The urease-catalyzed hydrolysis of thiourea and thioacetamide.
Jack bean urease catalyzes the hydrolysis of thiourea with a second-order rate constant (kcat/Km) of 1.6 (+/- 0.2) x 10(-3) M-1 S-1 at pH7, 25 degrees C. This value is lower than that for urea by a factor of 3 x 10(8). The corresponding substitution of S for O in acetamide reduces the kcat/Km value by only a factor of 33. This greater reactivity of the oxo compounds than of the corresponding thiono compounds, and the tighter binding of urea (Ks = 2.9 mM) than of either the guanidinium ion (Ki = 30 mM) or thiourea (Ki = 70 mM), suggests that the substrate chalcogen (S or O) is more likely to be stabilized in the transition state by coordination to the enzyme via a neutral hydrogen-bond donor (i.e., Brønsted acid catalysis) than by coordination via one of the active-site nickel ions (i.e., Lewis acid catalysis).
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Department of Chemistry, Tulane University, New Orleans, Louisiana 70118, USA.
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D007887:Fabaceae / Q000201:enzymology*; D006868:Hydrolysis; D007700:Kinetics; D010946:Plants, Medicinal; D011485:Protein Binding; D013379:Substrate Specificity; D013853:Thioacetamide / Q000378:metabolism*; D013890:Thiourea / Q000378:metabolism*; D014508:Urea / Q000378:metabolism; D014510:Urease / Q000378:metabolism*
D013853:Thioacetamide; D014508:Urea; D014510:Urease; D013890:Thiourea