Inhibition of jack bean urease (EC 3.5.1.5) by acetohydroxamic acid and by phosphoramidate. Equivalent weight for urease

1975 ◽  
Vol 97 (14) ◽  
pp. 4130-4131 ◽  
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

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 (EC 3.5.1.5). IV. The molecular size and the mechanism of inhibition by hydroxamic acids. Spectrophotometric titration of enzymes with reversible inhibitors

1980 ◽  
Vol 58 (12) ◽  
pp. 1323-1334 ◽  
Author(s):  
Nicholas E. Dixon ◽  
John A. Hinds ◽  
Ann K. Fihelly ◽  
Carlo Gazzola ◽  
Donald J. Winzor ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Active Site ◽  
Binding Sites ◽  
Spectrophotometric Titration ◽  
Hydroxamic Acids ◽  
Jack Bean Urease ◽  
Equivalent Weight ◽  
Guanidinium Chloride ◽  
Jack Bean ◽  
Equilibrium Ultracentrifugation

Kinetic, spectral, and other studies establish that hydroxamic acids bind reversibly to active-site nickel ion in jack bean urease. Equilibrium ultracentrifugation studies establish that the molecular weight of native urease is 590 000 ± 30 000 while that of the subunit formed in 6 M guanidinium chloride in the presence of β-mercaptoethanol is ~95 000. Essentially the same subunit molecular weight (~93 000) is found by polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate, subsequent to denaturation in a guanidinium chloride – β-mercaptoethanol system at various temperatures. Coupled with an equivalent weight of 96 600 for binding of the inhibitors acetohydroxamic acid and phosphoramidate, these results establish securely that urease is a hexamer with one active site per 96 600-dalton subunit. Consistent values for the equivalent weight are obtained by a routine spectrophotometric titration of the active site of freshly prepared urease with trans-cinnamoylhydroxamic acid. General equations are derived which describe spectrophotometric titrations of binding sites of any enzyme with a reversible inhibitor. These equations allow the evaluation of the difference spectrum of the protein–inhibitor complex even when the binding sites cannot readily be saturated with the inhibitor or vice versa.

In-silico Designing, ADMET Analysis, Synthesis and Biological Evaluation of Novel Derivatives of Diosmin Against Urease Protein and Helicobacter pylori Bacterium

2019 ◽  
Vol 19 (29) ◽  
pp. 2658-2675 ◽  
Author(s):  
Ritu Kataria ◽  
Anurag Khatkar
Keyword(s):  
Molecular Docking ◽  
In Silico ◽  
Acetohydroxamic Acid ◽  
Jack Bean Urease ◽  
Zone Of Inhibition ◽  
Jack Bean ◽  
Urease Inhibitory ◽  
H Pylori ◽  
Derivatives Of

Background: Designing drug candidates against the urease enzyme, which has been found responsible for many pathological disorders in human beings as well as in animals, was done by insilico means. Methods: Studies were carried out on a designed library of diosmin derivatives with the help of Schrodinger’s maestro package of molecular docking software against a crystallographic complex of plant enzyme Jack bean urease (PDB ID: 3LA4). Best twelve derivatives of diosmin were selected for synthesis by considering their interaction energy along with docking score and were further investigated for antioxidant, urease inhibitory and Anti-H. pylori activity by in- vitro method along with ADMET analysis. Results: In-vitro results of series concluded compounds D2a, D2d and D7 (IC50 12.6 ± 0.002, 14.14 ± 0.001 and 15.64 ± 0.012 µM respectively in urease inhibition and 5.195 ± 0.036, 5.39 ± 0.020 and 5.64± 0.005 µM in antioxidant behavior against DPPH) were found to be significantly potent with excellent docking score -11.721, -10.795, -10.188 and binding energy -62.674, -63.352, -56.267 kJ/ mol as compared to standard drugs thiourea and acetohydroxamic acid (-3.459, -3.049 and -21.156 kJ/mol and - 17.454 kJ/mol) whereas compounds D2b, D5b, D5d and D6 were found moderate in urease inhibitory activity. Conclusions: Selected candidates from the outcome of in-vitro urease inhibitory were further examined for anti- H. pylori activity by a well diffusion method against H. pylori bacterium (DSM 4867). Compound D2a showed good anti-H. Pylori activity with a zone of inhibition 10.00 ± 0.00 mm and MIC value 500µg/mL as compared to standard drug acetohydroxamic acid having a zone of inhibition 9.00 ± 0.50mm and MIC 1000µg/mL. In- silico studies played an important role in designing the potent ligands against urease protein as well as in explaining the binding pattern of designed and synthesized ligand within the active pocket of jack bean urease protein. ADMET studies were also carried out to check the drug similarity of designed compounds by the means of quikprop module of molecular docking software. Hence, the present investigation studies will provide a new vision for the discovery of potent agents against H. pylori and urease associated diseases.

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.

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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