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Inhibition of Urease by Cyclic β-Triketones and Fluoride Ions

Inhibition of Urease by Cyclic β-Triketones and Fluoride Ions Competitive inhibition of soybean urease by 11 cyclic β-triketones was studied in aqueous solutions at pH 7.4 and 36°C. This process was characterized quantitatively by the inhibition constant (K i), which showed a strong dependence on the structure of the organic chelating agents (nickel atoms in urease) and varied from 58.4 to 847 μM. Under similar conditions, the substrate analogue (hydroxyurea) acted as a weak urease inhibitor (K i = 6.47 mM). At 20°C, competitive inhibition of urease with the ligand of nickel atoms (fluoride anion) was pH-dependent. At pH 3.85–6.45, the value of K i for the process ranged from 36.5 to 4060 μM. Three nontoxic cyclic β-triketones with K i values of 58.4, 71.4, and 88.0 μM (36°C) were the most potent inhibitors of urease. Their efficacy was determined by the presence of three >C=O– groups in the molecule and minimum steric hindrances to binding with metal sites in soybean urease. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Applied Biochemistry and Microbiology Springer Journals

Inhibition of Urease by Cyclic β-Triketones and Fluoride Ions

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References (9)

Publisher
Springer Journals
Copyright
Copyright © 2004 by MAIK “Nauka/Interperiodica”
Subject
Life Sciences; Medical Microbiology; Biochemistry, general; Microbiology
ISSN
0003-6838
eISSN
1608-3024
DOI
10.1023/B:ABIM.0000033908.87711.b5
Publisher site
See Article on Publisher Site

Abstract

Competitive inhibition of soybean urease by 11 cyclic β-triketones was studied in aqueous solutions at pH 7.4 and 36°C. This process was characterized quantitatively by the inhibition constant (K i), which showed a strong dependence on the structure of the organic chelating agents (nickel atoms in urease) and varied from 58.4 to 847 μM. Under similar conditions, the substrate analogue (hydroxyurea) acted as a weak urease inhibitor (K i = 6.47 mM). At 20°C, competitive inhibition of urease with the ligand of nickel atoms (fluoride anion) was pH-dependent. At pH 3.85–6.45, the value of K i for the process ranged from 36.5 to 4060 μM. Three nontoxic cyclic β-triketones with K i values of 58.4, 71.4, and 88.0 μM (36°C) were the most potent inhibitors of urease. Their efficacy was determined by the presence of three >C=O– groups in the molecule and minimum steric hindrances to binding with metal sites in soybean urease.

Journal

Applied Biochemistry and MicrobiologySpringer Journals

Published: Oct 18, 2004

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