2 edition of expression, regulation and biological importance of the urease enzyme of Helicobacter Pylori found in the catalog.
expression, regulation and biological importance of the urease enzyme of Helicobacter Pylori
Beverly Joy Davies
Thesis (Ph.D) - University of Birmingham, School of Biosciences, Faculty of Science.
|Statement||by Beverly Joy Davies.|
|The Physical Object|
|Pagination||246 p. :|
|Number of Pages||246|
Highlights Recombinant Helicobacter pylori (rHPU) urease induces paw edema with neutrophil infiltration. rHPU is chemotactic to human neutrophils independently of its enzyme activity. rHPU promotes ROS release and inhibits apoptosis of human neutrophils. Lipoxygenase metabolite(s) mediate the pro-inflammatory effects of by: Helicobacter pylori, previously known as Campylobacter pylori, is a gram-negative, helically-shaped, microaerophilic bacterium usually found in the stomach. Its helical shape (from which the genus name, helicobacter, derives) is thought to have evolved in order to penetrate the mucoid lining of the stomach and thereby establish infection. The bacterium was first identified in by Pronunciation: /ˈhɛlɪkoʊˌbæktər paɪˈlɔːraɪ, pɪ-, -ri/.
Urease (EC ; urea amidohydrolase) is a nickel-containing enzyme found in archaea, bacteria, unicellular eukaryotes, and plants (Maroney & Ciurli, ; Zambelli, Musiani, Benini, & Ciurli, ).This protein acts in the last step of organic nitrogen mineralization, catalyzing the hydrolysis of urea to ammonia and carbamate, which spontaneously decomposes to give a second molecule of. active site of enzyme and the importance of nickel to this metalloenzyme. Inhibition Studies of Urease The inhibitions of urease were extensively studied because of their potential uses like: (i) Therapy against bacterial urease (eg: Helicobacter pylori) that induced human pathogenic states, such as, urinary.
The nickel-containing enzyme urease is an essential colonization factor of the gastric pathogen Helicobacter pylori, as it allows the bacterium to survive the acidic conditions in the gastric mucosa. Although urease can represents up to 10% of the total protein content of H. pylori, expression of urease genes is thought to be by: The presence of urease is used in the diagnosis of Helicobacter species. All bacterial ureases are solely cytoplasmic, except for those in Helicobacter pylori, which along with its cytoplasmic activity, has external activity with host cells. In contrast, all plant ureases are : BRENDA entry.
Access to Literature
ruling class =
An American Scrapbook Journal
A new English dictionary
Human Rights in the Context of EU Foreign Policy and Enlargement (Nomos Universitatsschriften, Recht)
Heat and mass transfer in materials processing
[Dedicated followers of fashion].
Rethinking development strategy in Northeast Asia
Desultory sketches and tales of Barbados.
Summary report on the petroleum and natural gas resources of Canada
Instead of an acidic pH regulation and biological importance of the urease enzyme of Helicobacter Pylori book urease suitable only for passage through the stomach, it has a neutral pH optimum urease that allows the cytoplasm to remain relatively neutral while the organism protects itself against acid by enhancing urea access to intrabacterial urease Cited by: 9.
Metal-Responsive Gene Regulation. Metal ions such as iron, nickel, and copper are essential elements for all organisms, where they function in basic cell metabolism. Nickel is of particular importance for H. pylori, as the urease enzyme, which is produced in large amounts, requires nickel as a cofactor (see chapter 16).
March H. PYLORI AND ACID: BIOLOGICAL IMPLICATIONS Role of Urease Activity H. pylori produces large amounts of urease, which hydrolyzes urea to ammonia and carbon dioxide and has been linked to its acid survival–15 Urease is highly conserved among each of the Helicobacter species that colo- nize the mammalian stomach, suggesting that it serves.
;Tsudaetal.,),urease expression and enzyme activity are controlled by an intricate regulatory network, centred on the environmental pH and the avail-ability of the cofactor nickel (Scott et al., ; van Vliet et al., b). For H. hepaticus and other urease-positive enterohepatic Helicobacter species, the role of urease in.
Helicobacter hepaticus is a pathogen of rodents, which causes diverse enteric and hepatic inflammatory diseases and malignancies. The urease enzyme is an important colonization factor of gastric Helicobacter species like Helicobacter pylori, but little is known about the role and regulation of urease in enterohepatic Helicobacter species.
Here it is reported that urease activity of H Cited by: Helicobacter hepaticus is a pathogen of rodents, which causes diverse enteric and hepatic inflammatory diseases and malignancies.
The urease enzyme is an important colonization factor of gastric Helicobacter species like Helicobacter pylori, but little is known about the role and regulation of urease in enterohepatic Helicobacter by: Urease. produces large quantities of urease, about 5 - 6 % of the total cell protein and it is a mulitmeric - kDa, cytosolic metalloenzyme that requires two nickel ions (Ni2+) in each of the six active sites for catalytic activity (Fulkerson et al, ; Mobley, ).
This enzyme catalyzes the hydrolysis of urea to ammonia and carbon dioxide (Cussac et al, ) as shown in the.
Abstract. Since the first report of the urease activity of Helicobacter pylori , this enzyme has captured a large amount of attention from researchers interested in the detection and pathogenicity of this gastric bacterium. This interest is in part aroused by the extraordinary urease activity seen in H.
pylori [2–5]. Another enzyme of H. pylori noted for its vigor is catalase .Cited by: Analysis of expression of CagA and VacA virulence factors in 43 strains of Helicobacter pylori reveals that clinical isolates can be divided into two major types and that CagA is not necessary for expression of the vacuolating by: The enzyme urease is widespread in nature and catalyzes the hydrolysis of urea to form ammonia and carbonic acid.
pylori ureA and ureB genes encoding both subunits of urease were expressed transgenically in a low-alkaloid line of tobacco (LA Burley 21). Analysis of transgene expression at both the mRNA and. The nickel-containing enzyme urease is an essential colonization factor of the gastric pathogen Helicobacter pylori, as it allows the bacterium to survive the acidic conditions in the gastric mucosa.
Although urease can represents up to 10% of the total protein content of H. pylori, expressionCited by: Purification and characterisation of Helicobacter pylori urease Article (PDF Available) in Journal of Biological Chemistry (16) July with 98 Reads How we measure 'reads'. Nickel is of particular importance for H.
pylori, as the urease enzyme, which is produced in large amounts, requires nickel as a cofactor. Phase variation is the apparently random on- and off-switching of gene expression, and this mechanism of gene regulation is often encountered in bacterial surface-exposed structures such as flagella, adhesins, and lipopolysaccharide (LPS).
Acid urease with good tolerance toward ethanol and acid is ideal enzyme for such applications. In the present work, the structural genes of urease from Providencia rettgeri JN-B, ureABC were efficiently expressed in E. coli BL21(DE3) in an active form (apourease) exhibiting both urease and urethanase (hydrolyze EC) by: 2.
Study of the Expression of Helicobacter Pylori Urei Gene by RT-PCR Article in Journal of Babol University of Medical Sciences 19(6) June with 12 Reads How we measure 'reads'.
Abstract. Helicobacter pylori is a human pathogen that infects the stomach, where it experiences variable pH. To survive the acidic gastric conditions, H. pylori produces large quantities of urease, a nickel enzyme that hydrolyzes urea to ammonia, which neutralizes the local environment.
One of the regulators of urease expression in H. pylori is HpNikR, a nickel-responsive transcription by: 8. Also, H. pylori adherence to gastric epithelial cells in vitro has been shown to induce not only the gene expression of iceA1 that encodes a well-known virulence factor (see below), but also hpyIM that encodes an adenine methyltransferase, indicating how regulation by DNA methylation may be important in H.
pylori. Urease, Urease, Urease subunit beta, Urease subunit alpha (ureA) This subpathway is part of the pathway urea degradation, which is itself part of Nitrogen metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes CO(2) and NH(3) from urea (urease route), the pathway urea degradation and in Nitrogen metabolism. Helicobacter pylori is the major aetiological agent of gastroduodenitis in humans.
Due to the potential importance of catalase in the growth and survival of Helicobacter pylori on the surface of. Analysis of Protein Expression Regulated by the Helicobacter pylori ArsRS Two-Component Signal Transduction System † John T. Loh,1 Shobhana S. Gupta,2 David B.
Friedman,4 Andrzej M. Krezel,3 and Timothy L. Cover1,2,5* Departments of Medicine,1 Microbiology and Immunology,2 and Biological Sciences,3 and Proteomics Laboratory,Cited by: Helicobacter pylori (strain ATCC / ) (Campylobacter pylori) Status.
The novel dodecameric structure of the enzyme may allow it to remain active at the cell surface at acidic gastric pH. Within this dodecameric structure the 12 active sites are clustered within the interior of the proteinaceous shell.
Urease, Urease subunit.Urea enzyme electrodes prepared with urease enzymes obtained from H. pylori and Jack bean based on PVC membrane ammonium-selective electrode showed very good analytical parameters: high sensitivity, dynamic stability over 2 months with less decrease of sensitivity, response time 1–2 by: