Abstract
Competitive inhibition of soybean urease by 15 triketone oximes has been studied at 36°C in aqueous solution (pH 4.95). The studied oximes are supposed chelators for the nickel atom in the urease metallocenter. The inhibition constants of urea hydrolysis (K i) varied in the range 2.7-248 μM depending on the oxime structure. Analysis of this dependency demonstrates that the optimal inhibitor is the one containing carbonyl group in position 1 of the cycle, the ethoxyimino group and alkyl residue in the substituent in position 2, as well as the methoxycarbonyl group in position 4 of the cycle.
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Translated from Biokhimiya, Vol. 69, No. 12, 2004, pp. 1649–1658.
Original Russian Text Copyright © 2004 by Tarun, Rubinov, Metelitza.
Originally published in Biochemistry (Moscow) On-Line Papers in Press, as Manuscript BM04-063, August 15, 2004.
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Tarun, E.I., Rubinov, D.B. & Metelitza, D.I. Inhibition of soybean urease by triketone oximes. Biochemistry (Moscow) 69, 1344–1352 (2004). https://doi.org/10.1007/s10541-005-0004-8
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DOI: https://doi.org/10.1007/s10541-005-0004-8