Lead Molecules for Targeted Urease Inhibition: An Updated Review from 2010 -2018

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Author(s): Ritu Kataria , Anurag Khatkar*.

Journal Name: Current Protein & Peptide Science

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Abstract:

The field of enzyme inhibition is a tremendous and quickly growing territory of research. Urease, a nickel containing metalloenzyme found in bacteria, algae, fungi, and plants, brings hydrolysis of urea and plays important role in the environmental nitrogen cycle. Apart from this it was found to be responsible for many pathological conditions due to its presence in many microorganisms such as H. pylori, a ureolytic bacteria having urease which elevates pH of gastric medium by hydrolyzing urea present in the alimentary canal and helps the bacteria to colonize and spread infection. Due to the infections caused by the various bacterial ureases found in infectious agents such as Bacillus pasteurii, Brucella abortus, H. pylori, H. mustelae, Klebsiella aerogenes, Klebsiella tuberculosis, Mycobacterium tuberculosis, Pseudomonas putida, Sporosarcina pasteurii and Yersinia enterocolitica, it has been a current topic of today’s research. Details about a wide range of compounds from the exhaustive literature survey has been discussed in this review which is enveloped into two expansive classes, as inhibitors from synthetic origin and inhibitors from natural origin. Moreover, active site details of enzyme, mechanism of catalysis of substrate by enzyme, uses of plant urease and its pathogenic behavior has been included in the current review. So, overall, this review article diagrams the current landscape of the developments in the improvements in the thriving field of urease inhibitory developments in medicinal chemistry from the years 2010 to 2018, with an emphasis on mechanism of action of inhibitors that may be used for more development of recent and strong urease inhibitors and open up new doors to assist examinations in a standout amongst the most lively and promising regions of research.

Keywords: Urea, Urease, Catalytic mechanism, Active site, H.Pylori.

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Article Details

(E-pub Ahead of Print)
DOI: 10.2174/1389203720666190320170215
Price: $95