scholarly journals Inhibition of Jack Bean Urease by 1,4-benzoquinone and 2,5-dimethyl-1,4-benzoquinone. Evaluation of the Inhibition Mechanism

2002 ◽  
Vol 17 (4) ◽  
pp. 247-253 ◽  
Author(s):  
Wiesława Zaborska ◽  
Mirosława Kot ◽  
Kinga Superata
Keyword(s):  
Inhibition Mechanism ◽  
Jack Bean Urease ◽  
Jack Bean

Jack Bean Urease Inhibitors, and Antioxidant Activity Based on Palmitic acid Derived 1-acyl-3- Arylthioureas: Synthesis, Kinetic Mechanism and Molecular Docking Studies

Drug Research ◽  
2017 ◽  
Vol 67 (10) ◽  
pp. 596-605 ◽  
Author(s):  
Aamer Saeed ◽  
Sajid ur-Rehman ◽  
Pervaiz Channar ◽  
Fayaz Larik ◽  
Qamar Abbas ◽  
...  
Keyword(s):  
Binding Affinity ◽  
Docking Study ◽  
Kinetic Mechanism ◽  
Inhibition Mechanism ◽  
Initial Structure ◽  
Urease Inhibitors ◽  
Jack Bean Urease ◽  
Jack Bean ◽  
Ic50 Value ◽  
Urease Enzyme

AbstractA series of acylthioureas was synthesized and their inhibitory effects on the DPPH and jack bean urease were evaluated. The results showed that all of the synthesized compounds exhibited significant jack bean urease inhibitory activities. Especially, 1-(4-chlorophenyl)-3 palmitoylthiourea 5a bearing 4-chloro substituted phenyl ring exhibited the most potent tyrosinase inhibitory activity with an IC50 value 0.0170 μM compared to the IC50 value of 4.720 μM of thiourea used as standard. The inhibition mechanism analyzed by Lineweaver–Burk plots revealed that the type of inhibition of compound 5a on tyrosinase was noncompetitive. The docking study against jack bean urease enzyme was also performed to determine the binding affinity of the compounds. The compounds 4c and 4e showed the highest binding affinity with the active binding site of tyrosinase. The initial structure activity relationships (SARs) analysis suggested that further development of such compounds might be of interest. The statistics of our results endorses that all compounds and particularly 5a may serve as a structural template for the design and development of novel urease inhibitors Graphical Abstract.

scholarly journals Inhibition of jack bean urease by amphiphilic peptides

2021 ◽  
Author(s):  
Zafar Ali Shah ◽  
Sadam Hussain ◽  
Serab Khan ◽  
Nawab Ali ◽  
Samiullah Burki ◽  
...  
Keyword(s):  
Jack Bean Urease ◽  
Jack Bean ◽  
Amphiphilic Peptides

Single-step purification of urease by affinity chromatography

1974 ◽  
Vol 20 (4) ◽  
pp. 623-630 ◽  
Author(s):  
Bassanio L. Wong ◽  
Charles R. Shobe
Keyword(s):  
Enzyme Activity ◽  
Affinity Chromatography ◽  
Single Step ◽  
Jack Bean Urease ◽  
Jack Bean ◽  
Specific Activities ◽  
Single Step Purification

Single-step purification of urease (urea aminohydrolase; EC. 3.5.1.5) from cell-free extracts of Proteus morganii and from partially purified preparations of jack bean urease were achieved in less than 90 min by affinity chromatography on hydroxyurea-substituted beaded agarose columns. The specific activities of the purified enzymes were as high as, or higher than, those reported by other authors for urease preparations obtained by conventional techniques. In addition, yields of enzyme activity were routinely 6 to 100 times greater than recoveries previously reported for this enzyme.

ChemInform Abstract: INHIBITION OF JACK BEAN UREASE (EC 3.5.1.5) BY ACETOHYDROXAMIC ACID AND BY PHOSPHORAMIDATE. AN EQUIVALENT WEIGHT FOR UREASE

1975 ◽  
Vol 6 (39) ◽  
Author(s):  
NICHOLAS E. DIXON ◽  
CARLO GAZZOLA ◽  
JAMES J. WATTERS ◽  
ROBERT L. BLAKELEY ◽  
BURT ZERNER
Keyword(s):  
Acetohydroxamic Acid ◽  
Jack Bean Urease ◽  
Equivalent Weight ◽  
Jack Bean

Jack bean urease inhibition by substituted ureas

1975 ◽  
Vol 5 (3) ◽  
pp. 221-225 ◽  
Author(s):  
S. Cervelli ◽  
P. Nannipieri ◽  
G. Giovannini ◽  
A. Perna
Keyword(s):  
Urease Inhibition ◽  
Jack Bean Urease ◽  
Jack Bean
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