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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)

1. Citrate isocitrate and 2-oxoglutarate levels were determined in isolated rat hepatocytes and in particulate and soluble fractions, thereof, obtained by the digitonin and silicone oil fractionation technique. 2. Caculated from isocitrate/2-oxoglutarate ratios ("indicator metabolite method"), the redox potential of mitochondrial free NADPH is -402 mV, whereas that of the extramitochondrial (cytosolic) space is about 10 mV more positive, -392 mV. 3; Addition of ammonia (either as ammonium chloride or from urea plus urease) to isolated hepatocytes causes preferential oxidation of mitochondrial NADPH, is demonstrated by spectrophotometry of the dihydro band and by the changes in the isocitrate/2-oxoglutarate ratios. The redox potential difference of free NADPH between mitochondria and cytosol is abolished or even reserved. 4. It is concluded that during urogenesis from ammonia mitochondrial isocitrate oxidation is shifted largely in favor of the NADP-linked as opposed to the NAD-linked enzyme; isocitrate concentration under these conditions is less than 10 muM, below the Km (isocitrate) of the NAD-linked enzyme but in the range of that for the NADP-linked enzyme. 5. Both in the absence and in the presence of ammonia there is a concentration gradient across the mitochondrial inner membrane (from mitochondria to cytosol) for citrate, isocitrate, and also, to a smaller extent, for 2-oxoglutarate. 6. These results and data in the literature on enzyme activity are in agreement with the assumption of near-equilibrium of NADP-dependent isocitrate dehydrogenases in the mitochondrial matrix and cytosolic spaces in the absence of ammonia; accordingly, during urea formation from added ammonia the redox potential of mitochondrial free NADPH is increased to -391 mV or possibly even higher if there exists an indicator error under this condition.
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PMID:Mitochondrial and cytosolic NADPH systems and isocitrate dehydrogenase indicator metabolites during ureogensis from ammonia in isolated rat hepatocytes. 1 98

A direct enzymatic micromethod (sample volume, 3mul) has been adapted to the centrifugal analyzer (ENI-GEMSAEC) for measurement of urea in plasma and urine. The method is based on urease (urea amidohydrolase, EC3.5.1.5)/glutamate dehydrogenase [l-glutamate:NAD(P)+oxidoreductase (deaminating), EC1.41.3] coupled reactions, and uses a two-point fixed-time (t(1)=20s,t(2)=50s)kinetic scheme for monitoring the rate of comsumption of NADH at 340 nm. Sensitivity and precision of the method are excellent,and results compare well with those from a commonly used continuous-flow method.
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PMID:Direct enzymatic determination of urea in plasma and urine with a centrifugal analyzer. 97 5

Semipermeable nylon-polyethylenimine artificial cells containing leucine dehydrogenase (EC 1.4.1.9), alcohol dehydrogenase (EC 1.1.1.1), urease (EC 3.5.1.5), and dextran-NAD+ were prepared. Artificial cells could convert ammonia or urea into L-leucine, L-valine, and L-isoleucine. For batch conversion in 20.0 mM of ammonium acetate substrate solutions, in 2 h 0.2 ml of artificial cells could produce 4.48 mumol of L-leucine, 9.98 mumol of L-valine, or 5.96 mumol of L-isoleucine. The corresponding conversion ratios were 22.4, 49.9, and 29.8%. In 20.0 mM of urea substrate solutions, 13.71 mumol of L-leucine, 16.12 mumol of L-valine, or 13.44 mumol of L-isoleucine was produced and the conversion ratios were 68.6, 80.6, and 67.2%. The substrate specificity of leucine dehydrogenase for the reductive amination was determined. Of the three branched-chain amino acids produced, the production rates of L-valine were the highest. The apparent Km values were as follows: 0.32 mM for alpha-ketoisocaproate, 1.63 mM for alpha-ketoisovalerate, and 0.73 mM for Dl-alpha-keto-beta-methyl-n-valerate. The leucine dehydrogenase multienzyme system had a good storage stability. It retained 72.0% of the original activity with artificial cells were stored at 4 degrees C for 6 weeks. The optimum conversion pH and temperature were 8.5-9.0 and 35-40 degrees C. The effects of urea and ammonium salts on conversion rate were also studied. The relative activities in ammonium salts solutions were 45.1-75.9% of those in urea solutions.
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PMID:Conversion of ammonia or urea into essential amino acids, L-leucine, L-valine, and L-isoleucine, using artificial cells containing an immobilized multienzyme system and dextran-NAD+. 2. Yeast alcohol dehydrogenase for coenzyme recycling. 169 39

A multienzyme system consisting of leucine dehydrogenase (EC 1.4.1.9), L-lactic dehydrogenase (EC 1.1.1.27), urease (EC 3.5.1.5), and dextran-NAD+ was microencapsulated within artificial cells. This system could convert ammonia and urea into essential amino acids, L-leucine, L-valine, and L-isoleucine. L-lactate acted as a cosubstrate for the regeneration of dextran-NADH. Greater concentrations of L-lactate favored the higher conversion ratios. The effects of ammonium salts and urea on reaction rate were also studied. The relative reaction rates in ammonium salts solutions were 44.6-78.8% of those in urea solutions. More than 90% of the original activity was retained when artificial cells were kept at 4 degrees C for 6 wk.
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PMID:Conversion of ammonia or urea into essential amino acids, L-leucine, L-valine, and L-isoleucine using artificial cells containing an immobilized multienzyme system and dextran-NAD. L-lactic dehydrogenase for coenzyme recycling. 170 78

Artificial cells containing glucose dehydrogenase (EC 1.1.1.47), leucine dehydrogenase (EC 1.4.1.9), urease (EC 3.5.1.5), and dextran-NAD+ were prepared. Ammonia or urea could be converted into L-leucine, L-valine, and L-isoleucine with artificial cells. Low-specific-activity glucose dehydrogenase could effectively regenerate dextran-NADH, which was recycled at a rate of 0.4 to 0.5 cycle per minute under reaction conditions. The effects of ammonium salts and urea on the conversion rate for the leucine dehydrogenase multienzyme system were also studied. The relative activities in ammonium salts solutions were 40 to 70% of those in urea solutions.
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PMID:Conversion of ammonia or urea into L-leucine, L-valine, and L-isoleucine using artificial cells containing an immobilized multienzyme system and dextran-NAD+. Glucose dehydrogenase for co-factor recycling. 245 27

Artificial cells containing leucine dehydrogenase (EC 1.4.1.9), alcohol dehydrogenase (EC 1.1.1.1; or glucose dehydrogenase, EC 1.1.1.47; or lactic dehydrogenase, EC 1.1.1.27; or malic dehydrogenase, EC 1.1.1.37), urease (EC 3.5.1.5) and dextran-NAD+ were prepared. Ammonia or urea could be converted into L-leucine, L-valine and L-isoleucine using artificial cells with four different multienzyme systems.
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PMID:Conversion of urea or ammonia into essential amino acids (L-leucine, L-valine, and L-isoleucine) using multienzyme systems and NADH-dextran immobilised in artificial cells. 344 45

A total of 307 lungs obtained from a slaughterhouse were cultured by a dilution technique for the isolation of Haemophilus spp. The technique consisted of performing serial (10-fold) dilutions of the tissue samples to a dilution of 10(-5). Two selective media were used. L broth consisted of a basal brain heart infusion broth containing 5% horse serum, 5% yeast extract, and 100 micrograms of NAD and 0.5 microgram of lincomycin per ml. L-B broth was identical to L broth, except 1.5 microgram of bacitracin per ml was included. The broths were incubated overnight and then plated onto blood agar. A total of 83 (27%) isolates were obtained, and both media proved to be necessary, as a proportion of isolates grew in one of the media employed but not in the other. Of the isolates, 66.3% were urease positive and most of these (98%) were classified as "minor group" strains. Urease-negative strains (27.7%) were classified as Haemophilus parasuis.
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PMID:Dilution technique for isolation of Haemophilus from swine lungs collected at slaughter. 635 Mar 43

Thirty Haemophilus strains and six Actinobacillus strains, all of porcine origin, were examined for their biochemical reactivity on API 20E and API ZYM test strips using dense cell suspensions (supplemented with NAD as appropriate) as strip inocula. When combined with a test for V-factor dependency, the use of both strips allowed adequate differentiation of closely related organisms. Numerical taxonomic analysis of the data demonstrated that the majority of the haemophili and actinobacilli studied could be placed in one of four major clusters; these clusters contained, respectively, the H. pleuropneumoniae--A. pleuropneumoniae strains, the H. parasuis strains, strains belonging to Haemophilus taxon "minor group," and strains belonging to an unusual group of mannitol-positive, urease-negative haemophili. A representative of Haemophilus species taxon C and an unusual Actinobacillus isolate appeared to be comparatively unrelated to organisms in the four major clusters. Although it may, on occasion, be difficult to place an unusual isolate in any one particular group, owing to the uncertain taxonomy of some of these organisms, it is concluded that API test strips can serve as useful tools for the characterization and differentiation of porcine haemophili and actinobacilli.
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PMID:Porcine haemophili and actinobacilli: characterization by means of API test strips and possible taxonomic implications. 650 90

The enzymic mechanism of metabolization of urea-formaldehyde condensation products (methyleneureas; MU) and the fate of the degradation products ammonium, urea and formaldehyde were studied in bacteria isolated from garden soil, which were able to use methyleneureas as the sole source of nitrogen for growth. An organism identified as Ochrobactrum anthropi completely degraded methylenediurea (MDU) and dimethylenetriurea (DMTU) to urea, ammonia, formaldehyde and carbon dioxide. An enzyme designated as methylenediurease (methylenediurea deiminase; MDUase) was responsible for the degradation of both MDU and DMTU as well as higher polymerized MU. Growth on MU as the nitrogen source specifically induced the synthesis of this enzyme, which seems to be located in the periplasm of the bacterium. Under these growth conditions, urease as well as NAD-specific formaldehyde and formiate dehydrogenase were expressed to high levels, efficiently using the products of MU degradation, and high-affinity transport systems for urea and ammonia were synthesized scavenging the environment for these products.
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PMID:Microbial urea-formaldehyde degradation involves a new enzyme, methylenediurease. 1052 91

A bacterial strain utilizing methanol as the sole source of carbon and energy was isolated from the maize phyllosphere. Cells are nonpigmented gram-negative motile rods that do not form spores or prosthecae and reproduce by binary fission. The strain does not require vitamins or supplementary growth factors. It is obligately aerobic and urease-, oxidase-, and catalase-positive. The optimum growth temperature is 35-40 degrees C; the optimum pH is 7.0-7.5. The doubling time is 2 h. The bacterium implements the ribulose monophosphate pathway and possesses NAD(+)-dependent 6-phosphogluconate dehydrogenase and enzymes of the glutamate cycle. alpha-Ketoglutarate dehydrogenase and enzymes of the glyoxylate cycle (isocitrate lyase and malate synthase) are absent. Fatty acids are dominated by palmitic (C16:0) and palmitoleic (C16:1) acids. The major phospholipids are phosphatidylethanolamine, phosphatidylglycerol, and phosphatidylcholine. Cardiolipin is present in minor amounts. The dominant ubiquinone is Q8. The bacterial genome contains genes controlling the synthesis and secretion of cytokinins. The G + C content of DNA is 57.2 mol %, as determined from the DNA thermal denaturation temperature (Tm). The bacterium shows low DNA homology (< 10%) with restricted facultative methylotrophic bacteria of the genus Methylophilus (M. methylotrophus NCIMB 10515T and M. leisingerii VKM B-2013T) and with the obligate methylotrophic bacterium (Methylobacillus glycogenes ATCC 29475T). DNA homology with the type representative of the genus Methylovorus, M. glucosetrophus VKM B-1745T, is high (58%). The new isolate was classified as a new species, Methylovorus mays sp. now.
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PMID:[Methylovorus mays--novel species of aerobic, obligatory methylotrophic bacteria associated with plants]. 1131 76


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