10 Urease Inhibition Muhammad

The design, synthesis, characterization and exploring the broad spectrum of potency of biologically active molecular building blocks have attracted the attention of scientific community since last couple of decades. The emergence of pathogenic resistance is a natural phenomenon and investigations toward the advances of new structurally diverse inhibitors have always been at the esteem of pharmaceutical research. This growing field has ever become an active area of research for the synthetic, biological and medicinal perspectives, looking at the molecular level. Enzyme inhibition has attracted great attention of biomedical scientist since last couple of decades. A variety of inhibitors have been discovered and used for the control of various diseases. One of the key features of enzyme is its selectivity towards certain inhibitors; the inhibitor can be a simple organic molecule or complex molecular architecture. The specificity of inhibitor depends on the size, shape and the interactive forces which result in the exact matching of inhibitor and the enzyme. These inhibitions block the activity of the enzyme under the physiological conditions. Urea and urease are the landmark molecules in the early days of synthetic organic chemistry. Urea was the first organic molecule synthesized in laboratory and urease was being first crystallized out from jack bean (Amtul et al., 2002; Hagar et al., 1925; Mobley et al., 1989; Amtul et al., 2006; Zonia et al., 1995). The significance of the urease enzyme is critically investigated due to its capacity to serve as a virulence factor of infections in the urinary and gastrointestinal tracts, maintaining equilibrium in the nitrogen cycles of nitrogenous wastes in the rumens of domestic livestock, and its importance in environmental transformations of nitrogenous compounds, including urea based fertilizers. The physiology of microbial ureases depends on their cellular location, regulation, genetic makeup and the relationships between the microbial urease and the well-characterized potent range of inhibitors. The urease (urea amido hydrolase; EC 3.5.1.5) is a nickel containing enzyme which hydrolyzes urea into ammonia and carbamic acid, the later compound produce ammonia and carbon dioxide on further decomposition. The hydrolysis of the urea yields high concentrations of ammonia which accompanying in pH elevation. Urease has been regarded as the important enzyme for the manipulation of urea and other nitrogenous ingredients in the biological, agricultural and environmental fields. Urease occurs in many plants, selected fungi, and a