Urease is the enzyme catalyzing the hydrolysis of urea into carbon dioxide and ammonia. This enzyme is substrate-specific, which means that the enzyme catalyzes the hydrolysis of urea only. This feature is a basic diagnostic criterion used in the determination of many bacteria species. Most of the methods utilized for detection of urease are based on analysis of its enzyme activity – the hydrol...

Urease of Proteus rettgeri is an inducible enzyme synthesized specifically in the presence of urea; urea analogues did not act as inducers. Once initiated, the biosynthesis of the enzyme proceeded as a constant fraction of the total protein formed. The rate of urease formation was affected by the carbon source used. In comparison with glycerol, glucose inhibited enzyme synthesis. The addition o...

The influence of urease activity on N distribution and losses after foliar urea application was investigated using wild-type and transgenic potato (Solanum tuberosum cv Désirée) plants in which urease activity was down-regulated. A good correlation between urease activity and (15)N urea metabolism (NH(3) accumulation) was found. The general accumulation of ammonium in leaves treated with urea i...

The important human pathogen Helicobacter pylori requires the abundant expression and activity of its urease enzyme for colonization of the gastric mucosa. The transcription, expression, and activity of H. pylori urease were previously demonstrated to be induced by nickel supplementation of growth media. Here it is demonstrated that the HP1338 protein, an ortholog of the Escherichia coli nickel...

UNLABELLED Urease in Cryptococcus neoformans plays an important role in fungal dissemination to the brain and causing meningoencephalitis. Although urea is not required for synthesis of apourease encoded by URE1, the available nitrogen source affected the expression of URE1 as well as the level of the enzyme activity. Activation of the apoenzyme requires three accessory proteins, Ure4, Ure6, an...

In this paper, methods of surface modification of different supports, i.e. glass and polymeric beads for enzyme immobilisation are described. The developed method of enzyme immobilisation is based on Schiff’s base formation between the amino groups on the enzyme surface and the aldehyde groups on the chemically modified surface of the supports. The surface of silicon modified by APTS and GOPS w...

Helicobacter pylori survives and grows at low pHs via acid acclimation mechanisms that enable periplasmic pH homeostasis. Important components include a cytoplasmic urease; a pH-gated urea channel, UreI; and periplasmic α-carbonic anhydrase. To allow the rapid adjustment of periplasmic pH, acid acclimation components are recruited to the inner membrane in acid. The ArsRS two-component system, i...

Urease is a metalloenzyme essential for the survival of Helicobacter pylori in acidic gastric environment. Maturation of urease involves carbamylation of Lys219 and insertion of two nickel ions at its active site. This process requires GTP hydrolysis and the formation of a preactivation complex consisting of apo-urease and urease accessory proteins UreF, UreH, and UreG. UreF and UreH form a com...

With black soil (Pachic Udic Argiboroll) of Northeastern China as the test object, an incubation test was conducted to investigate the effects of urease inhibitors, hydroquinone (HQ), phenyl phosphorodiamidate (PPD) and N-(n-Butyl) thiophosphoric triamide (NBPT), on the kinetic characteristics of soil urease under normal moisture and waterlogged conditions, aimed to study the changes of catalyt...

Baicalin (BA) is the principal component of Radix Scutellariae responsible for its pharmacological activity. In this study, kinetics and mechanism of inhibition by BA against jack-bean urease were investigated for its therapeutic potential. It was revealed that the IC₅₀ of BA against jack-bean urease was 2.74 ± 0.51 mM, which was proved to be a competitive and concentration-dependent inhibition...