Inhibition of soybean urease by triketone oximes.
Competitive inhibition of soybean urease by 15 triketone oximes has been studied at 36 degrees 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 microM 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.
Tarun
E I
EI
Institute of Bioorganic Chemistry, National Academy of Sciences of Belarus, Minsk 220141, Belarus.
Rubinov
D B
DB
Metelitza
D I
DI
D004791:Enzyme Inhibitors / Q000737:chemistry / Q000494:pharmacology*; D006863:Hydrogen-Ion Concentration; D007659:Ketones / Q000737:chemistry / Q000494:pharmacology*; D007700:Kinetics; D015394:Molecular Structure; D010091:Oximes / Q000737:chemistry / Q000494:pharmacology*; D013025:Glycine max / Q000201:enzymology*; D013379:Substrate Specificity; D014510:Urease / Q000037:antagonists & inhibitors*
D004791:Enzyme Inhibitors; D007659:Ketones; D010091:Oximes; D014510:Urease