1679 Jul 56


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