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In Silico and In Vitro Elucidation of the Inhibitory Mechanism of Chlorogenic Acid Against <i>Helicobacter pylori</i> Urease. [PDF]
Food Sci NutrWu L +6 more
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Ways to improve the negative impact of proton pump inhibitors on biopsy-based test accuracy for Helicobacter pylori detection. [PDF]
Indian J GastroenterolMalfertheiner P, Schulz C.
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Coordination Chemistry Reviews, 2021
Conventional ureases possess dinuclear nickel active sites that are oxygen-stable and require a set of accessory proteins for metallocenter biosynthesis. By contrast, oxygen-labile ureases have active sites containing dual ferrous ions and lack a requirement for maturation proteins. The structures of the two types of urease are remarkably similar, with
Robert Hausinger +2 more
exaly +3 more sources
Conventional ureases possess dinuclear nickel active sites that are oxygen-stable and require a set of accessory proteins for metallocenter biosynthesis. By contrast, oxygen-labile ureases have active sites containing dual ferrous ions and lack a requirement for maturation proteins. The structures of the two types of urease are remarkably similar, with
Robert Hausinger +2 more
exaly +3 more sources
Urological Research, 1979
Urinary stones form as a consequence of urinary supersaturation. Supersaturation occurs as a result of elevated concentrations of urinary solutes. Dietary, metabolic, endocrine, hereditary, and infectious processes alter urinary solute concentrations. Struvite (MgNH4PO.
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Urinary stones form as a consequence of urinary supersaturation. Supersaturation occurs as a result of elevated concentrations of urinary solutes. Dietary, metabolic, endocrine, hereditary, and infectious processes alter urinary solute concentrations. Struvite (MgNH4PO.
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2013
Urease is a nickel-dependent enzyme that catalyzes the reaction of water with urea. The reaction initially produces ammonia and carbamate, which then spontaneously decomposes to yield another molecule of ammonia and hydrogen carbonate. The structure and function of ureases are described.
S. Benini +2 more
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Urease is a nickel-dependent enzyme that catalyzes the reaction of water with urea. The reaction initially produces ammonia and carbamate, which then spontaneously decomposes to yield another molecule of ammonia and hydrogen carbonate. The structure and function of ureases are described.
S. Benini +2 more
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Metal Ion Interactions with Urease and UreD-Urease Apoproteins
Biochemistry, 1996Klebsiella aerogenes urease in a Ni-containing enzyme (two Ni per alpha beta gamma unit) that is purified as an apoprotein from cells grown in Ni-free medium. Partial activation of urease and UreD-urease apoproteins is achieved in vitro by incubation in the presence of Ni(II) and CO2, whereas incubation of these proteins with Ni alone leads to the ...
I S, Park, R P, Hausinger
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Nature, 1948
IN a previous communication1, we were able to confirm that urease is present in the gastric mucosa and, to some extent, in the duodenal mucosa. It was pointed out that the amount of the ferment present in the whole stomach of an animal is sufficient to release enough ammonia from urea to neutralize large amounts of hydrochloric acid.
O, FitzGERALD, P, MURPHY
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IN a previous communication1, we were able to confirm that urease is present in the gastric mucosa and, to some extent, in the duodenal mucosa. It was pointed out that the amount of the ferment present in the whole stomach of an animal is sufficient to release enough ammonia from urea to neutralize large amounts of hydrochloric acid.
O, FitzGERALD, P, MURPHY
openaire +2 more sources