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:6.3.4.6 (urease)
7,490 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The effect of LC(50) (1.8 MG/L) and a sublethal concentration (0.03 mg/L) of in vivo mercuric chloride exposure on the activities of acid and alkaline phosphatases, glucose-6-phosphatase, lipase and urease in the kidneys and ovaries of a teleost fish, Channa punctatus has been studied after 96 hr and 30 days respectively. It has been observed that the activities of all the enzymes except acid phosphatase were significantly inhibited in both the tissues. However, treatment for 96 hr resulted in more marked inhibition than 30 days of treatment. Acid phosphatase showed elevation in activity in the kidney after 96 hr of treatment.
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PMID:Mercuric chloride induced enzymological changes in kidney and ovary of a teleost fish, Channa punctatus. 22 98

The effect of LC(50) and a sublethal concentration of lead nitrate on the activities of alkaline phosphatase, acid phosphatase, glucose-6-phosphatase, lipase and urease in the kidneys and ovaries of a teleost fish, Channa punctatus has been examined after 96 hr and 30 days respectively. The results show that all the five enzymes in the two tissues are inhibited significantly at both the experimental stages. However, the inhibition produced after 30 days by the sublethal concentration ish higher indicating the cumulative action of lead. Further, the inhibition of enzymes is, more marked in kidney than in the ovary.
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PMID:Effects of lead nitrate on the activities of a few enzymes in the kidney and ovary Heteropneustes fossillis. 22

A new rapidly growing mycobacterium was isolated from human sputum. This organism grew at 22, 31, 37, and 41 degrees C and possessed catalase, acid phosphatase, acetamidase, urease, nicotinamidase, pyrazinamidase, and nitrate reductase activities. It did not produce nicotinic acid, hydrolyze Tween, or have benzamidase, isonicotinamidase, succinidamidase, and arylsulfatase activities. A mycolic acid analysis revealed a simple, unique pattern. The organism is susceptible to antituberculotic drugs. A comparative 16S rRNA sequence analysis placed this organism within the confines of the genus Mycobacterium, most closely related to the thermotolerant rapidly growing species. On the basis of the pattern of enzymatic activities and metabolic properties, as well as the unique 16S rRNA sequence, we propose that our single strain represents a new species, for which we propose the name Mycobacterium confluentis. The type strain is strain 1389/90; a culture of this strain has been deposited in the German Collection of Microorganisms and Cell Cultures as strain DSM 44017.
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PMID:Mycobacterium confluentis sp. nov. 137 23

In accordance with Recommendation 30b of the International Code of Nomenclature of Bacteria, which calls for the development of recommended minimal standards for describing new species, we propose minimal standards for describing the genus Mycobacterium and new slowly growing species of this genus. The minimal standards for assignment of a strain to the genus Mycobacterium include acid-alcohol fastness, a DNA G+C content in the range from 61 to 71 mol%, and mycolic acid detection with characterization of C22 to C26 pyrolysis esters. The recommended minimal standards for describing a new slowly growing Mycobacterium species are based on the results of phenotypic and genomic studies and include the results of the following conventional tests: growth at 25, 30, 33, 37, 42, and 45 degrees C; pigmentation; resistance to isoniazid, thiophene-2-carboxylic acid hydrazide, hydroxylamine, p-nitrobenzoic acid, sodium chloride, thiacetazone, picrate, and oleate; catalase activity; Tween hydrolysis; urease activity; niacin detection; and nitrate reductase, acid phosphatase, arylsulfatase, pyrazinamidase, and alpha-esterase activities. In addition, a mycolic acid profile should be determined, and DNA-DNA hybridization experiments in which the difference between the denaturation temperature of the homologous reaction and the denaturation temperature of the heterologous reaction is determined should be performed. This proposal has been endorsed by the members of the Subcommittee for Taxonomy of the Mycobacteria of the International Committee on Systematic Bacteriology.
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PMID:Proposed minimal standards for the genus Mycobacterium and for description of new slowly growing Mycobacterium species. 158 Nov 93

Benzoyl- and isopentenoyl phosphoric triamides (BPA and IPA) strongly inhibited urease activities from jack bean, soybean, watermelon seed, Proteus mirabilis, P. rettgeri, P. vulgaris, Mycobacterium smegmatis, and Ureaplasma urealyticum. Their I50 values (the final concentration causing 50% inhibition), independent of enzyme source, were 2-21 nM, which are about 1,000-fold lower than that of caprylohydroxamic acid, one of the most potent urease inhibitors. ATP-urea amidolyase activity was inhibited 50% by BPA at a higher concentration of 0.28 mM, but was not affected by IPA even at 1.3 mM. Thirteen kinds of hydrolases (trypsin, chymotrypsin, thermolysin, leucine aminopeptidase, papain, lipase, alpha-amylase, glucuronidase, asparaginase, arylsulfatase, alkaline phosphatase, acid phosphatase, and true cholinesterase), two oxidoreductases (catalase and alcohol dehydrogenase), three transferases (glutamic-oxaloacetic aminotransferase, gamma-glutamyl transpeptidase, and arylsulfotransferase) and two kinases (pyruvate kinase and creatine kinase) were not affected at all even at 1 mM BPA and IPA. Exceptionally, pseudo-cholinesterase from human serum was inhibited by BPA and IPA, whose I50 values were 70 nM and 10 muM, respectively, using acetylthiocholine as a substrate. These values increased to 0.55 muM and 54 muM, respectively, when acetylcholine was used as a substrate. These results show that N-acylphosphoric triamides potently and specifically inhibit urease activity at concentrations of nM order.
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PMID:Specific inhibition of urease by N-acylphosphoric triamides. 384 42

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.
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PMID:Proteus mirabilis urease: transcriptional regulation by UreR. 767 44

We analyzed 11 H. pylori isolates from humans using the artificial chromogenic substrate paranitrophenylphosphorylcholine to detect phospholipase C (PLC) activity. The range of PLC in sonicates was 8.8-92.3 (Mean 56.9 +/- 6.5) nmol of substrate hydrolysed min-1 mg-1 protein; the amount of activity was not associated with urease or cytotoxin levels. Addition of sorbitol or glycerol enhanced PLC activity of H. pylori sonicate and purified PLC from C. perfringens (PLC1) but not purified PLC from B. cereus (PLC3). H. pylori sonicates had little acid phosphatase and no detectable alkaline phosphatase activity, and H. pylori PLC showed markedly different biochemical characteristics from either phosphatase. In total, these studies indicate that activity measured in H. pylori sonicate by PLC assay is due to PLC and not phosphatase activity. The temperature optimum for PLC activity of H. pylori sonicate was 56 degrees C and for PLC 1 was 65 degrees C. For H. pylori PLC and PLC1, optimal activity occurred at pH 8. Despite multiple similarities between H. pylori PLC and PLC1, known PLC inhibitors show different interactions with each enzyme. Although PLC activity is present in many subcellular constituents of H. pylori, including culture supernatants and water extracts, highest specific activity is associated with a membrane-enriched fraction.
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PMID:Identification and characterization of Helicobacter pylori phospholipase C activity. 828 Sep 31

Antimicrobial susceptibility of 50 local isolates of Helicobacter pylori from patients with acid peptic diseases was investigated to commonly used antibiotics. The maximum resistance was (66%) detected to metronidazole (MIC > 8 micrograms/ml). The frequency of resistance to ampicillin, erythromycin, ciprofloxacin was in the range of 20-28 per cent; least resistance was observed to tetracycline (10%). The gradient disc diffusion method was found to give reproducible results and also correlated with agar dilution method for minimum inhibitory concentration (MIC). Study of the enzymatic activity of H. pylori isolates showed that all isolates had urease, catalase, oxidase, esterase-lipase, and naphthol-AS-beta-1-phosphohydrolase enzymes and were consistently negative for ten other enzymes tested. Majority of the isolates expressed alkaline phosphatase (17/18), esterase (17/18) and acid phosphatase (14/18). The acid phosphatase had the maximum mean enzymatic activity. There was no difference in enzymatic activity between H. pylori isolates from ulcer and gastritis patients. H. pylori isolates could be typed into five biotypes. Type III was found to be more common (44.4%). This study supports the existence of the strain variations among H. pylori on the basis of the enzyme profiles.
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PMID:Antimicrobial susceptibility pattern & biotyping of Helicobacter pylori isolates from patients with peptic ulcer diseases. 855 18

Helicobacter pylori was grown on solid medium for up to 5 weeks. Morphological conversion from spiral to coccoid forms began after 7 days incubation under microaerophilic conditions. Similar to the exponential cultures, the ageing bacteria produced alkaline phosphatase, acid phosphatase, leucine arylamidase and naphthol-AS-beta 1-phosphohydrolase, although there was a reduction in the levels of the latter two enzymes. Unlike the other enzymes, urease was not detected in 5-week-old cultures. By using primers based on urease subunit C and 26 kD protein genes for polymerase chain reaction (PCR) these two important gene fragments remained conserved despite the morphological conversion from spiral to coccoid forms. Furthermore, PCR-based random amplified polymorphic DNA (RAPD) fingerprinting showed similar DNA banding patterns from bacteria of various ages, demonstrating the conservation of the DNA composition despite morphological changes. This study shows that the aging coccoid form of H. pylori, although reportedly non-culturable in vitro, remains genetically unchanged indicating that it is likely to be viable.
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PMID:Is the coccoid form of Helicobacter pylori viable? 903 59

The present study was made to isolate and assess some physiological characteristics of root nodule-colonizing fungi. During this study, 17 fungal species were isolated from root nodule samples taken from faba bean plants (Vicia faba L.) collected from different sites at Assiut area (Egypt). The growth of faba bean plants in pots was significantly promoted by soil inoculation with most fungi. Growth was checked in pots with inocula of Cladosporium cladosporioides, Fusarium moniliforme, F: oxysporium, F solani, Macrophominia phaseolina and Rhizoctonia solani which were added separately. All growth-promoting fungi were capable of producing cellulase, pectin lyase, polygalacturonase, protease, urease, amidase, acid phosphatase, alkaline phosphatase and arylsulfatase in growth medium supplemented with the corresponding substrates. Four fungal species, Aspergillus awamori, A. flavus, Penicillium chrysogenum and Trichoderma koningii showed the highest rates of enzyme formation. The effect of the addition of six trace elements to the growth media at 30 micromol/ml on enzyme production revealed some dependency on species, enzyme and metal ion. Cd2+, Hg2+ and Zn2+ generally inhibited enzyme activity. Cu(1+), Fe3+ and Al3+ showed a stimulatory effect. Fungicides (afugan and tilt) and herbicides (brominal and fusilade) at 50 ppm generally promoted enzyme activity, but insecticides (kelthane and fenvalerate) caused some inhibition to enzyme activities. Salinization of the growth media with NaCl strongly inhibited the enzymatic activity of all fungi at concentrations between 0.5 and 1.5%.
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PMID:Physiological aspects of fungi isolated from root nodules of faba bean (Vicia faba L.). 1077 56


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