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• W2019689199 abstract "Formamide has been found to be a bona fide substrate for jackbean urease (urea amidohydrolase, EC 3.5.1.5) and can be hydrolyzed to completion by the enzyme. The pH maximum for the reaction was 5.2, the Michaelis constant was 0.5 (±0.05) M at pH 5.2 and at pH 6.8, and the maximal velocity was 50-fold lower than that for urea at pH 6.8 its pH maximum, which nevertheless represents the highest V for any of the second-substrates of urease. As a competitive inhibitor of urea at pH 6.8, formamide had a Ki = 0.4 (±0.11) M, indicating that the Michaelis constants for both urea and formamide approximate the true dissociation constants for the respective enzyme-substrate complexes. The ratios of formamide/urea hydrolysis remained constant during purification of the enzyme to maximal specific activity; and formamide hydrolysis was completely inhibited in the presence of 0.8 mM acetohydroxamate, a specific urease inhibitor. Formamide did not produce a progressive inhibition of urease, as had been found to occur with two other substrates possessing the hydroxamate functional group: hydroxyurea and dihydroxyurea. The kinetic constants for urease hydrolysis of formamide compare favorably with those of a representative bacterial aliphatic amidase. Urease did not hydrolyze the closest homologs of formamide: N-methyl formamide and acetamide. fa ]∗|The opinions or assertions contained herein are the private views of the authors and are not to be construed as official or as reflecting the views of the Department of the Army or the Department of Defense." @default.
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• W2019689199 date "1977-10-01" @default.
• W2019689199 modified "2023-09-27" @default.
• W2019689199 title "Formamide: the minimum-structure substrate for urease" @default.
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• W2019689199 doi "https://doi.org/10.1016/0005-2744(77)90099-7" @default.
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